CO2A1_XENTR
ID CO2A1_XENTR Reviewed; 1492 AA.
AC Q6P4Z2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Flags: Precursor;
GN Name=col2a1 {ECO:0000250|UniProtKB:P02458};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimers of alpha 1(II) chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
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:0000250|UniProtKB:P05539}.
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:0000250|UniProtKB:P05539}.
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:0000250|UniProtKB:P05539}.
CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC glycan consists of a Glc-Gal disaccharide.
CC {ECO:0000250|UniProtKB:P05539}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; BC063191; AAH63191.1; -; mRNA.
DR RefSeq; NP_989220.1; NM_203889.1.
DR AlphaFoldDB; Q6P4Z2; -.
DR SMR; Q6P4Z2; -.
DR PaxDb; Q6P4Z2; -.
DR PRIDE; Q6P4Z2; -.
DR Ensembl; ENSXETT00000043834; ENSXETP00000043834; ENSXETG00000010655.
DR GeneID; 394828; -.
DR KEGG; xtr:394828; -.
DR CTD; 1280; -.
DR Xenbase; XB-GENE-6258353; col2a1.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q6P4Z2; -.
DR OrthoDB; 337699at2759; -.
DR Reactome; R-XTR-1442490; Collagen degradation.
DR Reactome; R-XTR-1474244; Extracellular matrix organization.
DR Reactome; R-XTR-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-XTR-186797; Signaling by PDGF.
DR Reactome; R-XTR-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-XTR-216083; Integrin cell surface interactions.
DR Reactome; R-XTR-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-XTR-3000178; ECM proteoglycans.
DR Reactome; R-XTR-419037; NCAM1 interactions.
DR Reactome; R-XTR-8874081; MET activates PTK2 signaling.
DR Reactome; R-XTR-8948216; Collagen chain trimerization.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000010655; Expressed in neurula embryo and 21 other tissues.
DR ExpressionAtlas; Q6P4Z2; baseline.
DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0030903; P:notochord development; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 6.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..186
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000286181"
FT CHAIN 187..1246
FT /note="Collagen alpha-1(II) chain"
FT /id="PRO_0000286182"
FT PROPEP 1247..1492
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000286183"
FT DOMAIN 36..94
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1258..1492
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 98..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..1219
FT /note="Triple-helical region"
FT REGION 1220..1246
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 138..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 186..187
FT /note="Cleavage; by procollagen N-endopeptidase"
FT /evidence="ECO:0000250"
FT SITE 1246..1247
FT /note="Cleavage; by procollagen C-endopeptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 664
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 673
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 675
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 676
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 679
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 912
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 913
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 919
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 925
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1149
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1186
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1191
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1192
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1206
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1207
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1210
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1212
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1213
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1216
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1218
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1219
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT CARBOHYD 1393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1288..1320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1294
FT /note="Interchain (with C-1311)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1311
FT /note="Interchain (with C-1294)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1328..1490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1398..1443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ SEQUENCE 1492 AA; 142696 MW; DB7AF42B94210EB7 CRC64;
MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLATGSCVQ HGQRYSDKDV WKPEPCQICV
CDTGNVLCDE IICEDPKDCP NAEIPFGECC PICPTEQSST SSGQGVLKGQ KGEPGDIKDV
VGPKGPPGPQ GPSGEQGPRG DRGDKGEKGA PGPRGRDGEP GTPGNPGPVG PPGPPGPPGL
GGNFAAQMTG GFDEKAGGAQ MGVMQGPMGP MGPRGPPGPT GAPGPQGFQG NPGEPGEPGA
GGPMGPRGPP GPAGKPGDDG EAGKPGKSGE RGPPGPQGAR GFPGTPGLPG VKGHRGYPGL
DGSKGEAGAA GAKGEGGATG EAGSPGPMGP RGLPGERGRP GASGAAGARG NDGLPGPAGP
PGPVGPAGAP GFPGAPGSKG EAGPTGARGP EGAQGPRGES GTPGSPGPAG ASGNPGTDGI
PGAKGSSGAP GIAGAPGFPG PRGPPGPQGA TGPLGPKGQT GDPGVAGFKG EHGPKGEIGS
AGPQGAPGPA GEEGKRGARG EPGAAGPLGP PGERGAPGNR GFPGQDGLAG PKGAPGERGV
PGLGGPKGAN GDPGRPGEPG LPGARGLTGR PGDAGPQGKV GPSGASGEDG RPGPPGPQGA
RGQPGVMGFP GPKGANGEPG KAGEKGLLGA PGLRGLPGKD GETGAQGPNG PAGPAGERGE
QGPPGPSGFQ GLPGPPGSPG EGGKPGDQGV PGEAGAPGLV GPRGERGFPG ERGSSGPQGL
QGPRGLPGTP GTDGPKGATG PSGPNGAQGP PGLQGMPGER GAAGISGPKG DRGDTGEKGP
EGAPGKDGSR GLTGPIGPPG PSGPNGEKGE SGPSGPAGIV GARGAPGDRG ETGPPGPAGF
AGPPGADGQA GLKGDQGESG QKGDAGAPGP QGPSGAPGPQ GPTGVNGPKG ARGAQGPPGA
TGFPGAAGRV GPPGPNGNPG PSGAPGSAGK EGPKGARGDA GPTGRAGDPG LQGPAGVPGE
KGESGEDGPS GPDGPPGPQG LSGQRGIVGL PGQRGERGFP GLPGPSGEPG KQGGPGSAGD
RGPPGPVGPP GLTGPAGEPG REGNAGSDGP PGRDGATGIK GDRGETGPLG APGAPGAPGA
PGPVGPTGKQ GDRGESGPQG PLGPSGPAGA RGLPGPQGPR GDKGEAGEAG ERGQKGHRGF
TGLQGLPGPP GTAGDQGASG PAGPGGPRGP PGPVGPSGKD GSNGLPGPIG PPGPRGRGGE
TGPAGPPGQP GPPGPPGPPG PGIDMSAFAG LSQPEKGPDP MRYMRADQAS SSVPQRDVDV
EATLKSLNNQ IESIRSPDGT KKNPARTCRD LKLCHPEWKS GDYWIDPNQG CTVDAIKVFC
NMETGETCVY PNPSKIPKKN WWSAKGKEKK HIWFGETING GFQFSYGDDS SAPNTANIQM
TFLRLLSTDA TQNITYHCKN SIAFMDEASG NLKKAVLLQG SNDVEIRAEG NSRFTYNALE
DGCKKHTGKW SKTVIEYRTQ KTSRLPIVDI APMDIGGADQ EFGVDIGPVC FL
