CCN1_PANTR
ID CCN1_PANTR Reviewed; 381 AA.
AC A5A6L1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=CCN family member 1 {ECO:0000305};
DE AltName: Full=Cellular communication network factor 1;
DE AltName: Full=Cysteine-rich angiogenic inducer 61;
DE AltName: Full=Protein CYR61;
DE Flags: Precursor;
GN Name=CCN1; Synonyms=Cyr61;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
CC -!- FUNCTION: Promotes cell proliferation, chemotaxis, angiogenesis and
CC cell adhesion. Appears to play a role in wound healing by up-
CC regulating, in skin fibroblasts, the expression of a number of genes
CC involved in angiogenesis, inflammation and matrix remodeling including
CC VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and
CC alpha-5 (By similarity). CCN1-mediated gene regulation is dependent on
CC heparin-binding (By similarity). Down-regulates the expression of
CC alpha-1 and alpha-2 subunits of collagen type-1 (By similarity).
CC Promotes cell adhesion and adhesive signaling through integrin alpha-
CC 6/beta-1, cell migration through integrin alpha-1/beta-5 and cell
CC proliferation through integrin alpha-v/beta-3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interaction with integrins is heparin- and cell-type-dependent
CC and promotes cell adhesion. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR EMBL; AB222139; BAF62384.1; -; mRNA.
DR RefSeq; NP_001092023.1; NM_001098553.1.
DR AlphaFoldDB; A5A6L1; -.
DR SMR; A5A6L1; -.
DR STRING; 9598.ENSPTRP00000001581; -.
DR PaxDb; A5A6L1; -.
DR Ensembl; ENSPTRT00000001732; ENSPTRP00000001581; ENSPTRG00000000916.
DR GeneID; 456988; -.
DR KEGG; ptr:456988; -.
DR CTD; 3491; -.
DR VGNC; VGNC:6741; CCN1.
DR eggNOG; ENOG502QQQQ; Eukaryota.
DR GeneTree; ENSGT00940000155151; -.
DR HOGENOM; CLU_063247_1_0_1; -.
DR InParanoid; A5A6L1; -.
DR OMA; CPLEVPK; -.
DR OrthoDB; 999958at2759; -.
DR TreeFam; TF326070; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000000916; Expressed in fibroblast and 21 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0003278; P:apoptotic process involved in heart morphogenesis; IEA:Ensembl.
DR GO; GO:0060413; P:atrial septum morphogenesis; IEA:Ensembl.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0060591; P:chondroblast differentiation; IEA:Ensembl.
DR GO; GO:0060710; P:chorio-allantoic fusion; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0002041; P:intussusceptive angiogenesis; IEA:Ensembl.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; 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:0010518; P:positive regulation of phospholipase activity; IEA:Ensembl.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR GO; GO:0044319; P:wound healing, spreading of cells; IEA:Ensembl.
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; Chemotaxis; Disulfide bond; Growth factor binding;
KW Heparin-binding; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..381
FT /note="CCN family member 1"
FT /id="PRO_0000297553"
FT DOMAIN 25..94
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 228..273
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 286..360
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 279..315
FT /note="Heparin-binding"
FT /evidence="ECO:0000250|UniProtKB:P18406"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00622"
FT DISULFID 286..323
FT /evidence="ECO:0000250"
FT DISULFID 303..337
FT /evidence="ECO:0000250"
FT DISULFID 314..353
FT /evidence="ECO:0000250"
FT DISULFID 317..355
FT /evidence="ECO:0000250"
FT DISULFID 322..359
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 42013 MW; 923330133F2A7F8B CRC64;
MSSRIARALA LVVTLLHLTR LALSTCPAAC HCPLEAPKCA PGVGLVRDGC GCCKVCAKQL
NEDCSKTQPC DHTKGLECNF GASSTALKGI CRAQSEGRPC EYNSRIYQNG ESFQPNCKHQ
CTCIDGAVGC IPLCPQELSL PNLGCPNPRL VKVSGQCCEE WVCDEDSIKD PMEDQDGLLG
KELGFDASEV ELTRNNELIA VGKGSSLKRL PVFGMEPRIL YNPLQGQKCI VQTTSWSQCS
KTCGTGISTR VTNDNPECRL VKETRICEVR PCGQPVYSSL KKGKKCSKTK KSPEPVRFTY
AGCLSVKKYR PKYCGSCVDG RCCTPQLTRT VKMRFRCEDG ETFSKNVMMI QSCKCNYNCP
HANEAAFPFY RLFNDIHKFR D
