ID   CONA1_RAT               Reviewed;         532 AA.
AC   Q810Y4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Collagen alpha-1(XXIII) chain;
GN   Name=Col23a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT, AND PROTEOLYTIC
RP   PROCESSING.
RC   STRAIN=COP;
RX   PubMed=12644459; DOI=10.1074/jbc.m210616200;
RA   Banyard J., Bao L., Zetter B.R.;
RT   "Type XXIII collagen, a new transmembrane collagen identified in metastatic
RT   tumor cells.";
RL   J. Biol. Chem. 278:20989-20994(2003).
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12644459}.
CC   -!- INTERACTION:
CC       Q810Y4; Q810Y4: Col23a1; NbExp=2; IntAct=EBI-10095843, EBI-10095843;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12644459};
CC       Single-pass type II membrane protein {ECO:0000269|PubMed:12644459};
CC       Extracellular side {ECO:0000269|PubMed:12644459}.
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:0000269|PubMed:12644459}.
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DR   EMBL; AY158896; AAO18362.1; -; mRNA.
DR   RefSeq; NP_853667.1; NM_181636.2.
DR   RefSeq; XP_017453116.1; XM_017597627.1.
DR   RefSeq; XP_017459534.1; XM_017604045.1.
DR   AlphaFoldDB; Q810Y4; -.
DR   ComplexPortal; CPX-50; Collagen type XXIII trimer.
DR   STRING; 10116.ENSRNOP00000062298; -.
DR   PaxDb; Q810Y4; -.
DR   Ensembl; ENSRNOT00000064078; ENSRNOP00000062298; ENSRNOG00000003349.
DR   GeneID; 353303; -.
DR   KEGG; rno:353303; -.
DR   UCSC; RGD:727898; rat.
DR   CTD; 91522; -.
DR   RGD; 727898; Col23a1.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000162238; -.
DR   InParanoid; Q810Y4; -.
DR   OrthoDB; 669310at2759; -.
DR   PhylomeDB; Q810Y4; -.
DR   Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-RNO-8948216; Collagen chain trimerization.
DR   PRO; PR:Q810Y4; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IPI:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01391; Collagen; 6.
PE   1: Evidence at protein 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_0000245228"
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..163
FT                   /note="Collagen-like 1"
FT   DOMAIN          173..232
FT                   /note="Collagen-like 2"
FT   DOMAIN          242..297
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..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"
SQ   SEQUENCE   532 AA;  51397 MW;  061E92AA7E8B76DF CRC64;
     MGAGERAAGG GGTQDPGAGC GARALGALCL LLSVGSATAC LLLGAQAAAL HGRVAALEQE
     RELLRRAGPS GALAAWAETH LERLLREKLD GVAKLRTVRE APSECICPPG PPGRRGKPGR
     RGDPGPPGQS GRDGYPGPLG LDGKPGLPGP KGEKGAPGDF GPRGAQGQDG AAGPPGPPGP
     PGARGPPGDT GKDGPRGAQG PEGPRGESGQ DGEMGPMGPP GPKGEPGTPG KKGDDGIPSQ
     PGLPGPPGPK GEPGDVGPQG ETGVDGAPGL KGEPGHPGTD GAIGPRGPPG LKGEQGDTVV
     IDYDGRILDA LKGPPGPQGA PGPPGIPGAK GELGLPGAPG IDGEKGPKGP KGDPGEPGPA
     GPKGETGEMG LSGLPGADGP KGEKGESASD HLQESLAQII VEPGPPGPPG PPGPMGLQGI
     QGPKGLDGAK GEKGASGERG PHGLPGPVGP PGLIGLPGTK GEKGRPGEPG LDGFPGPRGE
     KGDRSERGEK GERGVPGRKG VKGQKGEPGP PGLDQPCPVG PDGLPVPGCW HK