CONA1_HUMAN
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 03-AUG-2022, entry version 157.
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; 13.
DR ComplexPortal; CPX-1764; Collagen type XXIII trimer.
DR IntAct; Q86Y22; 7.
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; Q86Y22; -.
DR PeptideAtlas; Q86Y22; -.
DR PRIDE; Q86Y22; -.
DR ProteomicsDB; 70352; -. [Q86Y22-1]
DR ProteomicsDB; 70353; -. [Q86Y22-2]
DR Antibodypedia; 29441; 155 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 CTD; 91522; -.
DR DisGeNET; 91522; -.
DR GeneCards; COL23A1; -.
DR HGNC; HGNC:22990; COL23A1.
DR HPA; ENSG00000050767; Tissue enriched (thyroid).
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; GDDGMPS; -.
DR OrthoDB; 669310at2759; -.
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 1068 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 103 other tissues.
DR ExpressionAtlas; Q86Y22; baseline and differential.
DR Genevisible; Q86Y22; HS.
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:0031012; C:extracellular matrix; IBA:GO_Central.
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 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
