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Search results 801 to 900 out of 961 for C9

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Type Details Score
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
19419965 | -
First Author: Phelan MM
Year: 2009
Journal: J Biol Chem
Title: Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangement.
Volume: 284
Issue: 29
Pages: 19637-49
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Publication
17692377 | -
First Author: Lovelace LL
Year: 2008
Journal: Mol Immunol
Title: Crystal structure of complement protein C8gamma in complex with a peptide containing the C8gamma binding site on C8alpha: implications for C8gamma ligand binding.
Volume: 45
Issue: 3
Pages: 750-6
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Protein Domain
IPR020067 | Frizzled_dom
Type: Domain
Description: The frizzled (fz) domain is an extracellular domain of about 120 amino acids.It was first identified in the alpha-1 chain of type XVIII collagen and in members of the Frizzled family of seven transmembrane (7TM) proteins which act as receptors for secreted Wingless (Wg)/Wnt glycoproteins []. In addition to these proteins, one or two copies of the fz domain are also found [, , , , ]in:The Frzb family; secreted frizzled-like proteins.Smoothened; another 7TM receptor involved in hedgehog signaling.Carboxpeptidase Z (CPZ).Transmembrane serine protease corin (atrial natriuretic peptide-converting enzyme).Two receptor tyrosine kinases (RTKs) subfamilies, the Ror family and the muscle-specific kinase (MuSK) family.As the fz domain contains 10 cysteines which are largely conserved, it has also been called cysteine-rich domain (CRD) []. The fz domain also contains several other highly conserved residues, for example, a basic amino acid follows C6, and a conserved proline residues lies four residues C-terminal to C9 []. The crystal structure of a fz domain shows that it is predominantly α-helical with all cysteines forming disulphide bonds. In addition to helical regions, two short β-strands at the N terminus form a minimal β-sheet with the second beta sheet passing through a knot created by disulphide bonds [].Several fz domains have been shown to be both necessary and sufficient for Wg/Wnt ligand binding, strongly suggesting that the fz domain is a Wg/Wnt interacting domain [, ].
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Protein Domain
IPR036790 | Frizzled_dom_sf
Type: Homologous_superfamily
Description: This entry represents the frizzled domain superfamily.The frizzled (fz) domain is an extracellular domain of about 120 amino acids.It was first identified in the alpha-1 chain of type XVIII collagen and in members of the Frizzled family of seven transmembrane (7TM) proteins which act as receptors for secreted Wingless (Wg)/Wnt glycoproteins []. In addition to these proteins, one or two copies of the fz domain are also found [, , , , ]in:The Frzb family; secreted frizzled-like proteins.Smoothened; another 7TM receptor involved in hedgehog signaling.Carboxpeptidase Z (CPZ).Transmembrane serine protease corin (atrial natriuretic peptide-converting enzyme).Two receptor tyrosine kinases (RTKs) subfamilies, the Ror family and the muscle-specific kinase (MuSK) family.As the fz domain contains 10 cysteines which are largely conserved, it has also been called cysteine-rich domain (CRD) []. The fz domain also contains several other highly conserved residues, for example, a basic amino acid follows C6, and a conserved proline residues lies four residues C-terminal to C9 []. The crystal structure of a fz domain shows that it is predominantly α-helical with all cysteines forming disulphide bonds. In addition to helical regions, two short β-strands at the N terminus form a minimal β-sheet with the second beta sheet passing through a knot created by disulphide bonds [].Several fz domains have been shown to be both necessary and sufficient for Wg/Wnt ligand binding, strongly suggesting that the fz domain is a Wg/Wnt interacting domain [, ].
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Publication
18662545 | J:139297
First Author: Dasen JS
Year: 2008
Journal: Cell
Title: Hox repertoires for motor neuron diversity and connectivity gated by a single accessory factor, FoxP1.
Volume: 134
Issue: 2
Pages: 304-16
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Publication
28009287 | J:239303
First Author: Amin S
Year: 2016
Journal: Cell Rep
Title: Cdx and T Brachyury Co-activate Growth Signaling in the Embryonic Axial Progenitor Niche.
Volume: 17
Issue: 12
Pages: 3165-3177
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Publication
34994686 | J:317827
   
First Author: Sawai A
Year: 2022
Journal: Elife
Title: PRC1 sustains the integrity of neural fate in the absence of PRC2 function.
Volume: 11
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Publication
20826310 | J:166088
First Author: Jung H
Year: 2010
Journal: Neuron
Title: Global control of motor neuron topography mediated by the repressive actions of a single hox gene.
Volume: 67
Issue: 5
Pages: 781-96
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Publication
21943603 | J:178550
First Author: Sabharwal P
Year: 2011
Journal: Neuron
Title: GDE2 regulates subtype-specific motor neuron generation through inhibition of Notch signaling.
Volume: 71
Issue: 6
Pages: 1058-70
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Publication
30959515 | J:283357
First Author: Nowotschin S
Year: 2019
Journal: Nature
Title: The emergent landscape of the mouse gut endoderm at single-cell resolution.
Volume: 569
Issue: 7756
Pages: 361-367
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Publication
28188179 | J:247259
First Author: Naruse C
Year: 2017
Journal: FASEB J
Title: New insights into the role of Jmjd3 and Utx in axial skeletal formation in mice.
Volume: 31
Issue: 6
Pages: 2252-2266
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Publication
22421546 | J:185743
First Author: Cotney J
Year: 2012
Journal: Genome Res
Title: Chromatin state signatures associated with tissue-specific gene expression and enhancer activity in the embryonic limb.
Volume: 22
Issue: 6
Pages: 1069-80
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Publication
28606110 | J:243875
First Author: Esanov R
Year: 2017
Journal: Mol Neurodegener
Title: A C9ORF72 BAC mouse model recapitulates key epigenetic perturbations of ALS/FTD.
Volume: 12
Issue: 1
Pages: 46
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Protein
Q6DFY8
Organism: Mus musculus/domesticus
Length: 783  
Fragment?: false
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Protein
Q920P3
Organism: Mus musculus/domesticus
Length: 760  
Fragment?: false
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Publication
7876242 | J:23590
First Author: Rehn M
Year: 1995
Journal: J Biol Chem
Title: Identification of three N-terminal ends of type XVIII collagen chains and tissue-specific differences in the expression of the corresponding transcripts. The longest form contains a novel motif homologous to rat and Drosophila frizzled proteins.
Volume: 270
Issue: 9
Pages: 4705-11
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Protein
A1L314
Organism: Mus musculus/domesticus
Length: 713  
Fragment?: false
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Protein
Q5RKV8
Organism: Mus musculus/domesticus
Length: 702  
Fragment?: false
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Protein
B1AQT5
Organism: Mus musculus/domesticus
Length: 250  
Fragment?: true
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Protein
A0A0A6YWU9
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: false
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Protein
D3YYF7
Organism: Mus musculus/domesticus
Length: 102  
Fragment?: true
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Protein
E9QN37
Organism: Mus musculus/domesticus
Length: 720  
Fragment?: false
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Protein
Q9JI82
Organism: Mus musculus/domesticus
Length: 752  
Fragment?: false
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Protein
A0A0U1RPV4
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
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Publication
8717036 | -
First Author: Bhanot P
Year: 1996
Journal: Nature
Title: A new member of the frizzled family from Drosophila functions as a Wingless receptor.
Volume: 382
Issue: 6588
Pages: 225-30
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Publication
9637908 | -
First Author: Xu YK
Year: 1998
Journal: Curr Biol
Title: The Frizzled CRD domain is conserved in diverse proteins including several receptor tyrosine kinases.
Volume: 8
Issue: 12
Pages: R405-6
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Publication
9852758 | -
First Author: Rehn M
Year: 1998
Journal: Trends Biochem Sci
Title: The frizzled motif: in how many different protein families does it occur?
Volume: 23
Issue: 11
Pages: 415-7
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Publication
9637909 | -
First Author: Masiakowski P
Year: 1998
Journal: Curr Biol
Title: The Wnt receptor CRD domain is also found in MuSK and related orphan receptor tyrosine kinases.
Volume: 8
Issue: 12
Pages: R407
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Publication
10082384 | -
First Author: Saldanha J
Year: 1998
Journal: Protein Sci
Title: Identification of a Frizzled-like cysteine rich domain in the extracellular region of developmental receptor tyrosine kinases.
Volume: 7
Issue: 8
Pages: 1632-5
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Publication
10329693 | J:55021
First Author: Yan W
Year: 1999
Journal: J Biol Chem
Title: Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart.
Volume: 274
Issue: 21
Pages: 14926-35
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Publication
9326585 | -
First Author: Lin K
Year: 1997
Journal: Proc Natl Acad Sci U S A
Title: The cysteine-rich frizzled domain of Frzb-1 is required and sufficient for modulation of Wnt signaling.
Volume: 94
Issue: 21
Pages: 11196-200
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Publication
17717151 | -
First Author: Rosado CJ
Year: 2007
Journal: Science
Title: A common fold mediates vertebrate defense and bacterial attack.
Volume: 317
Issue: 5844
Pages: 1548-51
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Protein Domain
IPR044936 | Alphavirus_nsp2pro_sf
Type: Homologous_superfamily
Description: The superfamily of alphaviruses includes 26 known members. They infect a variety of hosts including mosquitoes, birds, rodents and other mammals with worldwide distribution. Alphaviruses also pose a potential threat to human health in many areas. For example, Venezuelan Equine Encephalitis Virus (VEEV) causes encephalitis in humans as well as livestock in Central and South America, and some variants of Sinbis Virus (SIN) and Semliki Forest Virus (SFV) have been found to cause fever and arthritis in humans [].Alphaviruses possess a single-stranded RNA genome of approximately 12 kb. The genomic RNA of alphaviruses is translated into two polyproteins that, respectively, encode structural proteins and nonstructural proteins. The nonstructural proteins may be translated as one or two polyproteins, nsp123 or nsp1234, depending on the virus. These polyproteins are cleaved to generate nsp1, nsp2, nsp3 and nsp4 by a protease activity that resides within nsp2. The nsp2 protein of alphaviruses has multiple enzymatic activities. Its N-terminal domain has been shown to possess ATPase and GTPase activity, RNA helicase activity and RNA 5'-triphosphatase activity. The C-terminal nsp2pro domain of nsp2 is responsible for the regulation of 26S subgenome RNA synthesis, switching between negative- and positive-strand RNA synthesis, targeting nsp2 for nuclear transport and proteolytic processing of the nonstructural polyprotein [, ]. The nsp2pro domain is a member of peptidase family C9 of clan CA.The nsp2pro domain consists of two distinct subdomains. The nsp2pro N-terminal subdomain is largely α-helical and contains the catalytic dyad cysteine and histidine residues organised in a protein fold that differs significantly from any known cysteine protease or protein folds.The nsp2pro C-terminal subdomain displays structural similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases and provides essential elements that contribute to substrate recognition and may also regulate the structure of the substrate binding cleft [].This domain covers the entire nsp2pro domain.
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Publication
27568519 | J:253351
First Author: Hanley O
Year: 2016
Journal: Neuron
Title: Parallel Pbx-Dependent Pathways Govern the Coalescence and Fate of Motor Columns.
Volume: 91
Issue: 5
Pages: 1005-1020
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Publication
28570265 | J:356509
 
First Author: Mo Q
Year: 2017
Journal: JCI Insight
Title: Identification and characterization of a supraclavicular brown adipose tissue in mice.
Volume: 2
Issue: 11
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Protein
P10820
Organism: Mus musculus/domesticus
Length: 554  
Fragment?: false
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Protein
A2RSY7
Organism: Mus musculus/domesticus
Length: 554  
Fragment?: false
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Protein
Q499E0
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Publication
21529712 | J:173414
First Author: Kondrashov N
Year: 2011
Journal: Cell
Title: Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning.
Volume: 145
Issue: 3
Pages: 383-397
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Protein
A0A0G2JF07
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: true
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Protein
Q3TUV1
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: true
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Protein
A0A172Q396
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: true
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Publication
16962975 | -
First Author: Russo AT
Year: 2006
Journal: Structure
Title: The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease.
Volume: 14
Issue: 9
Pages: 1449-58
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Publication
19013248 | -
First Author: Zhang D
Year: 2009
Journal: Protein Expr Purif
Title: Molecular cloning, overproduction, purification and biochemical characterization of the p39 nsp2 protease domains encoded by three alphaviruses.
Volume: 64
Issue: 1
Pages: 89-97
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Publication
16971476 | J:119560
First Author: Choi MY
Year: 2006
Journal: Development
Title: A dynamic expression survey identifies transcription factors relevant in mouse digestive tract development.
Volume: 133
Issue: 20
Pages: 4119-29
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Protein
P39061
Organism: Mus musculus/domesticus
Length: 1774  
Fragment?: false
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Protein
Q61137
Organism: Mus musculus/domesticus
Length: 1302  
Fragment?: false
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Protein
Q80Z10
Organism: Mus musculus/domesticus
Length: 1352  
Fragment?: false
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Protein
Q61086
Organism: Mus musculus/domesticus
Length: 666  
Fragment?: false
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Protein
Q9JIP6
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
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Protein
Q8BKG4
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
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Protein
O70421
Organism: Mus musculus/domesticus
Length: 642  
Fragment?: false
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Protein
Q61088
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q9EQD0
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
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Protein
Q61089
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q61090
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
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Protein
Q61091
Organism: Mus musculus/domesticus
Length: 685  
Fragment?: false
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Protein
Q9R216
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: false
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Protein
Q8R4V4
Organism: Mus musculus/domesticus
Length: 654  
Fragment?: false
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Protein
P56726
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
Q9Z1N6
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
P97401
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Protein
Q8C4U3
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: false
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Protein
Q9WU66
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: false
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Protein
P97299
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
Q3V1B2
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q4VBD5
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
Q8CAH7
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Protein
Q6P551
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
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Protein
Q149J3
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
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Protein
Q3UUM9
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
Q9QY74
Organism: Mus musculus/domesticus
Length: 891  
Fragment?: false
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Protein
Q3UI35
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
A0A0R4J001
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: false
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Protein
Q542J1
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q149L3
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
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Protein
Q80VD0
Organism: Mus musculus/domesticus
Length: 439  
Fragment?: false
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Protein
Q71S95
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: false
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Protein
E9QPX1
Organism: Mus musculus/domesticus
Length: 1774  
Fragment?: false
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Protein
Q8BKS3
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q3UYZ0
Organism: Mus musculus/domesticus
Length: 357  
Fragment?: true
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Protein
Q810L8
Organism: Mus musculus/domesticus
Length: 750  
Fragment?: true
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Protein
Q8R382
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q3UHD7
Organism: Mus musculus/domesticus
Length: 1294  
Fragment?: false
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Protein
A0A0A6YWE6
Organism: Mus musculus/domesticus
Length: 1172  
Fragment?: false
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Protein
Q8BLL2
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: false
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Protein
Q8BRX1
Organism: Mus musculus/domesticus
Length: 891  
Fragment?: false
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Protein
A0A2I3BR53
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: false
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Protein
A0A2I3BQF8
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
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Protein Domain
IPR002620 | Alphavirus_nsp2pro
Type: Domain
Description: The family of alphaviruses includes 26 known members. They infect a variety of hosts including mosquitoes, birds, rodents and other mammals with worldwidedistribution. Alphaviruses also pose a potential threat to human health inmany area. For example, Venezuelan Equine Encephalitis Virus (VEEV) causesencephalitis in humans as well as livestock in Central and South America, andsome variants of Sinbis Virus (SIN) and Semliki Forest Virus (SFV) have beenfound to cause fever and arthritis in humans [].Alphaviruses possess a single-stranded RNA genome of approximately 12 kb. The genomic RNA of alphaviruses is translated into two polyproteins that,respectively, encode structural proteins and nonstructural proteins. Thenonstructural proteins may be translated as one or two polyproteins, nsp123 ornsp1234, depending on the virus. These polyproteins are cleaved to generatensp1, nsp2, nsp3 and nsp4 by a protease activity that resides within nsp2. Thensp2 protein of alphaviruses has multiple enzymatic acivities. Its N-terminaldomain has been shown to possess ATPase and GTPase activity, RNA helicaseactivity and RNA 5'-triphosphatase activity. The C-terminal nsp2pro domain ofnsp2 is responsible for the regulation of 26S subgenome RNA synthesis,switching between negative- and positive-strand RNA synthesis, targeting nsp2for nuclear transport and proteolytic processing of the nonstructuralpolyprotein [, ]. The nsp2pro domain is a member of peptidase family C9 of clan CA.The nsp2pro domain consists of two distinct subdomains. Thensp2pro N-terminal subdomain is largely α-helical and contains thecatalytic dyad cysteine and histidine residues organised in a protein foldthat differs significantly from any known cysteine protease or protein folds.The nsp2pro C-terminal subdomain displays structural similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases and provides essential elementsthat contribute to substrate recognition and may also regulate the structureof the substrate binding cleft [].This domain covers the entire nsp2pro domain.A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. In only one family of cysteine peptidases, is the role of the general base assigned to a residue other than a histidine: in peptidases from family C89 (acid ceramidase) an arginine is the general base. Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. From sequence similarities, cysteine peptidases can be clustered into over 80 different families []. Clans CF, CM, CN, CO, CP and PD contain only one family.Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They are inhibited by thiol chelators such as iodoacetate, iodoacetic acid, N-ethylmaleimide or p-chloromercuribenzoate.Clan CA includes proteins with a papain-like fold. There is a catalytic triad which occurs in the order: Cys/His/Asn (or Asp). A fourth residue, usually Gln, is important for stabilising the acyl intermediate that forms during catalysis, and this precedes the active site Cys. The fold consists of two subdomains with the active site between them. One subdomain consists of a bundle of helices, with the catalytic Cys at the end of one of them, and the other subdomain is a β-barrel with the active site His and Asn (or Asp). There are over thirty families in the clan, and tertiary structures have been solved for members of most of these. Peptidases in clan CA are usually sensitive to the small molecule inhibitor E64, which is ineffective against peptidases from other clans of cysteine peptidases [].Clan CD includes proteins with a caspase-like fold. Proteins in the clan have an α/β/α sandwich structure. There is a catalytic dyad which occurs in the order His/Cys. The active site His occurs in a His-Gly motif and the active site Cys occurs in an Ala-Cys motif; both motifs are preceded by a block of hydrophobic residues []. Specificity is predominantly directed towards residues that occupy the S1 binding pocket, so that caspases cleave aspartyl bonds, legumains cleave asparaginyl bonds, and gingipains cleave lysyl or arginyl bonds.Clan CE includes proteins with an adenain-like fold. The fold consists of two subdomains with the active site between them. One domain is a bundle of helices, and the other a β-barrell. The subdomains are in the opposite order to those found in peptidases from clan CA, and this is reflected in the order of active site residues: His/Asn/Gln/Cys. This has prompted speculation that proteins in clans CA and CE are related, and that members of one clan are derived from a circular permutation of the structure of the other.Clan CL includes proteins with a sortase B-like fold. Peptidases in the clan hydrolyse and transfer bacterial cell wall peptides. The fold shows a closed β-barrel decorated with helices with the active site at one end of the barrel []. The active site consists of a His/Cys catalytic dyad.Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases.
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Publication
22174793 | J:182258
First Author: Taher L
Year: 2011
Journal: PLoS One
Title: Global gene expression analysis of murine limb development.
Volume: 6
Issue: 12
Pages: e28358
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Protein
Q8K480
Organism: Mus musculus/domesticus
Length: 584  
Fragment?: false
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Protein
Q8K0Q8
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: true
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Protein
Q1XD56
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
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Protein
A0A0U1RNR7
Organism: Mus musculus/domesticus
Length: 584  
Fragment?: false
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