ID   CTHR1_RAT               Reviewed;         245 AA.
AC   Q8CG08;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Collagen triple helix repeat-containing protein 1;
DE   Flags: Precursor;
GN   Name=Cthrc1;
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], POSSIBLE FUNCTION, GLYCOSYLATION, INDUCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Carotid artery;
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).
CC   -!- FUNCTION: Its overexpression in smooth muscle cell lines increases
CC       their migratory ability and inhibits collagen type I expression. May
CC       act as a negative regulator of collagen matrix deposition.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:15618538}.
CC   -!- TISSUE SPECIFICITY: Expressed after injury in the carotid arteries (at
CC       protein level). Expressed in brain, lung, and after injury in
CC       fibroblasts of the adventitia and the neointima of the arteries.
CC       {ECO:0000269|PubMed:15618538}.
CC   -!- INDUCTION: Strongly induced in carotid arteries after injury (balloon
CC       catheter injury model). By various growth factor (BMP4, TGFB1) in NIH
CC       3T3 cell line. {ECO:0000269|PubMed:15618538}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15618538}.
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DR   EMBL; AY136824; AAN15748.1; -; mRNA.
DR   RefSeq; NP_758836.1; NM_172333.2.
DR   AlphaFoldDB; Q8CG08; -.
DR   STRING; 10116.ENSRNOP00000006142; -.
DR   GlyGen; Q8CG08; 1 site.
DR   PhosphoSitePlus; Q8CG08; -.
DR   PaxDb; Q8CG08; -.
DR   PRIDE; Q8CG08; -.
DR   GeneID; 282836; -.
DR   KEGG; rno:282836; -.
DR   UCSC; RGD:628801; rat.
DR   CTD; 115908; -.
DR   RGD; 628801; Cthrc1.
DR   VEuPathDB; HostDB:ENSRNOG00000004578; -.
DR   eggNOG; ENOG502QSJD; Eukaryota.
DR   HOGENOM; CLU_099891_0_0_1; -.
DR   InParanoid; Q8CG08; -.
DR   OMA; CADYPKG; -.
DR   OrthoDB; 1198971at2759; -.
DR   PhylomeDB; Q8CG08; -.
DR   TreeFam; TF328705; -.
DR   PRO; PR:Q8CG08; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000004578; Expressed in quadriceps femoris and 16 other tissues.
DR   Genevisible; Q8CG08; RN.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR   GO; GO:0005109; F:frizzled binding; ISO:RGD.
DR   GO; GO:0017147; F:Wnt-protein binding; ISO:RGD.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0090103; P:cochlea morphogenesis; ISO:RGD.
DR   GO; GO:0090177; P:establishment of planar polarity involved in neural tube closure; ISO:RGD.
DR   GO; GO:0060122; P:inner ear receptor cell stereocilium organization; ISO:RGD.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0043932; P:ossification involved in bone remodeling; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISO:RGD.
DR   GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISO:RGD.
PE   1: Evidence at protein level;
KW   Collagen; Extracellular matrix; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..245
FT                   /note="Collagen triple helix repeat-containing protein 1"
FT                   /id="PRO_0000021040"
FT   DOMAIN          59..92
FT                   /note="Collagen-like"
FT   REGION          64..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   245 AA;  26424 MW;  2296FD6DCDBA21F2 CRC64;
     MHPQGRAASP QLLLGLFLVL LLLLQLSAPS SASENPKVKQ KALIRQREVV DLYNGMCLQG
     PAGVPGRDGS PGANGIPGTP GIPGRDGFKG EKGECLRESF EESWTPNYKQ CSWSSLNYGI
     DLGKIAECTF TKMRSNSALR VLFSGSLRLK CRNACCQRWY FTFNGAECSG PLPIEAIIYL
     DQGSPELNST INIHRTSSVE GLCEGIGAGL VDVAIWVGTC SDYPKGDAST GWNSVSRIII
     EELPK