Search by BoMiProt ID - Bomi132


Primary Information

BoMiProt ID Bomi132
Protein Name Angiogenin2
Organism Bos taurus
Uniprot IdP80929
Milk FractionWhey
Amino Acid Lenth 123
Molecular Weight 14522
Fasta Sequence https://www.uniprot.org/uniprot/P80929.fasta
Gene Name ANG2
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function cell adhesion , nuclear translocation , actin binding , inhibition of cell-free translation or hydrolysis of tRNA; highly active in inducing blood-vessel growth
Biochemical Properties basic angiogenic protein that binds tightly to placental ribonuclease inhibitor; the amino-terminal and carboxyl-terminal residues are pyroglutamic acid and proline; ribonucleolytic activity that is similar to, but somewhat lower than bovine angiogenin 1; angiogenically potent on chicken chorioallantoic membrane; bovine angiogenin-2 was 20 kDa, larger than that of bovine angiogenin-I (14kDa)
Significance in milk Milk contains considerably more bovine angiogenin than does serum; binds to PRI but had very little RNase activit
PTMs cross-linked by three disulfide bonds, is glycosylated at Asn33; contained 5 - 6 mannose, 2- 3 glucosamine, 1-2 galactosamine, up to one xylose and no sialic acid residues;
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P80929|ANG2_BOVIN Angiogenin-2 OS=Bos taurus OX=9913 GN=ANG2 PE=1 SV=1
QNDAYRGFLRKHYDPSPTGHDDRYCNTMMERRN*33MTRPCKDTNTFIHGNSDDIRAVCDDRN GEPYRNGLRRSRSPFQVTTCRHRGGSPRPPCRYRAFRANRVIVIRCRDGFPIHLEENFIP PRP
Significance of PTMs modification of bovine angiogenin-2 is on Am33 and should physically cover a large surface area of bovine angiogenin-2, as on RNase B, some modulation of nuclear translocation may be possible, even though bovine angiogenin-2 is an active angiogenic molecule
Bibliography 1. Strydom, D. J., Bond, M. D., & Vallee, B. L. (1997). An angiogenic protein from bovine serum and milk--purification and primary structure of angiogenin-2. European Journal of Biochemistry, 247(2), 535–544. https://doi.org/10.1111/j.1432-1033.1997.00535.