Primary Information |
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BoMiProt ID | Bomi4808 |
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Protein Name | Collagen alpha-1(II) chain/Alpha-1 type II collagen |
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Organism | Bos taurus |
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Uniprot ID | P02459 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001001135.2 |
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Aminoacid Length | 1487 |
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Molecular Weight | 141828 |
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FASTA Sequence |
Download |
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Gene Name | COL2A1 |
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Gene ID | 407142 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Functioning of cartilaginous tissues.A fibrillar collagen found in cartilage and the vitreous humor of the eye. |
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PTMs | Hydroxylation on proline residues,N and O linked glycosylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P02459|CO2A1_BOVIN Collagen alpha-1(II) chain OS=Bos taurus OX=9913 GN=COL2A1 PE=1 SV=4
MIRLGAPQTLVLLTLLVAAVLRCHGQDVQKAGSCVQDGQRYNDKDVWKPEPCRICVCDTG
TVLCDDIICEDMKDCLSPETPFGECCPICSADLPTASGQPGPKGQKGEPGDIKDIVGPKG
PPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFA
AQMAGGFDEK*190AGGAQMGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMG
PRGPPGPPGKPGDDGEAGKPGKSGERGPPGPQGARGFPGTPGLPGVK*287GHRGYPGLDGAK*299G
EAGAPGVK*308GESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVG
PAGGPGFPGAPGAK*374GEAGPTGARGPEGAQGPRGEPGTPGSPGPAGAAGNPGTDGIPGAKG
SAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQG
APGPAGEEGKRGARGEPGGAGPAGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAG
PKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPG
VMGFPGPK*608GANGEPGKAGEK*629GLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPG
PSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGSQGLQGARG
LPGTPGTDGPKGAAGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPG
KDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGTAGARGAPGERGETGPPGPAGFAGPPG
ADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPG
AAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGDPGLQGPAGPPGEKGEPG
DDGPSGPDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPG
PVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAG
PIGKQGDRGEAGAQGPMGPAGPAGARGMPGPQGPRGDKGETGEAGERGLK*1130GHRGFTGLQG
LPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAG
PPGNPGPPGPPGPPGPGIDMSAFAGLGQREKGPDPLQYMRADEAAGNLRQHDAEVDATLK
SLNNQIESLRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETG
ETCVYPNPASVPKKNWWSSKSKDKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRL
LSTEGSQN*1388ITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTVLKDGCTK
HTGKWGKTMIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL
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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 the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains and Proline residues at the second position of G-P-X are hydroxylated in some of the chains.Prolines at the third position of the tripeptide repeat are 4-hydroxylated in some chains.O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. |
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Bibliography | 1.Butler WT, Miller EJ, Finch JE Jr. The covalent structure of cartilage collagen. Amino acid sequence of the NH2-terminal helical portion of the alpha 1 (II) chain. Biochemistry. 1976 Jul 13;15(14):3000-6. doi: 10.1021/bi00659a010. PMID: 782511. |