COAA1_CHICK
ID COAA1_CHICK Reviewed; 674 AA.
AC P08125;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Collagen alpha-1(X) chain;
DE Flags: Precursor;
GN Name=COL10A1;
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 [GENOMIC DNA] OF 48-674, PROTEIN SEQUENCE OF 103-117
RP AND 453-466, AND HYDROXYLATION AT PRO-453 AND PRO-456.
RX PubMed=3082876; DOI=10.1016/s0021-9258(19)89212-8;
RA Ninomiya Y., Gordon M., van der Rest M., Schmid T., Linsenmayer T.,
RA Olsen B.R.;
RT "The developmentally regulated type X collagen gene contains a long open
RT reading frame without introns.";
RL J. Biol. Chem. 261:5041-5050(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RX PubMed=2461368; DOI=10.1016/s0021-9258(19)81370-4;
RA LuValle P., Ninomiya Y., Rosenblum N.D., Olsen B.R.;
RT "The type X collagen gene. Intron sequences split the 5'-untranslated
RT region and separate the coding regions for the non-collagenous amino-
RT terminal and triple-helical domains.";
RL J. Biol. Chem. 263:18378-18385(1988).
RN [3]
RP PROTEIN SEQUENCE OF 19-34.
RX PubMed=2826450; DOI=10.1016/s0021-9258(19)57431-2;
RA Summers T.A., Irwin M.H., Mayne R., Balian G.;
RT "Monoclonal antibodies to type X collagen. Biosynthetic studies using an
RT antibody to the amino-terminal domain.";
RL J. Biol. Chem. 263:581-587(1988).
RN [4]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=2476437; DOI=10.1016/s0021-9258(18)71582-2;
RA Yamaguchi N., Benya P.D., van der Rest M., Ninomiya Y.;
RT "The cloning and sequencing of alpha 1(VIII) collagen cDNAs demonstrate
RT that type VIII collagen is a short chain collagen and contains triple-
RT helical and carboxyl-terminal non-triple-helical domains similar to those
RT of type X collagen.";
RL J. Biol. Chem. 264:16022-16029(1989).
CC -!- FUNCTION: Type X collagen is a product of hypertrophic chondrocytes and
CC has been localized to presumptive mineralization zones of hyaline
CC cartilage.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC {ECO:0000269|PubMed:3082876}.
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DR EMBL; M13496; AAA48736.1; ALT_SEQ; Genomic_DNA.
DR EMBL; J04194; AAA48634.1; -; Genomic_DNA.
DR PIR; S23297; S23297.
DR AlphaFoldDB; P08125; -.
DR SMR; P08125; -.
DR STRING; 9031.ENSGALP00000024087; -.
DR PaxDb; P08125; -.
DR PRIDE; P08125; -.
DR VEuPathDB; HostDB:geneid_100858979; -.
DR eggNOG; ENOG502QS5V; Eukaryota.
DR InParanoid; P08125; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; P08125; -.
DR PRO; PR:P08125; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 4.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; Direct protein sequencing; Extracellular matrix;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2826450"
FT CHAIN 19..674
FT /note="Collagen alpha-1(X) chain"
FT /id="PRO_0000005769"
FT DOMAIN 541..674
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 19..52
FT /note="Nonhelical region (NC2)"
FT REGION 49..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..512
FT /note="Triple-helical region"
FT REGION 513..674
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 56..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 620
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT MOD_RES 453
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3082876"
FT MOD_RES 456
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3082876"
FT CONFLICT 25
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 674 AA; 66433 MW; EAB48B1EF174B145 CRC64;
MHLQISLLLL FCLNIVHGSD GYFSERYQKQ SSIKGPPHFL PFNVKSQGVQ MRGEQGPPGP
PGPIGPRGQP GPAGKPGFGS PGPQGPPGPL GPPGFSTVGK LGMPGLPGKP GERGLNGEKG
EAGPVGLPGA RGPQGPPGIP GPAGLSVLGK PGPQGPPGAQ GPRGPPGEKG EPGVPGINGQ
KGEMGFGVPG RPGNRGLPGP QGPQGLPGSA GIGKPGENGL PGQPGMKGDR GLPGARGEAG
IPGPQGPPGE PGEVGIGKPG PMGPPGPAGI PGAKGLPGPA GLPGSPGLPG FGKPGLPGMK
GHRGPEGPPG FPGPKGDQGP AGVPGELGPA GPQGNMGPQG LKGLPGENGL PGPKGDMGPV
GPAGFPGAKG ERGLPGLDGK PGYPGEQGLP GPKGHPGLPG QKGDTGHAGH PGLPGPVGPQ
GVKGVPGING EPGPRGPSGI PGVRGPIGPP GMPGAPGAKG EAGAPGLPGP AGIVTKGLRG
PMGPLGPPGP KGNSGEPGLP GPPGPPGPPG QSTIPEGYVK GESRELSGMS FMKAGANQAL
TGMPVSAFTV ILSKAYPGAT VPIKFDKILY NRQQHYDPRT GIFTCRIPGL YYFSYHVHAK
GTNVWVALYK NGSPVMYTYD EYQKGYLDQA SGSAVIDLME NDQVWLQLPN SESNGLYSSE
YVHSSFSGFL FAQI
