ID   CCN5_RAT                Reviewed;         250 AA.
AC   Q9JHC6;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-NOV-2023, entry version 119.
DE   RecName: Full=CCN family member 5 {ECO:0000305};
DE   AltName: Full=CCN family protein COP-1;
DE   AltName: Full=Connective tissue growth factor-like protein;
DE            Short=CTGF-L;
DE   AltName: Full=WNT1-inducible-signaling pathway protein 2;
DE            Short=WISP-2;
DE   Flags: Precursor;
GN   Name=Ccn5; Synonyms=Cop1, Ctgfl, Wisp2;
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].
RX   PubMed=9742130; DOI=10.1128/mcb.18.10.6131;
RA   Zhang R., Averboukh L., Zhu W., Zhang H., Jo H., Dempsey P.J., Coffey R.J.,
RA   Pardee A.B., Liang P.;
RT   "Identification of rCop-1, a new member of the CCN protein family, as a
RT   negative regulator for cell transformation.";
RL   Mol. Cell. Biol. 18:6131-6141(1998).
CC   -!- FUNCTION: May play an important role in modulating bone turnover.
CC       Promotes the adhesion of osteoblast cells and inhibits the binding of
CC       fibrinogen to integrin receptors. In addition, inhibits osteocalcin
CC       production (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR   EMBL; AF259981; AAF69011.1; -; mRNA.
DR   RefSeq; NP_113778.1; NM_031590.1.
DR   AlphaFoldDB; Q9JHC6; -.
DR   SMR; Q9JHC6; -.
DR   STRING; 10116.ENSRNOP00000014346; -.
DR   GlyCosmos; Q9JHC6; 1 site, No reported glycans.
DR   GlyGen; Q9JHC6; 1 site.
DR   PaxDb; 10116-ENSRNOP00000014346; -.
DR   GeneID; 29576; -.
DR   KEGG; rno:29576; -.
DR   UCSC; RGD:621867; rat.
DR   AGR; RGD:621867; -.
DR   CTD; 8839; -.
DR   RGD; 621867; Ccn5.
DR   eggNOG; ENOG502RXIT; Eukaryota.
DR   InParanoid; Q9JHC6; -.
DR   OrthoDB; 2970572at2759; -.
DR   PhylomeDB; Q9JHC6; -.
DR   PRO; PR:Q9JHC6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0002102; C:podosome; IDA:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR   InterPro; IPR043973; TSP1_CCN.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11348:SF22; CCN FAMILY MEMBER 5; 1.
DR   PANTHER; PTHR11348; CONNECTIVE TISSUE GROWTH FACTOR-RELATED; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF19035; TSP1_CCN; 1.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR   PROSITE; PS00222; IGFBP_N_1; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS50092; TSP1; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..250
FT                   /note="CCN family member 5"
FT                   /id="PRO_0000014411"
FT   DOMAIN          24..103
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          98..164
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          194..238
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        26..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        32..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        39..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        64..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        70..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
SQ   SEQUENCE   250 AA;  27005 MW;  9A147074626BCA47 CRC64;
     MRGSPLIRLL ATSFLCLLSM VCAQLCRTPC TCPWTPPQCP QGVPLVLDGC GCCKVCARRL
     TESCEHLHVC EPSQGLVCQP GAGPGGHGAV CLLDEDDGDC EVNGRRYLDG ETFKPNCRVL
     CRCDDGGFTC LPLCSEDVTL PSWDCPRPKR IQVPGKCCPE WVCDQGVTPA IQRSAAQGHQ
     LSALVTPASA DAPWPNWSTA WGPCSTTCGL GIATRVSNQN RFCQLEIQRR LCLPRPCLAA
     RSHSSWNSAF
//