Search by BoMiProt ID - Bomi4807


Primary Information

BoMiProt ID Bomi4807
Protein Name Collagen alpha-1(I) chain/Alpha-1 type I collagen
Organism Bos taurus
Uniprot IdP02453
Milk FractionWhey
Ref Sequence Id NP_001029211.1
Aminoacid Length 1463
Molecular Weight 138938
Fasta Sequence https://www.uniprot.org/uniprot/P02453.fasta
Gene Name COL1A1
Gene Id 282187
Protein Existence Status reviewed

Secondary Information

Protein Function Type I collagen is a trimer formed by two α1 chains and one α2 chain. These subunits are encoded by COL1A1 and COL1A2 respectively. ECM component important for its assembly.COL1A1 inhibition triggers cumulus cell apoptosis.Has a potential role in the growth and development of bovine follicles.regulates mitochondrial activity, ROS, and autophagy level.
Biochemical Properties Collagen has a triple-stranded rope-like coiled structure. The major collagen of skin, tendon, and bone is the same protein containing 2 alpha-1 polypeptide chains and 1 alpha-2 chain.Contain triple-helical gly-X-Y repeats in each chain.
PTMs O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.Disulfide bond formation, Hydroxylation, Phosphorylation, Pyrrolidone carboxylic acid.
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P02453|CO1A1_BOVIN Collagen alpha-1(I) chain OS=Bos taurus OX=9913 GN=COL1A1 PE=1 SV=3 MFSFVDLRLLLLLAATALLTHGQEEGQEEGQEEDIPPVTCVQNGLRYHDRDVWKPVPCQI CVCDNGNVLCDDVICDELKDCPNAKVPTDECCPVCPEGQESPTDQETTGVEGPKGDTGPR GPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKS*171TGISVPGPM GPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRP GERGPPGPQGARGLPGTAGLPGMKGHRGFS*270GLDGAKGDAGPAGPKGEPGSPGENGAPGQM GPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEGGPQGPR GSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQ GPSGPPGPKGNSGEPGAPGSKGDTGAKGEPGPTGIQGPPGPAGEEGKRGARGEPGPAGLP GPPGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLT GSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVP GPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQ GVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQ GAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGKDGVRGLTGPIGPPGPAGAPGDK GEAGPS*786GPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPP GPAGPAGPPGPIGNVGAPGPKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPA GKEGSKGPRGETGPAGRPGEVGPPGPPGPAGEKGAPGADGPAGAPGTPGPQGIAGQRGVV GLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAE GSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPAGPIGPV GARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPR GPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDAGPAGPPGPPGPPGPPGPPSGGYDLSFL PQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRD LKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKEK RHVWYGESMTGGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQT GNLKKALLLQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIID VAPLDVGAPDQEFGFDVGPACFL
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Proline residues at Y position of the tripeptide repeating unit (G-X-Y) are hydroxylated.Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.
Bibliography 1.Rauterberg J, Fietzek P, Rexrodt F, Becker U, Stark M, Kühn K. The amino acid sequence of the carboxyterminal nonhelical cross link region of the alpha 1 chain of calf skin collagen. FEBS Lett. 1972 Mar;21(1):75-79. doi: 10.1016/0014-5793(72)80167-4. PMID: 11946479. 2.Fu XH, Chen CZ, Wang Y, Peng YX, Wang WH, Yuan B, Gao Y, Jiang H, Zhang JB. COL1A1 affects apoptosis by regulating oxidative stress and autophagy in bovine cumulus cells. Theriogenology. 2019 Nov;139:81-89. doi: 10.1016/j.theriogenology.2019.07.024. Epub 2019 Jul 23. PMID: 31377650.