ID   CONA1_HUMAN             Reviewed;         540 AA.
AC   Q86Y22; Q8IVR4; Q9NT93;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Collagen alpha-1(XXIII) chain;
GN   Name=COL23A1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RA   Koch M., Burgeson R.E., Gordon M.K.;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-540.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q86Y22; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-373279, EBI-371922;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86Y22-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86Y22-2; Sequence=VSP_019627, VSP_019628, VSP_019629,
CC                                  VSP_019630, VSP_019631;
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; AY158895; AAO18361.1; -; mRNA.
DR   EMBL; AY898961; AAX84028.1; -; mRNA.
DR   EMBL; BC042428; AAH42428.1; -; mRNA.
DR   EMBL; AL137461; CAB70749.1; -; mRNA.
DR   CCDS; CCDS4436.1; -. [Q86Y22-1]
DR   PIR; T46404; T46404.
DR   RefSeq; NP_775736.2; NM_173465.3. [Q86Y22-1]
DR   AlphaFoldDB; Q86Y22; -.
DR   BioGRID; 124839; 14.
DR   ComplexPortal; CPX-1764; Collagen type XXIII trimer.
DR   IntAct; Q86Y22; 8.
DR   MINT; Q86Y22; -.
DR   STRING; 9606.ENSP00000375069; -.
DR   GlyGen; Q86Y22; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86Y22; -.
DR   PhosphoSitePlus; Q86Y22; -.
DR   BioMuta; COL23A1; -.
DR   DMDM; 74723551; -.
DR   EPD; Q86Y22; -.
DR   MassIVE; Q86Y22; -.
DR   PaxDb; 9606-ENSP00000375069; -.
DR   PeptideAtlas; Q86Y22; -.
DR   ProteomicsDB; 70352; -. [Q86Y22-1]
DR   ProteomicsDB; 70353; -. [Q86Y22-2]
DR   Antibodypedia; 29441; 164 antibodies from 27 providers.
DR   DNASU; 91522; -.
DR   Ensembl; ENST00000390654.8; ENSP00000375069.3; ENSG00000050767.18. [Q86Y22-1]
DR   GeneID; 91522; -.
DR   KEGG; hsa:91522; -.
DR   MANE-Select; ENST00000390654.8; ENSP00000375069.3; NM_173465.4; NP_775736.2.
DR   UCSC; uc063kkp.1; human. [Q86Y22-1]
DR   AGR; HGNC:22990; -.
DR   CTD; 91522; -.
DR   DisGeNET; 91522; -.
DR   GeneCards; COL23A1; -.
DR   HGNC; HGNC:22990; COL23A1.
DR   HPA; ENSG00000050767; Group enriched (heart muscle, thyroid gland).
DR   MIM; 610043; gene.
DR   neXtProt; NX_Q86Y22; -.
DR   OpenTargets; ENSG00000050767; -.
DR   PharmGKB; PA134899251; -.
DR   VEuPathDB; HostDB:ENSG00000050767; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000162238; -.
DR   InParanoid; Q86Y22; -.
DR   OMA; PRMVFPH; -.
DR   OrthoDB; 5324524at2759; -.
DR   PhylomeDB; Q86Y22; -.
DR   TreeFam; TF338175; -.
DR   PathwayCommons; Q86Y22; -.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-8948216; Collagen chain trimerization.
DR   SignaLink; Q86Y22; -.
DR   BioGRID-ORCS; 91522; 11 hits in 1146 CRISPR screens.
DR   ChiTaRS; COL23A1; human.
DR   GenomeRNAi; 91522; -.
DR   Pharos; Q86Y22; Tbio.
DR   PRO; PR:Q86Y22; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q86Y22; Protein.
DR   Bgee; ENSG00000050767; Expressed in right lobe of thyroid gland and 105 other cell types or tissues.
DR   ExpressionAtlas; Q86Y22; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
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:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 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   PANTHER; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN ISOFORM X1-RELATED; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR   Pfam; PF01391; Collagen; 8.
DR   Genevisible; Q86Y22; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Collagen; Membrane;
KW   Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..540
FT                   /note="Collagen alpha-1(XXIII) chain"
FT                   /id="PRO_0000245226"
FT   TOPO_DOM        1..34
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..56
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..540
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          124..243
FT                   /note="Collagen-like 1"
FT   DOMAIN          251..305
FT                   /note="Collagen-like 2"
FT   DOMAIN          321..380
FT                   /note="Collagen-like 3"
FT   DOMAIN          412..460
FT                   /note="Collagen-like 4"
FT   DOMAIN          463..522
FT                   /note="Collagen-like 5"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..424
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..27
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019627"
FT   VAR_SEQ         28..98
FT                   /note="ATTAGSRAVSALCLLLSVGSAAACLLLGVQAAALQGRVAALEEERELLRRAG
FT                   PPGALDAWAEPHLERLLRE -> MESRSGIQAGVRCRDLGSLQPPPLALKQFSSLSLPS
FT                   SWDYRRLPPRCGFLFEVSETTNPPAGTNSRHTLTV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019628"
FT   VAR_SEQ         140..148
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019629"
FT   VAR_SEQ         296..345
FT                   /note="APGLKGEQGDTVVIDYDGRILDALKGPPGPQGPPGPPGIPGAKGELGLPG
FT                   -> DVRDPGLGSVSSCSQRLASSSKKNGSEPPPGCAGCPRPQGRAGRHSGDRL (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019630"
FT   VAR_SEQ         346..540
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019631"
FT   VARIANT         287
FT                   /note="T -> A (in dbSNP:rs890802)"
FT                   /id="VAR_026964"
SQ   SEQUENCE   540 AA;  51944 MW;  D64D3CA50F729297 CRC64;
     MGPGERAGGG GDAGKGNAAG GGGGGRSATT AGSRAVSALC LLLSVGSAAA CLLLGVQAAA
     LQGRVAALEE ERELLRRAGP PGALDAWAEP HLERLLREKL DGLAKIRTAR EAPSECVCPP
     GPPGRRGKPG RRGDPGPPGQ SGRDGYPGPL GLDGKPGLPG PKGEKGAPGD FGPRGDQGQD
     GAAGPPGPPG PPGARGPPGD TGKDGPRGAQ GPAGPKGEPG QDGEMGPKGP PGPKGEPGVP
     GKKGDDGTPS QPGPPGPKGE PGSMGPRGEN GVDGAPGPKG EPGHRGTDGA AGPRGAPGLK
     GEQGDTVVID YDGRILDALK GPPGPQGPPG PPGIPGAKGE LGLPGAPGID GEKGPKGQKG
     DPGEPGPAGL KGEAGEMGLS GLPGADGLKG EKGESASDSL QESLAQLIVE PGPPGPPGPP
     GPMGLQGIQG PKGLDGAKGE KGASGERGPS GLPGPVGPPG LIGLPGTKGE KGRPGEPGLD
     GFPGPRGEKG DRSERGEKGE RGVPGRKGVK GQKGEPGPPG LDQPCPVGPD GLPVPGCWHK
//