CO2A1_RAT
ID CO2A1_RAT Reviewed; 1419 AA.
AC P05539; Q63123; Q63565; Q78DY3;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Collagen alpha-1(II) chain {ECO:0000250|UniProtKB:P02458};
DE AltName: Full=Alpha-1 type II collagen {ECO:0000250|UniProtKB:P02458};
DE Contains:
DE RecName: Full=Collagen alpha-1(II) chain {ECO:0000250|UniProtKB:P02458};
DE Contains:
DE RecName: Full=Chondrocalcin {ECO:0000250|UniProtKB:P02458};
DE Flags: Precursor;
GN Name=Col2a1 {ECO:0000312|RGD:2375};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone;
RA Urabe K., Sarkar G., Bolander M.E.;
RT "Complete rat type II collagen cDNA sequence.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-122.
RX PubMed=6094525; DOI=10.1016/s0021-9258(18)89796-4;
RA Kohno K., Martin G.R., Yamada Y.;
RT "Isolation and characterization of a cDNA clone for the amino-terminal
RT portion of the pro-alpha 1(II) chain of cartilage collagen.";
RL J. Biol. Chem. 259:13668-13673(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=2984204; DOI=10.1016/s0021-9258(18)89284-5;
RA Kohno K., Sullivan M., Yamada Y.;
RT "Structure of the promoter of the rat type II procollagen gene.";
RL J. Biol. Chem. 260:4441-4447(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 370-422.
RC STRAIN=DA; TISSUE=Cartilage;
RX PubMed=8046350; DOI=10.1084/jem.180.2.745;
RA Michaelson E., Malmstrom V., Reis S., Engstrom A., Burkhardt H.,
RA Holmdahl R.;
RT "T-cell recognition of carbohydrates on type II collagen.";
RL J. Exp. Med. 180:745-749(1994).
RN [5]
RP HYDROXYLATION AT PRO-591; PRO-600; PRO-602; PRO-603; PRO-606; PRO-839;
RP PRO-840; PRO-846; PRO-852; PRO-1076; PRO-1113; PRO-1118; PRO-1119;
RP PRO-1133; PRO-1134; PRO-1137; PRO-1139; PRO-1140 PRO-1143; PRO-1145 AND
RP PRO-1146, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21757687; DOI=10.1074/jbc.m111.267906;
RA Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.;
RT "A role for prolyl 3-hydroxylase 2 in post-translational modification of
RT fibril-forming collagens.";
RL J. Biol. Chem. 286:30662-30669(2011).
CC -!- FUNCTION: Type II collagen is specific for cartilaginous tissues. It is
CC essential for the normal embryonic development of the skeleton, for
CC linear growth and for the ability of cartilage to resist compressive
CC forces.
CC -!- SUBUNIT: Homotrimers of alpha 1(II) chains.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Expressed in chondrocytes.
CC {ECO:0000269|PubMed:21757687}.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function (By similarity). {ECO:0000250}.
CC -!- PTM: Contains mostly 4-hydroxyproline. Prolines at the third position
CC of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or
CC all of the chains. {ECO:0000269|PubMed:21757687}.
CC -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs
CC on the first proline residue in the sequence motif Gly-Pro-Hyp, where
CC Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:21757687}.
CC -!- PTM: Lysine residues at the third position of the tripeptide repeating
CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
CC {ECO:0000305}.
CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC glycan consists of a Glc-Gal disaccharide. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; L48440; AAA79780.1; -; mRNA.
DR EMBL; K02804; AAA40919.1; -; mRNA.
DR EMBL; M10613; AAA40920.1; -; Genomic_DNA.
DR EMBL; X79816; CAA56213.1; -; mRNA.
DR PIR; A05152; A05152.
DR PIR; I60384; I60384.
DR RefSeq; NP_037061.1; NM_012929.1.
DR AlphaFoldDB; P05539; -.
DR BioGRID; 247447; 1.
DR IntAct; P05539; 1.
DR STRING; 10116.ENSRNOP00000016044; -.
DR GlyGen; P05539; 8 sites.
DR PaxDb; P05539; -.
DR PRIDE; P05539; -.
DR ABCD; P05539; 18 sequenced antibodies.
DR DNASU; 25412; -.
DR GeneID; 25412; -.
DR KEGG; rno:25412; -.
DR UCSC; RGD:2375; rat.
DR CTD; 1280; -.
DR RGD; 2375; Col2a1.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P05539; -.
DR OrthoDB; 337699at2759; -.
DR PhylomeDB; P05539; -.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1474244; Extracellular matrix organization.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-419037; NCAM1 interactions.
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR PRO; PR:P05539; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0005581; C:collagen trimer; ISO:RGD.
DR GO; GO:0005585; C:collagen type II trimer; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042289; F:MHC class II protein binding; ISO:RGD.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
DR GO; GO:0097065; P:anterior head development; ISO:RGD.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0001502; P:cartilage condensation; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; IEP:RGD.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEP:RGD.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071316; P:cellular response to nicotine; IEP:RGD.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEP:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0071306; P:cellular response to vitamin E; IEP:RGD.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0002062; P:chondrocyte differentiation; IEP:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0003417; P:growth plate cartilage development; IEP:RGD.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0060174; P:limb bud formation; ISO:RGD.
DR GO; GO:0035108; P:limb morphogenesis; ISO:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0030903; P:notochord development; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0071599; P:otic vesicle development; ISO:RGD.
DR GO; GO:0006029; P:proteoglycan metabolic process; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0071774; P:response to fibroblast growth factor; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0010165; P:response to X-ray; IEP:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 3.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..113
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005735"
FT CHAIN 114..1173
FT /note="Collagen alpha-1(II) chain"
FT /id="PRO_0000005736"
FT CHAIN 1174..1419
FT /note="Chondrocalcin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043407"
FT DOMAIN 1185..1419
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 28..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..1146
FT /note="Triple-helical region"
FT REGION 1147..1173
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 113..114
FT /note="Cleavage; by procollagen N-endopeptidase"
FT /evidence="ECO:0000250"
FT SITE 1173..1174
FT /note="Cleavage; by procollagen C-endopeptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 122
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 219
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 231
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 240
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 306
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 540
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 552
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 591
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 600
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 602
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 603
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 606
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 839
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 840
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 846
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 852
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1076
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1113
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1118
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1119
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1133
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1134
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1137
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1139
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1140
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1143
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1145
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1146
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21757687"
FT CARBOHYD 122
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 231
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 240
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 306
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 540
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 552
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1215..1247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1221
FT /note="Interchain (with C-1238)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1238
FT /note="Interchain (with C-1221)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1255..1417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1325..1370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 121
FT /note="E -> Q (in Ref. 2; AAA40919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1419 AA; 134570 MW; B7C63B77819CE50B CRC64;
MIRLGAPQSL VLLTLLIATV LQCQGQDARK LGPKGQKGEP GDIKDIIGPK GPPGPQGPAG
EQGPRGDRGD KGERGAPGPR GRDGEPGTPG NPGPPGPPGP PGPPGLGGGN FAAQMAGGFD
EKAGGAQMGV MQGPMGPMGP RGPPGPAGAP GPQGFQGNPG EPGEPGVSGP IGPRGPPGPA
GKPGDDGEAG KPGKAGERGL PGPQGARGFP GTPGLPGVKG HRGYPGLDGA KGEAGAPGVK
GESGSPGENG SPGPMGPRGL PGERGRTGPA GAAGARGNDG QPGPAGPPGP VGPAGGPGFL
GAPGAKGEAG PTGARGPEGA QGSRGEPGNP GSPGPAGASG NPGTDGIPGA KGSAGAPGIA
GAPGFPGPRG PPGPQGATGP LGPKGQTGEP GIAGFKGEQG PKGETGPAGP QGAPGPAGEE
GKRGARGEPG GAGPIGPPGE RGAPGNRGFP GQDGLAGPKG APGERGPSGL AGPKGANGDP
GRPGEPGLPG ARGLTGRPGD AGPQGKVGPS GAPGEDGRPG PPGPQGARGQ PGVMGFPGPK
GANGEPGKAG EKGLAGAPGL RGLPGKDGET GAAGPPGPSG PAGERGEQGA PGPSGFQGLP
GPPGPPGEGG KQGDQGIPGE AGAPGLVGPR GERGFPGERG SPGAQGLQGP RGLPGTPGTD
GPKGAAGPDG PPGAQGPPGL QGMPGERGAA GIAGPKGDRG DVGEKGPEGA PGKDGGRGLT
GPIGPPGPAG ANGEKGEVGP PGPSGSTGAR GAPGERGETG PPGPAGFAGP PGADGQPGAK
GDQGEAGQKG DAGAPGPQGP SGAPGPQGPT GVTGPKGARG AQGPPGATGF PGAAGRVGPP
GSNGNPGPAG PPGPAGKDGP KGARGDTGAP GRAGDPGLQG PAGAPGEKGE PGDDGPSGSD
GPPGPQGLAG QRGIVGLPGQ RGERGFPGLP GPSGEPGKQG APGASGDRGP PGPVGPPGLT
GPAGEPGREG SPGADGPPGR DGAAGVKGDR GETGALGAPG APGPPGSPGP AGPTGKQGDR
GEAGAQGPMG PSGPAGARGI AGPQGPRGDK GEAGEPGERG LKGHRGFTGL QGLPGPPGPS
GDQGTSGPAG PSGPRGPPGP VGPSGKDGSN GIPGPIGPPG PRGRSGETGP AGPPGNPGPP
GPPGPPGPGI DMSAFAGLGQ REKGPDPLQY MRADEADSTL RQHDVEVDAT LKSLNNQIES
IRSPDGSRKN PARTCQDLKL CHPEWKSGDY WIDPNQGCTL DAMKVFCNME TGESCVYPNP
ATVPRKNWWS SKSKEKKHIW FGETMNGGFH FSYGDGNLAP NTANVQMTFL RLLSTEGSQN
ITYHCKNSIA YLDEAAGNLK KALLIQGSND VEMRAEGNSR FTYTALKDGC TKHTGKWGKT
IIEYRSQKTS RLPIVDIAPM DIGGPDQEFG VDIGPVCFL
