CO2A1_CHICK
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 03-AUG-2022, entry version 141.
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}.
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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.ENSGALP00000035064; -.
DR PaxDb; P02460; -.
DR PRIDE; P02460; -.
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; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
DR GO; GO:0005585; C:collagen type II trimer; IPI:ComplexPortal.
DR GO; GO:0031012; C:extracellular matrix; EXP:ComplexPortal.
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; EXP:ComplexPortal.
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 Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 3.
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
