Primary Information |
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| BoMiProt ID | Bomi4807 |
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| Protein Name | Collagen alpha-1(I) chain/Alpha-1 type I collagen |
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| Organism | Bos taurus |
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| Uniprot ID | P02453 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001029211.1 |
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| Aminoacid Length | 1463 |
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| Molecular Weight | 138938 |
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| FASTA Sequence |
Download |
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| Gene Name | COL1A1 |
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| Gene ID | 282187 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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. |
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| 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. |
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| 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. |
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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
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| 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. |
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| 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. |
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