ID CO2A1_CHICK Reviewed; 859 AA. AC P02460; A0A1D5PJB4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2017, sequence version 2. DT 24-JAN-2024, entry version 147. 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; Fragment; GN Name=COL2A1 {ECO:0000250|UniProtKB:P02458}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl; RX PubMed=15592404; DOI=10.1038/nature03154; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V., RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., RA Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide unique RT perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 491-683 (ISOFORM 1). RX PubMed=3840018; DOI=10.1042/bj2290189; RA Deak F., Argraves W.S., Kiss I., Sparks K.J., Goetinck P.F.; RT "Primary structure of the telopeptide and a portion of the helical domain RT of chicken type II procollagen as determined by DNA sequence analysis."; RL Biochem. J. 229:189-196(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 572-859 (ISOFORM 2). RX PubMed=6330084; DOI=10.1016/s0021-9258(17)42868-7; RA Sandell L.J., Prentice H.L., Kravis D., Upholt W.B.; RT "Structure and sequence of the chicken type II procollagen gene. RT Characterization of the region encoding the carboxyl-terminal telopeptide RT and propeptide."; RL J. Biol. Chem. 259:7826-7834(1984). RN [4] RP NUCLEOTIDE SEQUENCE OF 604-859. RA Ninomiya Y., Showalter A.M., van der Rest M., Seidah N.G., Chretien M., RA Olsen B.R.; RT "Structure of the carboxyl propeptide of chicken type II procollagen RT determined by DNA and protein sequence analysis."; RL Biochemistry 23:617-624(1984). 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P02460-1; Sequence=Displayed; CC Name=2; CC IsoId=P02460-2; Sequence=VSP_058908; 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 -!- MISCELLANEOUS: [Isoform 1]: Incomplete sequence. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X02663; CAA26499.1; -; mRNA. DR EMBL; L00063; AAB59967.1; -; Genomic_DNA. DR EMBL; L00061; AAB59967.1; JOINED; Genomic_DNA. DR EMBL; L00062; AAB59967.1; JOINED; Genomic_DNA. DR PIR; A02860; CGCH6C. DR PIR; S07133; S07133. DR AlphaFoldDB; P02460; -. DR ComplexPortal; CPX-960; Collagen type II trimer. DR IntAct; P02460; 1. DR STRING; 9031.ENSGALP00000052906; -. DR GlyCosmos; P02460; 1 site, No reported glycans. DR PaxDb; 9031-ENSGALP00000035064; -. DR VEuPathDB; HostDB:geneid_395069; -. DR VEuPathDB; HostDB:geneid_418752; -. DR eggNOG; KOG3544; Eukaryota. DR HOGENOM; CLU_001074_2_3_1; -. DR InParanoid; P02460; -. DR PhylomeDB; P02460; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005585; C:collagen type II trimer; IPI:ComplexPortal. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central. DR GO; GO:0031012; C:extracellular matrix; EXP:ComplexPortal. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030199; P:collagen fibril organization; EXP:ComplexPortal. DR GO; GO:0030903; P:notochord development; IBA:GO_Central. DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central. DR Gene3D; 2.60.120.1000; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR000885; Fib_collagen_C. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 7. DR SMART; SM00038; COLFI; 1. DR PROSITE; PS51461; NC1_FIB; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Calcium; Collagen; Disulfide bond; KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding; KW Reference proteome; Repeat; Secreted. FT CHAIN <1..859 FT /note="Collagen alpha-1(II) chain" FT /id="PRO_0000005727" FT PROPEP 614..859 FT /note="C-terminal propeptide" FT /id="PRO_0000005728" FT DOMAIN 625..859 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 1..607 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 491..586 FT /note="Triple-helical region" FT REGION 587..613 FT /note="Nonhelical region (C-terminal)" FT COMPBIAS 281..295 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 554..587 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 673 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 675 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 676 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 678 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 681 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT SITE 613..614 FT /note="Cleavage; by procollagen C-endopeptidase" FT MOD_RES 31 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 40 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 42 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 43 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 46 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 279 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 280 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 286 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 292 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 516 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 553 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 558 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 559 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 573 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 574 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 577 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 579 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 580 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 583 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 585 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT MOD_RES 586 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P05539" FT CARBOHYD 760 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250|UniProtKB:P02458" FT DISULFID 655..687 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 655 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 661 FT /note="Interchain (with C-678)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 678 FT /note="Interchain (with C-661)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 687 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 695..857 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 765..810 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VAR_SEQ 731..811 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_058908" FT NON_TER 1 SQ SEQUENCE 859 AA; 83228 MW; 7C8A32F0CEF64705 CRC64; LQGLPGKDGE TGAAGPLDPG PVGERGEQGA PGPSGFQGLP GPPGPPGESG KPGDQGVPGE AGAPGLVGPR GERGFPGERG SPGAQGLQGP RGLPGTPGTD GPKGATGPAG PNGAQGPPGL QGMPGERGAA GIAGPKGDRG DVGEKGPEGA PGKDGARGLT GPIGPPGPAG PNGEKGESGP PGPSGAAGAR GAPGERGEPG APGPAGFAGP PGADGQPGAK GEQGEPGQKG DAGAPGPQGP SGAPGPQGPT GVTGPKGARG AQGPPGATGF PGAAGRVGPP GPNGNPGPPG PPGSAGKDGP KGVRGDAGPP GRAGDPGLQG PAGPPGEKGE PGEDGPAGPD GPPGPQGLAG QRGIVGLPGQ RGERGFPGLP GPSGEPGKQG APGSAGDRGP PGPVGPPGLT GPAGEPGREG NPGADGPPGR DGAAGVKGDR GETGPVGAPG APGAPGAPGP VGPTGKQGDR GETGAQGPMG PSGPAGARGM PGPQGPRGDK GETGEAGERG LKGHRGFTGL QGLPGPPGPS GDQGAAGPAG PSGPRGPPGP VGPSGKDGSN GMPGPIGPPG PRGRSGEPGP AGPPGNPGPP GPPGPPGTGI DMSAFAGLGQ TEKGPDPIRY MRADEAAGGL RQHDVEVDAT LKSLNNQIES IRSPEGSKKN PARTCRDIKL CHPEWKSGDY WIDPNQGCTL DAIKVFCNME TGETCVYPTP SSIPRKNWWT SKTKDKKHVW FAETINGGFH FSYGDENLSP NTASIQMTFL RLLSTEGSQN VTYHCKNSIA YMDEETGNLK KAILIQGSND VEIRAEGNSR FTYSVLEDGC TKHTGKWGKT VIEYRSQKTS RLPIVDIAPM DIGGADQEFG VDIGPVCFL //