COAA1_BOVIN
ID COAA1_BOVIN Reviewed; 674 AA.
AC P23206;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Collagen alpha-1(X) chain;
DE Flags: Precursor;
GN Name=COL10A1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cartilage;
RX PubMed=1703407; DOI=10.1042/bj2730141;
RA Thomas J.T., Kwan A.P.L., Grant M.E., Boot-Handford R.P.;
RT "Isolation of cDNAs encoding the complete sequence of bovine type X
RT collagen. Evidence for the condensed nature of mammalian type X collagen
RT genes.";
RL Biochem. J. 273:141-148(1991).
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: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
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; X53556; CAA37624.1; -; mRNA.
DR PIR; S13301; S13301.
DR RefSeq; NP_777059.1; NM_174634.1.
DR AlphaFoldDB; P23206; -.
DR SMR; P23206; -.
DR STRING; 9913.ENSBTAP00000004006; -.
DR PaxDb; P23206; -.
DR PRIDE; P23206; -.
DR GeneID; 282416; -.
DR KEGG; bta:282416; -.
DR CTD; 1300; -.
DR eggNOG; ENOG502QS5V; Eukaryota.
DR InParanoid; P23206; -.
DR OrthoDB; 1167208at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 6.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Hydroxylation;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT CHAIN 19..674
FT /note="Collagen alpha-1(X) chain"
FT /id="PRO_0000005768"
FT DOMAIN 541..674
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 19..56
FT /note="Nonhelical region (NC2)"
FT REGION 54..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..519
FT /note="Triple-helical region"
FT REGION 520..674
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 63..107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..519
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 460
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 463
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 194..197
FT /evidence="ECO:0000250"
SQ SEQUENCE 674 AA; 65546 MW; CD4CA73A03E004CA CRC64;
MLPQTALLLL MSLNLVHGVF YTERYQTPTG IKGPPSNTKT QFFIPYAIKG KGVSLRGEQG
IPGPPGPAGP RGHPGPSGPP GKPGTGSPGP QGQPGLPGPP GPSATGKPGL PGLPGKQGER
GLNGPKGDIG PAGLPGPRGP PGPPGIPGPA GISVPGKPGP QGPTGEPGPR GFPGEKGTSG
VPGLNGQKGE MGHCTPCRPG ERGLPGPQGP TGPPGPPGVG KRGENGLPGQ PGLKGDQGVP
GERGAAGPSG PQGPPGEQGP EGIGKPGAPG IPGQPGIPGM KGQPGAPGTA GLPGAPGFGK
PGLPGLKGQR GPVGLPGSPG AKGEQGPAGH PGEAGLPGPS GNMGPQGPKG IPGNPGLPGP
KGEMGPVGPA GNPGAKGERG SSGLDGKPGY PGEPGLNGPK GNPGLPGPKG DPGIAGSPGL
PGPVGPAGAK GVPGHNGEAG PRGVPGIPGT RGPIGPPGIP GFPGSKGDVG TPGPPGPAGI
AVKGLNGPTG PPGPPGPRGN AGEPGLPGPP GPPGPPGQVA LPEDFVKAGQ RPFVSANQGV
TGMPVSAFTV ILSKAYPAIG TPIPFDKILY NKQQHYDPRT GIFTCKIPGI YYFSYHIHVK
GTHAWVGLYK NGTPVMYTYD EYIKGYLDQA SGSAVIDLTE NDQVWLQLPN AGSNGLYSPE
YVHSSFSGFL VAPM
