COAA1_MOUSE
ID COAA1_MOUSE Reviewed; 680 AA.
AC Q05306;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Collagen alpha-1(X) chain;
DE Flags: Precursor;
GN Name=Col10a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=8424763; DOI=10.1042/bj2890247;
RA Elima K., Eerola I., Rosati R., Metsaranta M., Garofalo S., Perala M.,
RA de Crombrugghe B., Vuorio E.;
RT "The mouse collagen X gene: complete nucleotide sequence, exon structure
RT and expression pattern.";
RL Biochem. J. 289:247-253(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=8477738; DOI=10.1111/j.1432-1033.1993.tb17739.x;
RA Kong R.Y.C., Kwan K.M., Lau E.T., Thomas J.T., Boot-Handford R.P.,
RA Grant M.E., Cheah K.S.E.;
RT "Intron-exon structure, alternative use of promoter and expression of the
RT mouse collagen X gene, Col10a-1.";
RL Eur. J. Biochem. 213:99-111(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8492743; DOI=10.1016/s0934-8832(11)80075-2;
RA Apte S.S., Olsen B.R.;
RT "Characterization of the mouse type X collagen gene.";
RL Matrix 13:165-179(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-680.
RC STRAIN=DBA/2J;
RX PubMed=1587271; DOI=10.1111/j.1432-1033.1992.tb16919.x;
RA Apte S.S., Seldin M.F., Hayashi M., Olsen B.R.;
RT "Cloning of the human and mouse type X collagen genes and mapping of the
RT mouse type X collagen gene to chromosome 10.";
RL Eur. J. Biochem. 206:217-224(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 385-627.
RC STRAIN=C57BL/6J;
RX PubMed=1543751; DOI=10.1016/0167-4781(92)90465-c;
RA Elima K., Metsaeranta M., Kallio J., Peraelae M., Eerola I., Garofalo S.,
RA de Crombrugghe B., Vuorio E.;
RT "Specific hybridization probes for mouse alpha 2(IX) and alpha 1(X)
RT collagen mRNAs.";
RL Biochim. Biophys. Acta 1130:78-80(1992).
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.
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DR EMBL; X67348; CAA47763.1; -; Genomic_DNA.
DR EMBL; Z21610; CAA79736.1; -; Genomic_DNA.
DR EMBL; X65121; CAA46237.1; -; Genomic_DNA.
DR EMBL; X63013; CAA44741.1; -; mRNA.
DR CCDS; CCDS23780.1; -.
DR PIR; S31216; S31216.
DR RefSeq; NP_034055.1; NM_009925.4.
DR AlphaFoldDB; Q05306; -.
DR SMR; Q05306; -.
DR ComplexPortal; CPX-2971; Collagen type X trimer.
DR STRING; 10090.ENSMUSP00000101150; -.
DR iPTMnet; Q05306; -.
DR PhosphoSitePlus; Q05306; -.
DR MaxQB; Q05306; -.
DR PaxDb; Q05306; -.
DR PRIDE; Q05306; -.
DR ProteomicsDB; 277991; -.
DR DNASU; 12813; -.
DR Ensembl; ENSMUST00000105511; ENSMUSP00000101150; ENSMUSG00000039462.
DR GeneID; 12813; -.
DR KEGG; mmu:12813; -.
DR UCSC; uc011xcr.1; mouse.
DR CTD; 1300; -.
DR MGI; MGI:88445; Col10a1.
DR VEuPathDB; HostDB:ENSMUSG00000039462; -.
DR eggNOG; ENOG502QS5V; Eukaryota.
DR GeneTree; ENSGT00940000163953; -.
DR HOGENOM; CLU_001074_21_0_1; -.
DR InParanoid; Q05306; -.
DR OMA; DEYIKGY; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; Q05306; -.
DR TreeFam; TF334029; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12813; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q05306; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q05306; protein.
DR Bgee; ENSMUSG00000039462; Expressed in humerus and 73 other tissues.
DR Genevisible; Q05306; MM.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005599; C:collagen type X trimer; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO: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:0051216; P:cartilage development; ISO:MGI.
DR GO; GO:0001958; P:endochondral ossification; ISO:MGI.
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 2: Evidence at transcript level;
KW Calcium; Collagen; Extracellular matrix; Hydroxylation; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..680
FT /note="Collagen alpha-1(X) chain"
FT /id="PRO_0000005771"
FT DOMAIN 547..680
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 19..56
FT /note="Nonhelical region (NC2)"
FT REGION 54..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..519
FT /note="Triple-helical region"
FT REGION 520..680
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 60..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..151
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 626
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 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 634
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 634
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 CONFLICT 13
FT /note="L -> F (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="T -> S (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="P -> L (in Ref. 3; no nucleotide entry and 4;
FT CAA46237)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> S (in Ref. 2; CAA79736)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> F (in Ref. 3; no nucleotide entry and 4;
FT CAA46237)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="T -> S (in Ref. 3; no nucleotide entry and 4;
FT CAA46237)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="R -> K (in Ref. 5; CAA44741)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="H -> L (in Ref. 3; no nucleotide entry and 4;
FT CAA46237)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..572
FT /note="APIPFD -> CPHPIY (in Ref. 3; no nucleotide entry and
FT 4; CAA46237)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="Q -> T (in Ref. 3; no nucleotide entry and 4;
FT CAA46237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 66775 MW; FE984CA99AF708E2 CRC64;
MLPQIPFLLL MFLTLVHGMF YAERYQTPTG IKGPLASPKT QYFIPYAIKS KGIPVRGEQG
IPGPPGPTGP RGHPGPSGPP GKPGYGSPGL QGEPGLPGPP GISATGKPGL PGPPGKPGER
GPYGHKGDIG PAGLPGPRGP PGPPGIPGPA GISVPGKPGQ QGLTGAPGPR GFPGEKGAQG
APGVNGRKGE TGYGSPGRPG ERGLPGPQGP IGPPGPSGVG RRGENGFPGQ PGIKGDRGFP
GEMGPSGPPG PQGPPGKQGR EGIGKPGAIG SPGQPGIPGE KGHPGAPGIA GPPGAPGFGK
QGLPGLRGQR GPAGLPGAPG AKGERGPAGH PGEPGLPGSP GNMGPQGPKG IPGNHGIPGA
KGEIGLVGPA GPPGARGARG PPGLDGKTGY PGEPGLNGPK GNPGLPGQKG DPGVGGTPGL
RGPVGPVGAK GVPGHNGEAG PRGEPGIPGT RGPTGPPGVP GFPGSKGDPG NPGAPGPAGI
ATKGLNGPTG PPGPPGPRGH SGEPGLPGPP GPPGPPGQAV MPDGFIKAGQ RPRLSGMPLV
SANHGVTGMP VSAFTVILSK AYPAVGAPIP FDEILYNRQQ HYDPRSGIFT CKIPGIYYFS
YHVHVKGTHV WVGLYKNGTP TMYTYDEYSK GYLDQASGSA IMELTENDQV WLQLPNAESN
GLYSSEYVHS SFSGFLVAPM
