Search by BoMiProt ID - Bomi4808


Primary Information

BoMiProt ID Bomi4808
Protein Name Collagen alpha-1(II) chain/Alpha-1 type II collagen
Organism Bos taurus
Uniprot IDP02459
Milk FractionWhey
Ref Sequence ID NP_001001135.2
Aminoacid Length 1487
Molecular Weight 141828
FASTA Sequence Download
Gene Name COL2A1
Gene ID 407142
Protein Existence Status reviewed

Secondary Information

Protein Function Functioning of cartilaginous tissues.A fibrillar collagen found in cartilage and the vitreous humor of the eye.
PTMs Hydroxylation on proline residues,N and O linked glycosylation
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
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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.
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.