CCN4_RAT
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 25-MAY-2022, entry version 119.
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 GlyGen; Q99PP0; 4 sites.
DR PaxDb; Q99PP0; -.
DR GeneID; 65154; -.
DR KEGG; rno:65154; -.
DR UCSC; RGD:69431; rat.
DR CTD; 8840; -.
DR RGD; 69431; Wisp1.
DR eggNOG; ENOG502QQQQ; Eukaryota.
DR InParanoid; Q99PP0; -.
DR OrthoDB; 601212at2759; -.
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:0060548; P:negative regulation of cell death; IBA:GO_Central.
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; 2.20.100.10; -; 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 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; SSF57184; SSF57184; 1.
DR SUPFAM; SSF82895; SSF82895; 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 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
