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Search results 1 to 13 out of 13 for Wap

Category restricted to ProteinDomain (x)

0.018s

Categories

Category: ProteinDomain
« show all
Type Details Score
Protein Domain
IPR037490 | WAP
Type: Family
Description: This family of plant proteins consists of WPP domain-associated proteins (WAPs). WAP interacts through its coiled-coil domain with several WPP-domain containing proteins and it is localized at the Golgi. It is required for complex formation of WPP-domain proteins [].
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Protein Domain
IPR029726 | Wfdc3
Type: Family
Description: WAP four-disulfide core domain protein 3 (Wfdc3) contains WAP domains []. Its function is not clear.
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Protein Domain
IPR029720 | WFDC13
Type: Family
Description: WAP four-disulfide core domain protein 13 (WFDC13) contains a WAP domain and is a putative acid-stable proteinase inhibitor.
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Protein Domain
IPR029721 | WFDC10A
Type: Family
Description: WAP four-disulfide core domain protein 10A (WFDC10A) contains a WAP domain. In monkeys, it is expressed in the epididymis and have antibacterial activity [].
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Protein Domain
IPR042931 | WFDC8
Type: Family
Description: The function of WAP four-disulfide core domain protein 8 (WFDC8) is not clear.
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Protein Domain
IPR029718 | WFDC12
Type: Family
Description: WAP four-disulfide core domain protein 12 (WFDC12, also known as Swam2) is an antibacterial protein that might function as a acid-stable proteinase inhibitor [].
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Protein Domain
IPR042357 | WFDC1
Type: Family
Description: WAP four-disulfide core domain protein 1 (WFDC1), also known as ps20, has been implicated in epithelial cell behaviour and angiogenesis []. It has been linked to prostate cancer [].
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Protein Domain
IPR020310 | WFDC11
Type: Family
Description: Protein WFDC11 was isolated in a region containing several WAP proteins and were defined as WAP proteins, however, it does not contain a classical WAP domain. In rats, WFDC11 is expressed in the epididymis of the male reproductive tract [].
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Protein Domain
IPR029725 | WFDC9
Type: Family
Description: Protein WFDC9 was isolated in a region containing several WAP proteins and was defined as a WAP protein; however, it doesn't contain a classical WAP domain. Its function is not clear.
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Protein Domain
IPR008197 | WAP_dom
Type: Domain
Description: The four-disulfide core (4-DSC) or WAP domain comprises eight cysteine residues involved in disulfide bonds in a conserved arrangement []. The four disulphide core containing Whey Acidic Proteins (WAP) are the major whey proteins in the milk of many mammals and are considered to be the prototypic members of the family. However the WAP domain is not exclusive to WAP proteins, but it is found in many other proteins, a number of which have been shown to exhibit antiproteinase function [].One or more of the WAP domains occur in the WDNM1 protein, which is involved in the metastatic potential of adenocarcinomas in rats []; Kallmann syndrome protein []; caltrin-like protein II from guinea pig [], which inhibits calcium transport into spermatozoa; elafin, a serine elastase inhibitor which belongs to MEROPS inhibitor family I17 []; and papilin, a metalloendopeptidase inhibitor which belongs to MEROPS inhibitor family I2 and is effective against procollagen N-proteinase [].
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Protein Domain
IPR010909 | PLAC
Type: Domain
Description: The PLAC (protease and lacunin) domain is a six-cysteine region of about 40 residues that is present at or near the C-terminal of various enzymes and matrix proteins, including: mammalian PACE4 (paired basic amino acid cleaving enzyme 4), mammalian PCSK5 (proprotein convertase subtilisin/kexin type 5), mammalian metalloproteinases ADAMTS-2, -3, -10, -12, -14, -16, -17, and -19, and manduca Sexta matrix protein lacunin []. The PLAC domain is often associated with other domains, such as the thrombospondin type I repeat (TSP1) (), the Kunitz proteinase inhibitor domain (), the Ig-like domain (), the WAP domain (), the subtilase domain (), or the ADAM-type metalloprotease domain ().
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Protein Domain
IPR019541 | Trappin_transglut-bd_rpt
Type: Repeat
Description: Trappin-2,a protease inhibitor, has a unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase []. This domain contains several repeated motifs (rpresented by this entry) with the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalysed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyse the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond []. Cementoin is associated with the WAP family, , at the C terminus.
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Protein Domain
IPR033638 | WFIKKN1/2
Type: Family
Description: WFIKKN proteins are secreted multidomain proteins containing a WAP (whey acidic protein)-, a follistatin/Kazal-, an immunoglobulin-, two Kunitz-type protease inhibitor-domains, and an NTR (netrin) domain. They have been reported to inhibit the activity of trypsin, and to bind GDF11 (growth and differentiation factor 11) and myostatin (GDF8) []. Due to the presence of multiple domains that frequently serve as protease inhibitors, WFIKKN proteins are presumed to control the action of diverse serine proteases as well as metalloproteinases [].In humans, WFIKKN1 expression is observed in pancreas, liver, thymus, kidney, testis and lung and WFIKKN2 (also known as WFIKKNRP) expression is observed in ovary, testis, pancreas, brain and lung [].
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