|Ref Sequence ID||NP_001029503.1|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||serum, cerebrospinal fluid, urine, saliva,sweat, semen, amniotic fluid|
|Protein Function||Stimulate lipolysis; potential biomarker for several carcinomas; has RNAse activity; regulation of melanin production; hinder tumor proliferation; transport of nephritic by-products; has important role in fertilization|
|Biochemical Properties||serum ZAG has blocked NH2 terminus; seminal ZAG has free NH2 terminus; complexed with the prolactin-inducible protein found in human seminal fluid and has blocked NH2 terminus due to the presence of pyroglutamine; presence of high tryptophan and tyrosine residues; high extinction coefficient (E1%1cm) of 18.0; the amino acid sequence of ZAG contains four half-cystine residues; the position of cysteine and disulfide pairing reveals the bond formation in between residues 101 and 164 and second one between residues 203 and 258; the far-UV CD spectrum of the native ZAG measured at pH 7.4 and 25°C has an intense negative peak at 218 nm; shows a reversible thermal transition curve - CD signal changes at 218 nm, which disappeared gradually on heating the protein sample in the temperature range 25°C to 85°C; shows high stability in the absence of peptide and ß2M|
|Significance in milk||Regulates lipid metabolism during lactation|
|PTMs||Glycosylated; typical N-linked biantennary structure,substituted with N-acetylneuraminic acid in a 2,6 linkage and lacks fucose; 4 putative glycosylation sites; Asn 89, 92,106, 239; Asn 89,106, 239 carry glucosamines; Asn 239 is heavilly silalylated on mannose 2,6 arm;|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||No TM helices|
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