Predicate | Object |
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rdf:type | |
biopax3:comment |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2. Interacts with TRAM2 (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains. PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates. SIMILARITY: Belongs to the fibrillar collagen family. SIMILARITY: Contains 1 fibrillar collagen NC1 domain. SIMILARITY: Contains 1 VWFC domain. GENE SYNONYMS:Col1a1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
SEQUENCE 1453 AA; 137953 MW; BCDDC40C3167AE59 CRC64;
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biopax3:xref |
urn:biopax:RelationshipXref:NCBI GENE_29393,
urn:biopax:RelationshipXref:RAT GENOME DATABASE_61817,
urn:biopax:RelationshipXref:REFSEQ_NP_445756,
urn:biopax:UnificationXref:UNIPROT_A3KNA1,
urn:biopax:UnificationXref:UNIPROT_P02454,
urn:biopax:UnificationXref:UNIPROT_P02455,
urn:biopax:UnificationXref:UNIPROT_Q63079
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biopax3:displayName |
CO1A1_RAT
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biopax3:name |
Alpha-1 type I collagen,
Col1a1
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biopax3:entityFeature |
urn:biopax:ModificationFeature:CO1A1_RAT_1,
urn:biopax:ModificationFeature:CO1A1_RAT_10,
urn:biopax:ModificationFeature:CO1A1_RAT_11,
urn:biopax:ModificationFeature:CO1A1_RAT_12,
urn:biopax:ModificationFeature:CO1A1_RAT_2,
urn:biopax:ModificationFeature:CO1A1_RAT_3,
urn:biopax:ModificationFeature:CO1A1_RAT_4,
urn:biopax:ModificationFeature:CO1A1_RAT_5,
urn:biopax:ModificationFeature:CO1A1_RAT_6,
urn:biopax:ModificationFeature:CO1A1_RAT_7,
urn:biopax:ModificationFeature:CO1A1_RAT_8,
urn:biopax:ModificationFeature:CO1A1_RAT_9
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biopax3:organism | |
biopax3:sequence |
MFSFVDLRLLLLLGATALLTHGQEDIPEVSCIHNGLRVPNGETWKPDVCLICICHNGTAVCDGVLCKEDLDCPNPQKREGECCPFCPEEYVSPDAEVIGVEGPKGDPGPQGPRGPVGPPGQDGIPGQPGLPGPPGPPGPPGPPGLGGNFASQMSYGYDEKSAGVSVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDTGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPPGSAGARGNDGAVGAAGPPGPTGPTGPPGFPGAAGAKGEAGPQGARGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGAPGPKGNSGEPGAPGNKGDTGAKGEPGPAGVQGPPGPAGEEGKRGARGEPGPSGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPAGPPGARGQAGVMGFPGPKGTAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGAPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGNNGAPGNDGAKGDTGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGETGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDTGVKGDAGPPGPAGPAGPPGPIGNVGAPGPKGSRGAAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPVGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGSPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGSPGAEGSPGRDGAPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKNGDRGETGPAGPAGPIGPAGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGSPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDSGPAGPPGPPGPPGPPGPPSGGYDFSFLPQPPQEKSQDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVYCNMETGQTCVFPTQPSVPQKNWYISPNPKEKKHVWFGESMTDGFQFEYGSEGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKSLLLQGSNEIELRGEGNSRFTYSTLVDGCTSHTGTWGKTVIEYKTTKTSRLPIIDVAPLDIGAPDQEFGMDIGPACFV
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biopax3:standardName |
Collagen alpha-1(I) chain
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