Search by BoMiProt ID - Bomi4814


Primary Information

BoMiProt ID Bomi4814
Protein Name Collagen alpha-2(I) chain/Alpha-2 type I collagen
Organism Bos taurus
Uniprot IdP02465
Milk FractionWhey
Ref Sequence Id NP_776945.1
Aminoacid Length 1364
Molecular Weight 129064
Fasta Sequence https://www.uniprot.org/uniprot/P02465.fasta
Gene Name COL1A2
Gene Id 282188
Protein Existence Status reviewed

Secondary Information

Protein Function ECM component,responsible for ECM assembly.Type ! Collagen is composed of two α1 chains and one α2 chain encoded by two distinct genes, type I α1 collagen (COL1A1) and type I α2 collagen (COL1A2).major producer of collagen type I in the fibrotic liver.
PTMs Disulfide bond formation, Glycosylation, Hydroxylation, Pyrrolidone carboxylic acid addition.
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P02465|CO1A2_BOVIN Collagen alpha-2(I) chain OS=Bos taurus OX=9913 GN=COL1A2 PE=1 SV=2 MLSFVDTRTLLLLAVTSCLATCQSLQEATARKGPSGDRGPRGERGPPGPPGRDGDDGIPG PPGPPGPPGPPGLGGNFAAQFDAKGGGPGPMGLMGPRGPPGASGAPGPQGFQGPPGEPGE PGQTGPAGARGPPGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFK*175GIRGH NGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGP VGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGA NGLPGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGE PGAVGQPGPPGPSGEEGKRGSTGEIGPAGPPGPPGLRGNPGSRGLPGADGRAGVMGPAGS RGATGPAGVRGPNGDSGRPGEPGLMGPRGFPGSPGNIGPAGKEGPVGLPGIDGRPGPIGP AGARGEPGNIGFPGPKGPSGDPGKAGEKGHAGLAGARGAPGPDGNNGAQGPPGLQGVQGG KGEQGPAGPPGFQGLPGPAGTAGEAGKPGERGIPGEFGLPGPAGARGERGPPGESGAAGP TGPIGSRGPSGPPGPDGNKGEPGVVGAPGTAGPSGPSGLPGERGAAGIPGGKGEKGETGL RGDIGSPGRDGARGAPGAIGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGP NGFAGPAGAAGQPGAKGERGTKGPKGENGPVGPTGPVGAAGPSGPNGPPGPAGSRGDGGP PGATGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRSGETGASGPPGF VGEKGPSGEPGTAGPPGTPGPQGLLGAPGFLGLPGSRGERGLPGVAGSVGEPGPLGIAGP PGARGPPGNVGNPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNAGPVGAAGA PGPQGPVGPVGKHGNRGEPGPAGAVGPAGAVGPRGPSGPQGIRGDKGEPGDKGPRGLPGL KGHNGLQGLPGLAGHHGDQGAPGAVGPAGPRGPAGPSGPAGKDGRIGQPGAVGPAGIRGS QGSQGPAGPPGPPGPPGPPGPSGGGYEFGFDGDFYRADQPRSPTSLRPKDYEVDATLKSL NNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGET CIRAQPEDIPVKNWYRNSKAKKHVWVGETINGGTQFEYNVEGVTTKEMATQLAFMRLLAN HASQN*1265ITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTN EWQKTIIEYKTNKPSRLPILDIAPLDIGGADQEIRLNIGPVCFK
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Hydroxylation of proline and lysine occurs only in the Y-position of the triplet Gly-X-Y.
Bibliography 1.Fietzek PP, Rexrodt FW. The covalent structure of collagen. The amino-acid sequence of alpha2-CB4 from calf-skin collagen. Eur J Biochem. 1975 Nov 1;59(1):113-8. doi: 10.1111/j.1432-1033.1975.tb02431.x. PMID: 173531. 2.Zhao Y, Shi X, Ding C, Feng D, Li Y, Hu Y, Wang L, Gao D, Tian X, Yao J. Carnosic acid prevents COL1A2 transcription through the reduction of Smad3 acetylation via the AMPKα1/SIRT1 pathway. Toxicol Appl Pharmacol. 2018 Jan 15;339:172-180. doi: 10.1016/j.taap.2017.12.010. Epub 2017 Dec 15. PMID: 29253500.