WW Domain-Binding Protein 1 (WBP1) is widely expressed in many tissues, but it is lowly expressed in the lung, placenta, kidney, and liver. WBP1 contains two WW-binding motifs: WW-binding 1 and WW-binding 2 that are involved in mediating protein-protein interactions through the binding of polyproline ligands. The WW-binding domain is composed of 38 to 40 semi-conserved amino acids shared by proteins with diverse functions including structural, regulatory, and signaling proteins. In addition, WBP1 also encodes a ligand of the WW domain of the Yes kinase-associated protein. This function has not been determined.
WW Domain-Binding Protein 2 (WBP2) is a ubiquitous protein that contains one GRAM domain. The WW domain is composed of 38 to 40 semi-conserved AA shared by proteins of diverse functions including structural, regulatory, and signaling proteins. The domain is participated in mediating protein-protein interactions. WBP2 binds to the WW domain of YAP1, WWP1 and WWP2. The WW-binding 1 motif of WBP2 mediates interaction with NEDD4. The function of this protein WBP2 has not been determined. Some researches demonstrate that WBP-2 also interacts with the thyroid-specific transcription factor Pax8.
Human protein N-terminal glutamine amidohydrolase (WDYHV1) is an enzyme that in humans is encoded by the WDYHV1 gene, belongs to the NTAQ1 family.WDYHV1 mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, which is an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. However,it does not act on substrates with internal or C-terminal glutamine andnon-glutamine residues in any position. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine.
WAP Four-Disulfide Core Domain Protein 2 (WFDC2) is a 25 kDa secreted glycoprotein containing two WAP domains. Mature human WFDC2 is 94 amino acids (aa) in length. It contains two WAP domains that likely mediate antiprotease and/or antimicrobial activity (aa 31 - 73 and 74 - 123). There are four potential splice variants. One shows a deletion of aa 27-74, while three others show aa substitutions: 28 aa for aa 75-124, 23 aa for aa 1 - 74, and 10 aa for aa 71-124. WFDC2 is a member of a family of stable 4-disulfide core proteins that are secreted at high levels. It is expressed by a wide variety of epithelial cells, including respiratory epithelium, salivary gland mucous cells, breast duct epithelium, distal tubule renal epithelium, and epididymal epithelium. WFDC2 may be a component of the innate immune defences of the lung, nasal and oral cavities and suggest that WFDC2 functions in concert with related WAP domain containing proteins in epithelial host defence. WFDC2 re-expression in lung carcinomas may prove to be associated with tumour type and should be studied in further detail. Mammary gland expression of tammar WFDC2 during the course of lactation showed WFDC2 was elevated during pregnancy, reduced in early lactation and absent in mid-late lactation. WFDC2 can undergo a complex series of alternative splicing events that can potentially yield five distinct WAP domain containing protein isoforms.
WAP, kazal, immunoglobulin, kunitz and NTR domain-containing protein 2, also known as Growth and differentiation factor-associated serum protein 1, WAP, follistatin, immunoglobulin, kunitz and NTR domain-containing-related protein, WFIKKN-related protein, WFIKKN2 and GASP1, is a secreted protein which belongs to theWFIKKN family. WFIKKN2 contains twoBPTI/Kunitz inhibitor domains, oneIg-like C2-type (immunoglobulin-like) domain, oneKazal-like domain, oneNTR domain and oneWAP domain. WFIKKN2 is primarily expressed in ovary, testis and brain, but not in liver. In fetal tissues, it is primarily expressed in brain, skeletal muscle, thymus and kidney. WFIKKN2 is protease-inhibitor that contains multiple distinct protease inhibitor domains. It probably has serine protease- and metalloprotease-inhibitor activity. It inhibits the biological activity of mature myostatin, but not activin. WFIKKN2 protein binds mature GDF8/myostatin and myostatin propeptide and inhibits the biological activity of myostatin.
Downstream regulator in the Wnt/Frizzled-signaling pathway. Associated with cell survival. Attenuates p53-mediated apoptosis in response to DNA damage through activation of AKT kinase. Up-regulates the anti-apoptotic Bcl-X(L) protein. Adheres to skin and melanoma fibroblasts. In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan. Expressed in heart, kidney, lung, pancreas, placenta, ovary, small intestine and spleen. Isoform 2 is expressed predominantly in scirrhous gastric carcinoma and, weakly in placenta. Overexpression is associated with several cancers including breast cancer and colon tumors. Isoform 2 is overexpressed in scirrhous gastric carcinoma.
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