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 27-MAR-2024, entry version 144. 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}. 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; 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 SMR; 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; 10090-ENSMUSP00000099826; -. DR ProteomicsDB; 283604; -. DR Antibodypedia; 29441; 164 antibodies from 27 providers. DR DNASU; 237759; -. DR Ensembl; ENSMUST00000102765.9; ENSMUSP00000099826.3; ENSMUSG00000063564.14. DR GeneID; 237759; -. DR KEGG; mmu:237759; -. DR UCSC; uc033fvj.1; mouse. DR AGR; MGI:2653243; -. 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; PRMVFPH; -. DR OrthoDB; 5324524at2759; -. 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 76 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 214 other cell types or tissues. DR ExpressionAtlas; Q8K4G2; baseline and differential. DR GO; GO:0005604; C:basement membrane; IBA:GO_Central. DR GO; GO:0009986; C:cell surface; ISO:MGI. 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:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0008201; F:heparin binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR InterPro; IPR008160; Collagen. DR PANTHER; PTHR37456:SF5; -; 1. DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1. DR Pfam; PF01391; Collagen; 6. DR Genevisible; Q8K4G2; MM. 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 //