CTHR1_HUMAN
ID CTHR1_HUMAN Reviewed; 243 AA.
AC Q96CG8; G3V141; Q6UW91; Q8IX63;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Collagen triple helix repeat-containing protein 1;
DE Flags: Precursor;
GN Name=CTHRC1; ORFNames=UNQ762/PRO1550;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Aorta;
RX PubMed=15618538; DOI=10.1161/01.res.0000154262.07264.12;
RA Pyagay P., Heroult M., Wang Q., Lehnert W., Belden J., Liaw L.,
RA Friesel R.E., Lindner V.;
RT "Collagen triple helix repeat containing 1, a novel secreted protein in
RT injured and diseased arteries, inhibits collagen expression and promotes
RT cell migration.";
RL Circ. Res. 96:261-268(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Sanuki N., Fujiki K., Kanai A., Tanaka Y., Iwata T.;
RT "Novel polypeptide found in human cornea cDNA library.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [7]
RP PROTEIN SEQUENCE OF 31-45 (ISOFORM 1).
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP INVOLVEMENT IN BE, AND VARIANT PRO-44.
RX PubMed=21791690; DOI=10.1001/jama.2011.1029;
RA Orloff M., Peterson C., He X., Ganapathi S., Heald B., Yang Y.R., Bebek G.,
RA Romigh T., Song J.H., Wu W., David S., Cheng Y., Meltzer S.J., Eng C.;
RT "Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with Barrett
RT esophagus and esophageal adenocarcinoma.";
RL JAMA 306:410-419(2011).
CC -!- FUNCTION: May act as a negative regulator of collagen matrix
CC deposition. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96CG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CG8-2; Sequence=VSP_013622, VSP_013623;
CC Name=3;
CC IsoId=Q96CG8-3; Sequence=VSP_013622;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in calcified atherosclerotic
CC plaque and chondrocyte-like cells. {ECO:0000269|PubMed:15618538}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Barrett esophagus (BE) [MIM:614266]: A condition characterized
CC by a metaplastic change in which normal esophageal squamous epithelium
CC is replaced by a columnar and intestinal-type epithelium. Patients with
CC Barrett esophagus have an increased risk of esophageal adenocarcinoma.
CC The main cause of Barrett esophagus is gastroesophageal reflux. The
CC retrograde movement of acid and bile salts from the stomach into the
CC esophagus causes prolonged injury to the esophageal epithelium and
CC induces chronic esophagitis, which in turn is believed to trigger the
CC pathologic changes. {ECO:0000269|PubMed:21791690}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CTHRC1ID40193ch8q22.html";
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DR EMBL; AY136825; AAN15749.1; -; mRNA.
DR EMBL; AF395488; AAO17919.1; -; mRNA.
DR EMBL; AY358914; AAQ89273.1; -; mRNA.
DR EMBL; AC012213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91876.1; -; Genomic_DNA.
DR EMBL; BC014245; AAH14245.1; -; mRNA.
DR CCDS; CCDS59110.1; -. [Q96CG8-3]
DR CCDS; CCDS6299.1; -. [Q96CG8-1]
DR RefSeq; NP_001243028.1; NM_001256099.1. [Q96CG8-3]
DR RefSeq; NP_612464.1; NM_138455.3. [Q96CG8-1]
DR AlphaFoldDB; Q96CG8; -.
DR BioGRID; 125461; 29.
DR IntAct; Q96CG8; 3.
DR STRING; 9606.ENSP00000330523; -.
DR GlyGen; Q96CG8; 1 site.
DR iPTMnet; Q96CG8; -.
DR PhosphoSitePlus; Q96CG8; -.
DR BioMuta; CTHRC1; -.
DR DMDM; 67462315; -.
DR jPOST; Q96CG8; -.
DR MassIVE; Q96CG8; -.
DR MaxQB; Q96CG8; -.
DR PaxDb; Q96CG8; -.
DR PeptideAtlas; Q96CG8; -.
DR PRIDE; Q96CG8; -.
DR ProteomicsDB; 32251; -.
DR ProteomicsDB; 76186; -. [Q96CG8-1]
DR ProteomicsDB; 76187; -. [Q96CG8-2]
DR Antibodypedia; 26375; 329 antibodies from 36 providers.
DR DNASU; 115908; -.
DR Ensembl; ENST00000330295.10; ENSP00000330523.5; ENSG00000164932.13. [Q96CG8-1]
DR Ensembl; ENST00000520337.1; ENSP00000430550.1; ENSG00000164932.13. [Q96CG8-3]
DR GeneID; 115908; -.
DR KEGG; hsa:115908; -.
DR MANE-Select; ENST00000330295.10; ENSP00000330523.5; NM_138455.4; NP_612464.1.
DR UCSC; uc003ylk.5; human. [Q96CG8-1]
DR CTD; 115908; -.
DR DisGeNET; 115908; -.
DR GeneCards; CTHRC1; -.
DR HGNC; HGNC:18831; CTHRC1.
DR HPA; ENSG00000164932; Tissue enhanced (gallbladder, placenta, urinary bladder).
DR MalaCards; CTHRC1; -.
DR MIM; 610635; gene.
DR MIM; 614266; phenotype.
DR neXtProt; NX_Q96CG8; -.
DR OpenTargets; ENSG00000164932; -.
DR PharmGKB; PA38701; -.
DR VEuPathDB; HostDB:ENSG00000164932; -.
DR eggNOG; ENOG502QSJD; Eukaryota.
DR GeneTree; ENSGT00390000018094; -.
DR HOGENOM; CLU_099891_0_0_1; -.
DR InParanoid; Q96CG8; -.
DR OMA; CADYPKG; -.
DR OrthoDB; 1198971at2759; -.
DR PhylomeDB; Q96CG8; -.
DR TreeFam; TF328705; -.
DR PathwayCommons; Q96CG8; -.
DR SignaLink; Q96CG8; -.
DR BioGRID-ORCS; 115908; 11 hits in 1067 CRISPR screens.
DR GenomeRNAi; 115908; -.
DR Pharos; Q96CG8; Tbio.
DR PRO; PR:Q96CG8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96CG8; protein.
DR Bgee; ENSG00000164932; Expressed in tibia and 162 other tissues.
DR ExpressionAtlas; Q96CG8; baseline and differential.
DR Genevisible; Q96CG8; HS.
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; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0090177; P:establishment of planar polarity involved in neural tube closure; IEA:Ensembl.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0043932; P:ossification involved in bone remodeling; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
PE 1: Evidence at protein level;
KW Alternative splicing; Collagen; Direct protein sequencing;
KW Extracellular matrix; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT CHAIN 31..243
FT /note="Collagen triple helix repeat-containing protein 1"
FT /id="PRO_0000021038"
FT DOMAIN 57..90
FT /note="Collagen-like"
FT REGION 62..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..50
FT /note="MRPQGPAASPQRLRGLLLLLLLQLPAPSSASEIPKGKQKAQLRQREVVDL
FT -> MWPPGRSITVKLREKTVSRKLEMNGPSAFQGLICGK (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_013622"
FT VAR_SEQ 243
FT /note="K -> IYML (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_013623"
FT VARIANT 44
FT /note="Q -> P (found in patients with Barrett esophagus;
FT dbSNP:rs387907029)"
FT /evidence="ECO:0000269|PubMed:21791690"
FT /id="VAR_066589"
FT CONFLICT 73
FT /note="G -> V (in Ref. 3; AAQ89273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 243 AA; 26224 MW; A11FFEB1C66867F9 CRC64;
MRPQGPAASP QRLRGLLLLL LLQLPAPSSA SEIPKGKQKA QLRQREVVDL YNGMCLQGPA
GVPGRDGSPG ANGIPGTPGI PGRDGFKGEK GECLRESFEE SWTPNYKQCS WSSLNYGIDL
GKIAECTFTK MRSNSALRVL FSGSLRLKCR NACCQRWYFT FNGAECSGPL PIEAIIYLDQ
GSPEMNSTIN IHRTSSVEGL CEGIGAGLVD VAIWVGTCSD YPKGDASTGW NSVSRIIIEE
LPK
