CONA1_MOUSE
ID CONA1_MOUSE Reviewed; 532 AA.
AC Q8K4G2; Q5SUQ0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Collagen alpha-1(XXIII) chain;
GN Name=Col23a1;
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 [MRNA].
RC TISSUE=Cartilage;
RA Koch M., Jin W., Burgeson R.E.;
RT "Alpha 1(XXIII), a new member of the transmembrane collagens.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.
CC -!- PTM: Undergoes proteolytic cleavage by furin protease to yield a 60 kDa
CC soluble form that forms a homotrimer and exhibits a low affinity
CC interaction with heparin. {ECO:0000250}.
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DR EMBL; AF410792; AAN03649.1; -; mRNA.
DR EMBL; AL645907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24652.1; -.
DR RefSeq; NP_700442.2; NM_153393.2.
DR AlphaFoldDB; Q8K4G2; -.
DR BioGRID; 231903; 3.
DR ComplexPortal; CPX-3005; Collagen type XXIII trimer.
DR STRING; 10090.ENSMUSP00000099826; -.
DR iPTMnet; Q8K4G2; -.
DR PhosphoSitePlus; Q8K4G2; -.
DR PaxDb; Q8K4G2; -.
DR PRIDE; Q8K4G2; -.
DR ProteomicsDB; 283604; -.
DR Antibodypedia; 29441; 155 antibodies from 27 providers.
DR DNASU; 237759; -.
DR Ensembl; ENSMUST00000102765; ENSMUSP00000099826; ENSMUSG00000063564.
DR GeneID; 237759; -.
DR KEGG; mmu:237759; -.
DR UCSC; uc033fvj.1; mouse.
DR CTD; 91522; -.
DR MGI; MGI:2653243; Col23a1.
DR VEuPathDB; HostDB:ENSMUSG00000063564; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000162238; -.
DR HOGENOM; CLU_001074_21_2_1; -.
DR InParanoid; Q8K4G2; -.
DR OMA; GDDGMPS; -.
DR OrthoDB; 669310at2759; -.
DR PhylomeDB; Q8K4G2; -.
DR TreeFam; TF338175; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 237759; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8K4G2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K4G2; protein.
DR Bgee; ENSMUSG00000063564; Expressed in median eminence of neurohypophysis and 211 other tissues.
DR ExpressionAtlas; Q8K4G2; baseline and differential.
DR Genevisible; Q8K4G2; MM.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 7.
PE 2: Evidence at transcript level;
KW Cell membrane; Collagen; Membrane; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Collagen alpha-1(XXIII) chain"
FT /id="PRO_0000245227"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 108..166
FT /note="Collagen-like 1"
FT DOMAIN 173..232
FT /note="Collagen-like 2"
FT DOMAIN 240..298
FT /note="Collagen-like 3"
FT DOMAIN 313..372
FT /note="Collagen-like 4"
FT DOMAIN 404..452
FT /note="Collagen-like 5"
FT DOMAIN 455..514
FT /note="Collagen-like 6"
FT REGION 102..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 288
FT /note="A -> P (in Ref. 1; AAN03649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 51476 MW; 035E8538D5642486 CRC64;
MGAGERAAGG GGAQDPGAGC GSRALSALCL LLSVGSAAAC LLLGAQAAAL HGRVAALEQE
RELLRHAGPS GALAAWAETH LERLLREKLD GVAKLRTVRE APSECICPPG PPGRRGKPGR
RGDPGPPGQS GRDGYPGPLG LDGKPGLPGP KGEKGTPGDF GPRGAQGQDG VAGPPGPPGP
PGARGPPGDT GKDGPRGAQG PAGPRGEPGQ DGEMGPKGPP GPKGEPGIPG KKGDDGMANQ
PGLPGPPGPK GEPGDVGPRG ENGVDGIPGL KGEPGHPGVD GATGPRGAPG LKGEQGDTVV
IDYDGRILDA LKGPPGPQGA PGPPGIPGAK GELGLPGAPG IDGEKGPKGP KGDPGEPGPA
GPKGETGEMG LSGLPGADGP KGEKGESASD HLQESLAQII VEPGPPGPPG PPGPMGLQGI
QGPKGLDGAK GEKGTSGERG PHGLPGPVGP PGLIGLPGTK GEKGRPGEPG LDGFPGPRGE
KGDRSERGEK GERGVPGRKG VKGQKGEPGP PGLDQPCPVG PDGLPVPGCW HK
