ID   CO2A1_XENLA             Reviewed;        1486 AA.
AC   Q91717; Q7ZTI6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 98.
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 laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=1918153; DOI=10.1083/jcb.115.2.565;
RA   Su M.W., Suzuki H.R., Bieker J.J., Solursh M., Ramirez F.;
RT   "Expression of two nonallelic type II procollagen genes during Xenopus
RT   laevis embryogenesis is characterized by stage-specific production of
RT   alternatively spliced transcripts.";
RL   J. Cell Biol. 115:565-575(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-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   -!- DEVELOPMENTAL STAGE: Initially, the transcripts are localized to
CC       notochord, somites, and the dorsal region of the lateral plate
CC       mesoderm. At later stages of development and parallel to increased mRNA
CC       accumulation, collagen expression becomes progressively more confined
CC       to chondrogenic regions of the tadpole. {ECO:0000269|PubMed:1918153}.
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; M63595; AAA49678.1; -; mRNA.
DR   EMBL; BC048221; AAH48221.1; -; mRNA.
DR   EMBL; BC111515; AAI11516.1; -; mRNA.
DR   PIR; A40333; A40333.
DR   PIR; B40333; B40333.
DR   RefSeq; NP_001081258.1; NM_001087789.1.
DR   AlphaFoldDB; Q91717; -.
DR   SMR; Q91717; -.
DR   GlyCosmos; Q91717; 1 site, No reported glycans.
DR   DNASU; 397738; -.
DR   GeneID; 397738; -.
DR   KEGG; xla:397738; -.
DR   AGR; Xenbase:XB-GENE-6252613; -.
DR   CTD; 397738; -.
DR   Xenbase; XB-GENE-6252613; col2a1.L.
DR   OrthoDB; 2970887at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 397738; Expressed in internal ear and 7 other cell types or tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 7.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 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..183
FT                   /note="N-terminal propeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000286178"
FT   CHAIN           184..1243
FT                   /note="Collagen alpha-1(II) chain"
FT                   /id="PRO_0000286179"
FT   PROPEP          1244..1486
FT                   /note="C-terminal propeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000286180"
FT   DOMAIN          36..94
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          1252..1486
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          100..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..1216
FT                   /note="Triple-helical region"
FT   REGION          1217..1243
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        353..367
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..448
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1202..1219
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1300
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1302
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1303
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1305
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   SITE            183..184
FT                   /note="Cleavage; by procollagen N-endopeptidase"
FT                   /evidence="ECO:0000250"
FT   SITE            1243..1244
FT                   /note="Cleavage; by procollagen C-endopeptidase"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         661
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         670
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         672
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         673
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         676
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         910
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         916
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         922
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1146
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1188
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1189
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1203
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1204
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1207
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1209
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1210
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1213
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1215
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1216
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   CARBOHYD        1387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1282..1314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1288
FT                   /note="Interchain (with C-1305)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1305
FT                   /note="Interchain (with C-1288)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1322..1484
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1392..1437
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   CONFLICT        456
FT                   /note="Q -> E (in Ref. 1; AAA49678)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1287
FT                   /note="L -> I (in Ref. 1; AAA49678)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1315
FT                   /note="D -> N (in Ref. 1; AAA49678)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1486 AA;  142263 MW;  02C18E5F5807100E CRC64;
     MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLDTGSCVQ HGQRYSDKDV WKPEPCQICV
     CDTGTVLCDD IICEESKDCP NAEIPFGECC PICPTEQSST SSGQGVLKGQ KGEPGDIKDV
     LGPRGPPGPQ GPSGEQGSRG ERGDKGEKGA PGPRGRDGEP GTPGNPGPVG PPGPPGLGGN
     FAAQMTGGFD EKAGGAQMGV MQGPMGPMGP RGPPGPTGAP GPQGFQGNPG EPGEPGAGGP
     MGPRGPPGPS GKPGDDGEAG KPGKSGERGP PGPQGARGFP GTPGLPGVKG HRGYPGLDGA
     KGEAGAAGAK GEGGATGEAG SPGPMGPRGL PGERGRPGSS GAAGARGNDG LPGPAGPPGP
     VGPAGAPGFP GAPGSKGEAG PTGARGPEGA QGPRGESGTP GSPGPAGASG NPGTDGIPGA
     KGSSGGPGIA GAPGFPGPRG PPGPQGATGP LGPKGQTGDP GVAGFKGEQG PKGEIGSAGP
     QGAPGPAGEE GKRGARGEPG AAGPNGPPGE RGAPGNRGFP GQDGLAGPKG APGERGVPGL
     GGPKGGNGDP GRPGEPGLPG ARGLTGRPGD AGPQGKVGPS GASGEDGRPG PPGPQGARGQ
     PGVMGFPGPK GANGEPGKAG EKGLVGAPGL RGLPGKDGET GSQGPNGPAG PAGERGEQGP
     PGPSGFQGLP GPPGSPGEGG KPGDQGVPGE AGAPGLVGPR GERGFPGERG SSGPQGLQGP
     RGLPGTPGTD GPKGASGPSG PNGAQGPPGL QGMPGERGAA GISGPKGDRG DTGEKGPEGA
     SGKDGSRGLT GPIGPPGPAG PNGEKGESGP SGPPGIVGAR GAPGDRGENG PPGPAGFAGP
     PGADGQSGLK GDQGESGQKG DAGAPGPQGP SGAPGPQGPT GVFGPKGARG AQGPAGATGF
     PGAAGRVGTP GPNGNPGPPG PPGSAGKEGP KGVRGDAGPP GRAGDPGLQG AAGAPGEKGE
     PGEDGPSGPD GPPGPQGLSG QRGIVGLPGQ RGERGFPGLP GPSGEPGKQG GPGSSGDRGP
     PGPVGPPGLT GPSGEPGREG NPGSDGPPGR DGATGIKGDR GETGPLGAPG APGAPGAPGS
     VGPTGKQGDR GESGPQGPLG PSGPAGARGL AGPQGPRGDK GEAGEAGERG QKGHRGFTGL
     QGLPGPPGSA GDQGATGPAG PAGPRGPPGP VGPSGKDGSN GISGPIGPPG PRGRSGETGP
     SGPPGQPGPP GPPGPPGPGI DMSAFAGLSQ PEKGPDPMRY MRADQASNSL PVDVEATLKS
     LNNQIENIRS PDGTKKNPAR TCRDLKLCHP EWKSGDYWID PNQGCTVDAI KVFCDMETGE
     TCVYPNPSKI PKKNWWSAKG KEKKHIWFGE TINGGFQFSY GDDSSAPNTA NIQMTFLRLL
     STDASQNITY HCKNSIAFMD EASGNLKKAV LLQGSNDVEI RAEGNSRFTY NALEDGCKKH
     TGKWSKTVIE YRTQKTSRLP IVDIAPMDIG GADQEFGVDI GPVCFL
//