ID   CCN4_RAT                Reviewed;         367 AA.
AC   Q99PP0; Q9WUW4;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=CCN family member 4 {ECO:0000305};
DE   AltName: Full=ELM-1;
DE   AltName: Full=WNT1-inducible-signaling pathway protein 1;
DE            Short=WISP-1;
DE   Flags: Precursor;
GN   Name=Ccn4; Synonyms=Elm1, Wisp1;
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].
RC   TISSUE=Hair follicle dermal papilla;
RX   PubMed=11031104; DOI=10.1006/geno.2000.6300;
RA   Sleeman M.A., Murison J.G., Strachan L., Kumble K.D., Glenn M.P.,
RA   McGrath A., Bickerstaff P., Grierson A., Havukkala I., Tan P., Watson J.D.;
RT   "Gene expression in rat dermal papilla cells: analysis of 2529 ESTs.";
RL   Genomics 69:214-224(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-74.
RA   Jia J.D., Bauer M., Schuppan D.;
RT   "Partial cDNA-sequence of rat ELM1.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Downstream regulator in the Wnt/Frizzled-signaling pathway
CC       (By similarity). Associated with cell survival. Adheres to skin and
CC       melanoma fibroblasts (By similarity). In vitro binding to skin
CC       fibroblasts occurs through the proteoglycans, decorin and biglycan (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR   EMBL; AF228049; AAK00729.1; -; mRNA.
DR   EMBL; AJ236871; CAB41995.1; -; mRNA.
DR   RefSeq; NP_113904.1; NM_031716.1.
DR   AlphaFoldDB; Q99PP0; -.
DR   SMR; Q99PP0; -.
DR   STRING; 10116.ENSRNOP00000009673; -.
DR   GlyCosmos; Q99PP0; 4 sites, No reported glycans.
DR   GlyGen; Q99PP0; 4 sites.
DR   PhosphoSitePlus; Q99PP0; -.
DR   PaxDb; 10116-ENSRNOP00000009673; -.
DR   GeneID; 65154; -.
DR   KEGG; rno:65154; -.
DR   UCSC; RGD:69431; rat.
DR   AGR; RGD:69431; -.
DR   CTD; 8840; -.
DR   RGD; 69431; Ccn4.
DR   eggNOG; ENOG502QQQQ; Eukaryota.
DR   InParanoid; Q99PP0; -.
DR   OrthoDB; 2970572at2759; -.
DR   PhylomeDB; Q99PP0; -.
DR   PRO; PR:Q99PP0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0060348; P:bone development; ISO:RGD.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISO:RGD.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR   GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR   GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:UniProtKB.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR   GO; GO:0001817; P:regulation of cytokine production; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; IPR006207; Cys_knot_C.
DR   InterPro; IPR006208; Glyco_hormone_CN.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR012395; IGFBP_CNN.
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:SF4; CCN FAMILY MEMBER 4; 1.
DR   PANTHER; PTHR11348; CONNECTIVE TISSUE GROWTH FACTOR-RELATED; 1.
DR   Pfam; PF00007; Cys_knot; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF19035; TSP1_CCN; 1.
DR   Pfam; PF00093; VWC; 1.
DR   PIRSF; PIRSF036495; IGFBP_rP_CNN; 1.
DR   SMART; SM00041; CT; 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; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 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; Proto-oncogene;
KW   Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..367
FT                   /note="CCN family member 4"
FT                   /id="PRO_0000014408"
FT   DOMAIN          45..118
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          121..186
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          215..260
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          273..347
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        53..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        55..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        62..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        87..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        93..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        273..310
FT                   /evidence="ECO:0000250"
FT   DISULFID        290..324
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        304..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        309..346
FT                   /evidence="ECO:0000250"
FT   CONFLICT        17
FT                   /note="V -> L (in Ref. 2; CAB41995)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  40614 MW;  8A4A34C69D3243D2 CRC64;
     MRWLLPWTLA AVAVLMVGNI LATALSPTPT TMTFTPAPLE ETITRPEFCK WPCECPQAPP
     RCPLGVSLIT DGCECCKICA QQLGDNCTEA AVCDPHRGLY CDYSGDRPRY AIGVCAQVVG
     VGCVLDGVRY TNGESFQPNC RYNCTCIDGT VGCTPLCLSP RPPRLWCRQP RHVRVPGQCC
     EQWVCDDDAR RPRQTALLDT RAFAASGAVE QRYENCIAYT SPWSPCSTTC GLGISTRISN
     VNARCWPEQE SRLCNLRPCD VDIRPHIKAG KKCLAVYQPE EATNFTLAGC VSTRTYRPKY
     CGVCTDNRCC IPYKSKTISV DFQCPEGPGF SRQVLWINAC FCNLSCRNPN DIFADLESYP
     DFAEIAN
//