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Search results 7701 to 7800 out of 8285 for C2

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Type Details Score
Publication
26655900 | J:314576
First Author: Narayanan R
Year: 2015
Journal: Cell Rep
Title: Loss of BAF (mSWI/SNF) Complexes Causes Global Transcriptional and Chromatin State Changes in Forebrain Development.
Volume: 13
Issue: 9
Pages: 1842-54
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Publication
30352686 | J:270543
First Author: Tanahashi H
Year: 2018
Journal: Biochem Biophys Res Commun
Title: Deletion of Lrp4 increases the incidence of microphthalmia.
Volume: 506
Issue: 3
Pages: 478-484
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Publication
38575788 | J:355679
First Author: Vercellino I
Year: 2024
Journal: Nat Struct Mol Biol
Title: SCAF1 drives the compositional diversity of mammalian respirasomes.
Volume: 31
Issue: 7
Pages: 1061-1071
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Publication
38374152 | J:345473
First Author: Lee JG
Year: 2024
Journal: Nat Commun
Title: PIBF1 regulates trophoblast syncytialization and promotes cardiovascular development.
Volume: 15
Issue: 1
Pages: 1487
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Protein
Q8CI52
Organism: Mus musculus/domesticus
Length: 662  
Fragment?: false
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Protein
Q8K2H6
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: false
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Protein
Q8VEF1
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
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Protein
Q80TI0
Organism: Mus musculus/domesticus
Length: 738  
Fragment?: false
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Protein
Q8C5J8
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
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Protein
A0A0R4J0A0
Organism: Mus musculus/domesticus
Length: 583  
Fragment?: false
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Protein
F7CUV7
Organism: Mus musculus/domesticus
Length: 274  
Fragment?: true
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Protein
A0A1W2P6I7
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: true
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Protein
A0A1L1SQ42
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: false
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Protein
Q3TS15
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: true
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Protein
D3YWR0
Organism: Mus musculus/domesticus
Length: 761  
Fragment?: false
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Protein
F8WJ74
Organism: Mus musculus/domesticus
Length: 688  
Fragment?: false
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Protein
A0A1D5RLT6
Organism: Mus musculus/domesticus
Length: 767  
Fragment?: false
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Protein
C6EQJ2
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: false
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Protein
F7CD65
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: true
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Protein
Q8BVK4
Organism: Mus musculus/domesticus
Length: 228  
Fragment?: false
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Protein
F7AI87
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
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Protein
A0A494BBM2
Organism: Mus musculus/domesticus
Length: 39  
Fragment?: false
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Protein
Q9CW76
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Protein
A2BE97
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Protein
A0A571BEM4
Organism: Mus musculus/domesticus
Length: 311  
Fragment?: false
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Protein
A2BE96
Organism: Mus musculus/domesticus
Length: 238  
Fragment?: true
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Protein
A0A087WP03
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
E9PWM5
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
A0JLM7
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Protein
E9Q4N1
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: false
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Publication
1419362 | -
 
First Author: Rhee SG
Year: 1992
Journal: Adv Second Messenger Phosphoprotein Res
Title: Multiple forms of phospholipase C isozymes and their activation mechanisms.
Volume: 26
Pages: 35-61
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Publication
1849017 | -
First Author: Meldrum E
Year: 1991
Journal: Biochim Biophys Acta
Title: The PtdIns-PLC superfamily and signal transduction.
Volume: 1092
Issue: 1
Pages: 49-71
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Publication
9488668 | -
First Author: Young P
Year: 1998
Journal: J Biol Chem
Title: Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a.
Volume: 273
Issue: 10
Pages: 5461-7
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Publication
12062168 | -
First Author: Buchberger A
Year: 2002
Journal: Trends Cell Biol
Title: From UBA to UBX: new words in the ubiquitin vocabulary.
Volume: 12
Issue: 5
Pages: 216-21
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Publication
11406394 | -
First Author: Hofmann K
Year: 2001
Journal: Trends Biochem Sci
Title: A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems.
Volume: 26
Issue: 6
Pages: 347-50
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Publication
12121618 | -
First Author: Oldham CE
Year: 2002
Journal: Curr Biol
Title: The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination.
Volume: 12
Issue: 13
Pages: 1112-6
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Publication
11919614 | -
First Author: Riezman H
Year: 2002
Journal: Nature
Title: Cell biology: the ubiquitin connection.
Volume: 416
Issue: 6879
Pages: 381-3
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Publication
1919637 | -
First Author: Reece DE
Year: 1991
Journal: J Clin Oncol
Title: Intensive chemotherapy with cyclophosphamide, carmustine, and etoposide followed by autologous bone marrow transplantation for relapsed Hodgkin's disease.
Volume: 9
Issue: 10
Pages: 1871-9
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Publication
15112237 | -
First Author: Staub E
Year: 2004
Journal: Bioessays
Title: Insights into the evolution of the nucleolus by an analysis of its protein domain repertoire.
Volume: 26
Issue: 5
Pages: 567-81
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Protein Domain
IPR022684 | Calpain_cysteine_protease
Type: Family
Description: This group of cysteine peptidases belong to the MEROPS peptidase family C2 (calpain family, clan CA). A type example is calpain, which is an intracellular protease involved in many important cellular functions that are regulated by calcium [, ]. The protein is a complex of 2 polypeptide chains (light and heavy), with eleven known active peptidases in humans and two non-peptidase homologues known as calpamodulin and androglobin []. These include a highly calcium-sensitive (i.e., micro-molar range) form known as mu-calpain, mu-CANP or calpain I; a form sensitive to calcium in the milli-molar range, known as m-calpain, m-CANP or calpainII; and a third form, known as p94, which is found in skeletal muscle only [].All forms have identical light but different heavy chains. Both mu- and m-calpain are heterodimers containing an identical 28kDa subunit and an 80kDa subunit that shares 55-65% sequence homology between the two proteases [, ]. The crystallographic structure of m-calpain reveals six "domains"in the 80kDa subunit [, ]: A 19-amino acid NH2-terminal sequence;Active site domain IIa;Active site domain IIb. Domain 2 showslow levels of sequence similarity to papain; although the catalytic His hasnot been located by biochemical means, it is likely that calpain and papainare related [].Domain III;An 18-amino acid extended sequence linking domain III to domain IV;Domain IV, which resembles the penta EF-hand family of polypeptides, binds calcium and regulates activity []. Ca2+-binding causes a rearrangement of the protein backbone, the net effect of which is that a Trp side chain, which acts as a wedge between catalytic domains IIa and IIb in the apo state, moves away from the active site cleft allowing for the proper formation of the catalytic triad []. Calpain-like mRNAs have been identified in other organisms including bacteria, but the molecules encoded by these mRNAs have not been isolated, so little is known about their properties. How calpain activity is regulated in these organisms cells is still unclear In metazoans, the activity of calpain is controlled by a single proteinase inhibitor, calpastatin (). The calpastatin gene can produce eight or more calpastatin polypeptides ranging from 17 to 85kDa by use of different promoters and alternative splicing events. The physiological significance of these different calpastatins is unclear, although all bind to three different places on the calpain molecule; binding to at least two of the sites is Ca2+ dependent. The calpains ostensibly participate in a variety of cellular processes including remodelling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis. Deregulated calpain activity following loss of Ca2+ homeostasis results in tissue damage in response to events such as myocardial infarcts, stroke, and brain trauma [].
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Protein Domain
IPR036146 | Cyclotide_sf
Type: Homologous_superfamily
Description: Cyclotides (cyclo peptides) are plant peptides of ~30 amino acids with a head to-tail cyclic backbone and six cysteine residues involved in three disulphide bonds. The cyclotides are extremely resistant to proteolysis and are remarkably stable. Cyclotides display a diverse range of biological activities, including uterotonic activity, inhibition of neurotensin binding, hemolytic, anti-HIV and anti-microbial activity. This range of biological activities makes cyclotides amenable to potential pharmaceutical and agricultural applications. Although their precise role in plants has not yet been reported, it appears that they are most likely present as defence molecules [, , , ].The three-dimensional structure of cyclotides is compact and contains a number of β-turns, three β-strands arranged in a distorted triple-stranded β-sheet, a short helical segment, and a network of disulphide bonds which form a cystine knot. The cystine knot consists of an embedded ring in the structure, formed by two disulphide bonds and their connecting backbone segments is threaded by a third disulphide bond. Although the cystine knot motif is now well known in a wide variety of proteins, the cyclotides remain as the only example in which a cystine knot is embedded within a circular protein backbone, a motif that is referred to as the cyclic cystine knot (CCK) [, , , ].Cyclotides can be separated into two sub-families, one of which tends to contain a larger number of positively charged residues and has a bracelet-like circularisation of the backbone. The second subfamily contains a backbone twist due to a cis-Pro peptide bond and may conceptually be regarded as a molecular Moebius strip [, ]. Bracelet and Moebius families of cyclotides possess a Knottin scaffold. The cyclotide family of proteins is abundant in plants from the Rubiaceae and Violaceae families and includes:Kalata B1.Circulins.Cyclopsychotride A.Cycloviolacin O1.Also included in this entry are cliotides from the leguminous plant Clitoria ternatea. These are cyclotides with known medicinal properties that have antimicrobial activities against Escherichia coli and are cytotoxic to HeLa cells [].This entry also includes chassatides. There are 18 chassatides peptides: 14 new cyclotides and 4 uncyclotides from the Rubiaceae family. Uncyclotides are the most potent chassatides for antimicrobial, cytotoxic, and hemolytic activities. All uncyclotides belong to the bracelet subfamily, all lacking the Asn/Asp residue at their C termini, which is crucial for backbone cyclization. Genetic characterization of novel cyclotides revealed that their precursors are highly shortened. They consist of five bracelet, two Möbius, and two hybrid cyclotides. Two Met-oxidized derivatives of chassatide C2 and C11 have been isolated, while we know that oxydation of methionine to methionine sulfoxide (MetO) causes a complete loss of biological activities [].
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Protein Domain
IPR019018 | Rab-bd_FIP-RBD
Type: Domain
Description: The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognise the active form of Rab11. FIPs are diverse in sequence length and composition toward their N-termini, presumably a feature that underpins their specific roles in Rab11-mediated vesicle trafficking. They have been divided into three subfamilies (classe I, II, and III)on the basis of domain architecture. Class I FIPs comprises a subfamily of three proteins (Rip11/pp75/FIP5, Rab-coupling protein (RCP), and FIP2) that possess an N-terminal C2 domain, localize to recycling endosomes, and regulate plasma membrane recycling. The class II subfamily consists of two proteins (FIP3/eferin/arfophilin and FIP4) with tandem EF hands and a proline-rich region. Class II FIPs localize to recycling endosomes, the trans-Golgi network, and have been implicated in the regulation of membrane trafficking during cytokinesis. The class III subfamily consists of a single protein, FIP1, which does not contain obvious homology domains or motifs other than the FIP-RBD [, , , ].The FIP-RBD domain is also found in Rab6-interacting protein Erc1/Elks. Erc1 is the regulatory subunit of the IKK complex and probably recruits IkappaBalpha/NFKBIA to the complex []. It may be involved in the organisation of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. It may also be involved in vesicle trafficking at the CAZ, as well as in Rab-6 regulated endosomes to Golgi transport [].The FIB-RBD domain consists of an N-terminal long α-helix, followed by a 90 degrees bend at a conserved proline residue, a 3(10) helix and a C-terminal short β-strand, adopting an "L"shape. The long α-helix forms a parallel coiled-coil homodimer that symmetrically interacts with two Rab11 molecules on both sides, forming a quaternary Rab11-(FIP)2-Rab11 complex. The Rab11-interacting region of FIP-RBD is confined to the C-terminal 24 amino acids, which cover the C-terminal half of the long α-helix and the short β-strand [, , , ]. This entry represents the FIP-RBD C-terminal domain.
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Protein Domain
IPR033883 | C2_III
Type: Domain
Description: This group of cysteine peptidases belong to the MEROPS peptidase family C2 (calpain family, clan CA). A type example is calpain, which is an intracellular protease involved in many important cellular functions that are regulated by calcium [, ]. The protein is a complex of 2 polypeptide chains (light and heavy), with eleven known active peptidases in humans and two non-peptidase homologues known as calpamodulin and androglobin []. These include a highly calcium-sensitive (i.e., micro-molar range) form known as mu-calpain, mu-CANP or calpain I; a form sensitive to calcium in the milli-molar range, known as m-calpain, m-CANP or calpain II; and a third form, known as p94, which is found in skeletal muscle only [].All forms have identical light but different heavy chains. Both mu- and m-calpain are heterodimers containing an identical 28kDa subunit and an 80kDa subunit that shares 55-65% sequence homology between the two proteases [, ]. The crystallographic structure of m-calpain reveals six "domains"in the 80kDa subunit [, ]: A 19-amino acid NH2-terminal sequence;Active site domain IIa;Active site domain IIb. Domain 2 showslow levels of sequence similarity to papain; although the catalytic His hasnot been located by biochemical means, it is likely that calpain and papainare related [].Domain III;An 18-amino acid extended sequence linking domain III to domain IV;Domain IV, which resembles the penta EF-hand family of polypeptides, binds calcium and regulates activity []. Ca2+-binding causes a rearrangement of the protein backbone, the net effect of which is that a Trp side chain, which acts as a wedge between catalytic domains IIa and IIb in the apo state, moves away from the active site cleft allowing for the proper formation of the catalytic triad []. Calpain-like mRNAs have been identified in other organisms including bacteria, but the molecules encoded by these mRNAs have not been isolated, so little is known about their properties. How calpain activity is regulated in these organisms cells is still unclear In metazoans, the activity of calpain is controlled by a single proteinase inhibitor, calpastatin (). The calpastatin gene can produce eight or more calpastatin polypeptides ranging from 17 to 85kDa by use of different promoters and alternative splicing events. The physiological significance of these different calpastatins is unclear, although all bind to three different places on the calpain molecule; binding to at least two of the sites is Ca2+ dependent. The calpains ostensibly participate in a variety of cellular processes including remodelling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis. Deregulated calpain activity following loss of Ca2+ homeostasis results in tissue damage in response to events such as myocardial infarcts, stroke, and brain trauma []. This entry includes subdomain III of typical and atypical calpains.
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Protein Domain
IPR020863 | MACPF_CS
Type: Conserved_site
Description: The membrane attack complex/perforin (MACPF) domain is conserved in bacteria, fungi, mammals and plants. It was originally identified and named as being common to five complement components (C6, C7, C8-alpha, C8-beta, and C9) and perforin. These molecules perform critical functions in innate and adaptive immunity. The MAC family proteins and perforin are known to participate in lytic pore formation. In response to pathogen infection, a sequential and highly specific interaction between the constituent elements occurs to form transmembrane channels which are known as the membrane-attack complex (MAC).Only a few other MACPF proteins have been characterised and several are thought to form pores for invasion or protection [, , ]. Examples are proteins from malarial parasites [], the cytolytic toxins from sea anemones [], and proteins that provide plant immunity [, ]. Functionally uncharacterised MACPF proteins are also evident in pathogenic bacteria such as Chlamydia spp []and Photorhabdus luminescens (Xenorhabdus luminescens) [].The MACPF domain is commonly found to be associated with other N- and C-terminal domains, such as TSP1 (see ), LDLRA (see ), EGF-like (see ),Sushi/CCP/SCR (see ), FIMAC or C2 (see ). They probably control or target MACPF function [, ]. The MACPF domain oligomerizes, undergoes conformational change, and is required for lytic activity.The MACPF domain consists of a central kinked four-stranded antiparallel beta sheet surrounded by alpha helices and beta strands, forming two structural segments. Overall, the MACPF domain hasa thin L-shaped appearance. MACPF domains exhibit limited sequence similarity but contain a signature [YW]-G-[TS]-H-[FY]-x(6)-G-G motif [, , ].Some proteins known to contain a MACPF domain are listed below:Vertebrate complement proteins C6 to C9. Complement factors C6 to C9 assemble to form a scaffold, the membrane attack complex (MAC), that permits C9 polymerisation into pores that lyse Gram-negative pathogens [, ].Vertebrate perforin. It is delivered by natural killer cells and cytotoxic T lymphocytes and forms oligomeric pores (12 to 18 monomers) in the plasma membrane of either virus-infected or transformed cells.Arabidopsis thaliana (Mouse-ear cress) constitutively activated cell death 1 (CAD1) protein. It is likely to act as a mediator that recognises plant signals for pathogen infection [].Arabidopsis thaliana (Mouse-ear cress) necrotic spotted lesions 1 (NSL1) protein [].Venomous sea anemone Phyllodiscus semoni (Night anemone) toxins PsTX-60A and PsTX-60B [].Venomous sea anemone Actineria villosa (Okinawan sea anemone) toxin AvTX-60A [].Plasmodium sporozoite microneme protein essential for cell traversal 2 (SPECT2). It is essential for the membrane-wounding activity of the sporozoite and is involved in its traversal of the sinusoidal cell layer prior to hepatocyte-infection [].P. luminescens Plu-MACPF. Although nonlytic, it was shown to bind to cell membranes [].Chlamydial putative uncharacterised protein CT153 [].
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Protein Domain
IPR020864 | MACPF
Type: Domain
Description: The membrane attack complex/perforin (MACPF) domain is conserved in bacteria, fungi, mammals and plants. It was originally identified and named as being common to five complement components (C6, C7, C8-alpha, C8-beta, and C9) and perforin. These molecules perform critical functions in innate and adaptive immunity. The MAC family proteins and perforin are known to participate in lytic pore formation. In response to pathogen infection, a sequential and highly specific interaction between the constituent elements occurs to form transmembrane channels which are known as the membrane-attack complex (MAC).Only a few other MACPF proteins have been characterised and several are thought to form pores for invasion or protection [, , ]. Examples are proteins from malarial parasites [], the cytolytic toxins from sea anemones [], and proteins that provide plant immunity [, ]. Functionally uncharacterised MACPF proteins are also evident in pathogenic bacteria such as Chlamydia spp []and Photorhabdus luminescens (Xenorhabdus luminescens) [].The MACPF domain is commonly found to be associated with other N- and C-terminal domains, such as TSP1 (see ), LDLRA (see ), EGF-like (see ),Sushi/CCP/SCR (see ), FIMAC or C2 (see ). They probably control or target MACPF function [, ]. The MACPF domain oligomerizes, undergoes conformational change, and is required for lytic activity.The MACPF domain consists of a central kinked four-stranded antiparallel beta sheet surrounded by alpha helices and beta strands, forming two structural segments. Overall, the MACPF domain has a thin L-shaped appearance. MACPF domainsexhibit limited sequence similarity but contain a signature [YW]-G-[TS]-H-[FY]-x(6)-G-G motif [, , ].Some proteins known to contain a MACPF domain are listed below:Vertebrate complement proteins C6 to C9. Complement factors C6 to C9 assemble to form a scaffold, the membrane attack complex (MAC), that permits C9 polymerisation into pores that lyse Gram-negative pathogens [, ].Vertebrate perforin. It is delivered by natural killer cells and cytotoxic T lymphocytes and forms oligomeric pores (12 to 18 monomers) in the plasma membrane of either virus-infected or transformed cells.Arabidopsis thaliana (Mouse-ear cress) constitutively activated cell death 1 (CAD1) protein. It is likely to act as a mediator that recognises plant signals for pathogen infection [].Arabidopsis thaliana (Mouse-ear cress) necrotic spotted lesions 1 (NSL1) protein [].Venomous sea anemone Phyllodiscus semoni (Night anemone) toxins PsTX-60A and PsTX-60B [].Venomous sea anemone Actineria villosa (Okinawan sea anemone) toxin AvTX-60A [].Plasmodium sporozoite microneme protein essential for cell traversal 2 (SPECT2). It is essential for the membrane-wounding activity of the sporozoite and is involved in its traversal of the sinusoidal cell layer prior to hepatocyte-infection [].P. luminescens Plu-MACPF. Although nonlytic, it was shown to bind to cell membranes [].Chlamydial putative uncharacterised protein CT153 [].
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Protein Domain
IPR005535 | Cyclotide
Type: Family
Description: Cyclotides (cyclo peptides) are plant peptides of ~30 amino acids with a head to-tail cyclic backbone and six cysteine residues involved in three disulphide bonds. The cyclotides are extremely resistant to proteolysis and are remarkably stable. Cyclotides display a diverse range of biological activities, including uterotonic activity, inhibition of neurotensin binding, hemolytic, anti-HIV and anti-microbial activity. This range of biological activities makes cyclotides amenable to potential pharmaceutical and agricultural applications. Although their precise role in plants has not yet been reported, it appears that they are most likely present as defence molecules [, , , ].The three-dimensional structure of cyclotides is compact and contains a number of β-turns, three β-strands arranged in a distorted triple-stranded β-sheet, a short helical segment, and a network of disulphide bonds which form a cystine knot. The cystine knot consists of an embedded ring in the structure, formed by two disulphide bonds and their connecting backbone segments is threaded by a third disulphide bond. Although the cystine knot motif is now well known in a wide variety of proteins, the cyclotides remain as the only example in which a cystine knot is embedded within a circular protein backbone, a motif that is referred to as the cyclic cystine knot (CCK) [, , , ].Cyclotides can be separated into two sub-families, one of which tends to contain a larger number of positively charged residues and has a bracelet-like circularisation of the backbone. The second subfamily contains a backbone twist due to a cis-Pro peptide bond and may conceptually be regarded as a molecular Moebius strip [, ]. Bracelet and Moebius families of cyclotides possess a Knottin scaffold. The cyclotide family of proteins is abundant in plants from the Rubiaceae and Violaceae families and includes:Kalata B1.Circulins.Cyclopsychotride A.Cycloviolacin O1.Also included in this entry are cliotides from the leguminous plant Clitoria ternatea. These are cyclotides with known medicinal properties that have antimicrobial activities against Escherichia coli and are cytotoxic to HeLa cells [].This entry also includes chassatides. There are 18 chassatides peptides: 14 new cyclotides and 4 uncyclotides from the Rubiaceae family. Uncyclotides are the most potent chassatides for antimicrobial, cytotoxic, and hemolytic activities. All uncyclotides belong to the bracelet subfamily, all lacking the Asn/Asp residue at their C termini, which is crucial for backbone cyclization. Genetic characterization of novel cyclotides revealed that their precursors are highly shortened. They consist of five bracelet, two Möbius, and two hybrid cyclotides. Two Met-oxidized derivatives of chassatide C2 and C11 have been isolated, while we know that oxydation of methionine to methionine sulfoxide (MetO) causes a complete loss of biological activities [].
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Protein Domain
IPR037245 | FIP-RBD_C_sf
Type: Homologous_superfamily
Description: The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognise the active form of Rab11. FIPs are diverse in sequence length and composition toward their N-termini, presumably a feature that underpins their specific roles in Rab11-mediated vesicle trafficking. They have been divided into three subfamilies (classe I, II, and III)on the basis of domain architecture. Class I FIPs comprises a subfamily of three proteins (Rip11/pp75/FIP5, Rab-coupling protein (RCP), and FIP2) that possess an N-terminal C2 domain, localize to recycling endosomes, and regulate plasma membrane recycling. The class II subfamily consists of two proteins (FIP3/eferin/arfophilin and FIP4) with tandem EF hands and a proline-rich region. Class II FIPs localize to recycling endosomes, the trans-Golgi network, and have been implicated in the regulation of membrane trafficking during cytokinesis. The class III subfamily consists of a single protein, FIP1, which does not contain obvious homology domains or motifs other than the FIP-RBD [, , , ].The FIP-RBD domain is also found in Rab6-interacting protein Erc1/Elks. Erc1 is the regulatory subunit of the IKK complex and probably recruits IkappaBalpha/NFKBIA to the complex []. It may be involved in the organisation of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. It may also be involved in vesicle trafficking at the CAZ, as well as in Rab-6 regulated endosomes to Golgi transport [].The FIB-RBD domain consists of an N-terminal long α-helix, followed by a 90 degrees bend at a conserved proline residue, a 3(10) helix and a C-terminal short β-strand, adopting an "L"shape. The long α-helix forms a parallel coiled-coil homodimer that symmetrically interacts with two Rab11 molecules on both sides, forming a quaternary Rab11-(FIP)2-Rab11 complex. The Rab11-interacting region of FIP-RBD is confined to the C-terminal 24 amino acids, which cover the C-terminal half of the long α-helix and the short β-strand [, , , ]. This entry represents the FIP-RBD C-terminal domain.
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Protein Domain
IPR003903 | UIM_dom
Type: Conserved_site
Description: The Ubiquitin Interacting Motif (UIM), or 'LALAL-motif', is a stretch of about 20 amino acid residues, which was first described in the 26S proteasome subunit PSD4/RPN-10 that is known to recognise ubiquitin [, ]. In addition, the UIM is found, often in tandem or triplet arrays, in a variety of proteins either involved in ubiquitination and ubiquitin metabolism, or known to interact with ubiquitin-like modifiers. Among the UIM proteins are two different subgroups of the UBP (ubiquitin carboxy-terminal hydrolase) family of deubiquitinating enzymes, one F-box protein, one family of HECT-containing ubiquitin-ligases (E3s) from plants, and several proteins containing ubiquitin-associated UBA and/or UBX domains []. In most of these proteins, the UIM occurs in multiple copies and in association with other domains such as UBA (), UBX (), ENTH, EH (), VHS (), SH3 (), HECT (), VWFA (), EF-hand calcium-binding, WD-40 (), F-box (), LIM (), protein kinase (), ankyrin (), PX (), phosphatidylinositol 3- and 4-kinase (), C2 (), OTU (), dnaJ (), RING-finger () or FYVE-finger (). UIMs have been shown to bind ubiquitin and to serve as a specific targeting signal important for monoubiquitination. Thus, UIMs may have several functions in ubiquitin metabolism each of which may require different numbers of UIMs [, , ]. The UIM is unlikely to form an independent folding domain. Instead, based on the spacing of the conserved residues, the motif probably forms a short α-helix that can be embedded into different protein folds []. Some proteins known to contain an UIM are listed below: Eukaryotic PSD4/RPN-10/S5, a multi-ubiquitin binding subunit of the 26S proteasome. Vertebrate Machado-Joseph disease protein 1 (Ataxin-3), which acts as a histone-binding protein that regulates transcription; defects in Ataxin-3 cause the neurodegenerative disorder Machado-Joseph disease (MJD).Vertebrate epsin and epsin2. Vertebrate hepatocyte growth factor-regulated tyrosine kinase substrate (HRS). Mammalian epidermal growth factor receptor substrate 15 (EPS15), which is involved in cell growth regulation. Mammalian epidermal growth factor receptor substrate EPS15R. Drosophila melanogaster (Fruit fly) liquid facets (lqf), an epsin. Yeast VPS27 vacuolar sorting protein, which is required for membrane traffic to the vacuole.
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Publication
33589589 | J:304624
First Author: Wu H
Year: 2021
Journal: Nat Commun
Title: Distinct subtypes of proprioceptive dorsal root ganglion neurons regulate adaptive proprioception in mice.
Volume: 12
Issue: 1
Pages: 1026
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Publication
11929610 | J:77736
First Author: Monier S
Year: 2002
Journal: Traffic
Title: Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport.
Volume: 3
Issue: 4
Pages: 289-97
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Protein
Q99MI1
Organism: Mus musculus/domesticus
Length: 1120  
Fragment?: false
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Protein
Q8CHD8
Organism: Mus musculus/domesticus
Length: 1047  
Fragment?: false
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Protein
Q8BQP8
Organism: Mus musculus/domesticus
Length: 635  
Fragment?: false
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Protein
P62897
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Protein
P00015
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Protein
Q8BMS2
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
E0CY47
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
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Protein
Q9DAC8
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: false
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Protein
Q6KAS6
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: true
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Protein
Q920R9
Organism: Mus musculus/domesticus
Length: 35  
Fragment?: true
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Protein
Q8BIJ1
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: false
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Protein
Q920R8
Organism: Mus musculus/domesticus
Length: 44  
Fragment?: true
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Protein
Q6PBG3
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Protein
G4XXT0
Organism: Mus musculus/domesticus
Length: 56  
Fragment?: true
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Protein
Q8VD28
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
V9GXP8
Organism: Mus musculus/domesticus
Length: 1116  
Fragment?: false
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Protein
V9GXF0
Organism: Mus musculus/domesticus
Length: 1088  
Fragment?: false
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Protein
A0A0R4J075
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
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Protein
D3Z049
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein
B9EKA5
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
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Protein
Q5DTH0
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: true
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Protein
F8VPM7
Organism: Mus musculus/domesticus
Length: 1120  
Fragment?: false
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Protein
Q56A15
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
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Publication
22467870 | -
First Author: Nguyen GK
Year: 2012
Journal: J Biol Chem
Title: Novel cyclotides and uncyclotides with highly shortened precursors from Chassalia chartacea and effects of methionine oxidation on bioactivities.
Volume: 287
Issue: 21
Pages: 17598-607
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Publication
16905101 | -
First Author: Jagoe WN
Year: 2006
Journal: Structure
Title: Crystal structure of rab11 in complex with rab11 family interacting protein 2.
Volume: 14
Issue: 8
Pages: 1273-83
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Publication
17007872 | -
First Author: Eathiraj S
Year: 2006
Journal: J Mol Biol
Title: Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes.
Volume: 364
Issue: 2
Pages: 121-35
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Publication
17030804 | -
First Author: Shiba T
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.
Volume: 103
Issue: 42
Pages: 15416-21
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Publication
19119858 | -
First Author: Wei J
Year: 2009
Journal: Biochemistry
Title: Disorder and structure in the Rab11 binding domain of Rab11 family interacting protein 2.
Volume: 48
Issue: 3
Pages: 549-57
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Publication
15218148 | -
First Author: Ducut Sigala JL
Year: 2004
Journal: Science
Title: Activation of transcription factor NF-kappaB requires ELKS, an IkappaB kinase regulatory subunit.
Volume: 304
Issue: 5679
Pages: 1963-7
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Publication
17872444 | -
First Author: Hadders MA
Year: 2007
Journal: Science
Title: Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense.
Volume: 317
Issue: 5844
Pages: 1552-4
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Publication
16900325 | -
First Author: Noutoshi Y
Year: 2006
Journal: Plant Mol Biol
Title: Loss of Necrotic Spotted Lesions 1 associates with cell death and defense responses in Arabidopsis thaliana.
Volume: 62
Issue: 1-2
Pages: 29-42
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Publication
18440555 | -
First Author: Slade DJ
Year: 2008
Journal: J Mol Biol
Title: Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit.
Volume: 379
Issue: 2
Pages: 331-42
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Publication
15659064 | -
First Author: Ishino T
Year: 2005
Journal: Cell Microbiol
Title: A Plasmodium sporozoite protein with a membrane attack complex domain is required for breaching the liver sinusoidal cell layer prior to hepatocyte infection.
Volume: 7
Issue: 2
Pages: 199-208
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Publication
17368498 | -
First Author: Satoh H
Year: 2007
Journal: Toxicon
Title: Characterization of PsTX-60B, a new membrane-attack complex/perforin (MACPF) family toxin, from the venomous sea anemone Phyllodiscus semoni.
Volume: 49
Issue: 8
Pages: 1208-10
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Publication
15799997 | -
First Author: Morita-Yamamuro C
Year: 2005
Journal: Plant Cell Physiol
Title: The Arabidopsis gene CAD1 controls programmed cell death in the plant immune system and encodes a protein containing a MACPF domain.
Volume: 46
Issue: 6
Pages: 902-12
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Publication
10608922 | -
First Author: Ponting CP
Year: 1999
Journal: Curr Biol
Title: Chlamydial homologues of the MACPF (MAC/perforin) domain.
Volume: 9
Issue: 24
Pages: R911-3
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Publication
26720279 | J:310568
First Author: Parikh BA
Year: 2015
Journal: PLoS Pathog
Title: Dual Requirement of Cytokine and Activation Receptor Triggering for Cytotoxic Control of Murine Cytomegalovirus by NK Cells.
Volume: 11
Issue: 12
Pages: e1005323
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Strain
MGI:2159739 | SJL/J
Attribute String: inbred strain
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Publication
32632165 | J:294172
First Author: Kawabe T
Year: 2020
Journal: Nat Commun
Title: Requirements for the differentiation of innate T-bethigh memory-phenotype CD4+ T lymphocytes under steady state.
Volume: 11
Issue: 1
Pages: 3366
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Publication
29084838 | J:256756
First Author: Fernandez-Ruiz D
Year: 2017
Journal: J Immunol
Title: Development of a Novel CD4+ TCR Transgenic Line That Reveals a Dominant Role for CD8+ Dendritic Cells and CD40 Signaling in the Generation of Helper and CTL Responses to Blood-Stage Malaria.
Volume: 199
Issue: 12
Pages: 4165-4179
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Publication
33022229 | J:306893
First Author: Bilate AM
Year: 2020
Journal: Immunity
Title: T Cell Receptor Is Required for Differentiation, but Not Maintenance, of Intestinal CD4+ Intraepithelial Lymphocytes.
Volume: 53
Issue: 5
Pages: 1001-1014.e20
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Publication
32025032 | J:292580
First Author: Tan SH
Year: 2020
Journal: Nature
Title: AQP5 enriches for stem cells and cancer origins in the distal stomach.
Volume: 578
Issue: 7795
Pages: 437-443
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Publication
33358867 | J:303932
First Author: Ishikawa K
Year: 2021
Journal: Biochim Biophys Acta Gen Subj
Title: Attempts to understand the mechanisms of mitochondrial diseases: The reverse genetics of mouse models for mitochondrial disease.
Volume: 1865
Issue: 3
Pages: 129835
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Publication
31092921 | J:283354
First Author: Guiu J
Year: 2019
Journal: Nature
Title: Tracing the origin of adult intestinal stem cells.
Volume: 570
Issue: 7759
Pages: 107-111
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Publication
27576369 | J:241907
 
First Author: Gamrekelashvili J
Year: 2016
Journal: Nat Commun
Title: Regulation of monocyte cell fate by blood vessels mediated by Notch signalling.
Volume: 7
Pages: 12597
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Publication
26585400 | J:227252
First Author: Hayakawa Y
Year: 2015
Journal: Cancer Cell
Title: Mist1 Expressing Gastric Stem Cells Maintain the Normal and Neoplastic Gastric Epithelium and Are Supported by a Perivascular Stem Cell Niche.
Volume: 28
Issue: 6
Pages: 800-814
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Publication
31913277 | J:345107
First Author: Middelhoff M
Year: 2020
Journal: Nat Commun
Title: Prox1-positive cells monitor and sustain the murine intestinal epithelial cholinergic niche.
Volume: 11
Issue: 1
Pages: 111
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Publication
29340033 | J:256521
First Author: Sakitani K
Year: 2017
Journal: Oncotarget
Title: CXCR4-expressing Mist1+ progenitors in the gastric antrum contribute to gastric cancer development.
Volume: 8
Issue: 67
Pages: 111012-111025
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Publication
34758021 | J:320966
First Author: Udagawa T
Year: 2021
Journal: PLoS Biol
Title: Lineage-tracing and translatomic analysis of damage-inducible mitotic cochlear progenitors identifies candidate genes regulating regeneration.
Volume: 19
Issue: 11
Pages: e3001445
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Publication
29897330 | J:277457
   
First Author: McKinley KL
Year: 2018
Journal: Elife
Title: Cellular aspect ratio and cell division mechanics underlie the patterning of cell progeny in diverse mammalian epithelia.
Volume: 7
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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