PDGFC_GEKJA
ID PDGFC_GEKJA Reviewed; 345 AA.
AC A8WCC4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Platelet-derived growth factor C;
DE Short=PDGF-C;
DE Contains:
DE RecName: Full=Platelet-derived growth factor C, latent form;
DE Short=PDGFC latent form;
DE Contains:
DE RecName: Full=Platelet-derived growth factor C, receptor-binding form;
DE Short=PDGFC receptor-binding form;
DE Flags: Precursor;
GN Name=PDGFC;
OS Gekko japonicus (Schlegel's Japanese gecko).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Gekkota; Gekkonidae; Gekkoninae; Gekko.
OX NCBI_TaxID=146911;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fan Z., Liu Y., Liu M., Ding F., Zhou Y., Gu X.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Growth factor that plays an essential role in the regulation
CC of embryonic development, cell proliferation, cell migration, survival
CC and chemotaxis. Potent mitogen and chemoattractant for cells of
CC mesenchymal origin. Required for normal skeleton formation during
CC embryonic development. Required for normal skin morphogenesis during
CC embryonic development. Plays an important role in wound healing, in
CC angiogenesis and blood vessel development (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRA homodimers,
CC and with heterodimers formed by PDGFRA and PDGFRB (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Proteolytic removal of the N-terminal CUB domain releasing the
CC core domain is necessary for unmasking the receptor-binding epitopes of
CC the core domain. Cleavage after basic residues in the hinge region
CC (region connecting the CUB and growth factor domains) gives rise to the
CC receptor-binding form (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; EU219970; ABW95041.1; -; mRNA.
DR RefSeq; NP_001310426.1; NM_001323497.1.
DR RefSeq; XP_015285271.1; XM_015429785.1.
DR AlphaFoldDB; A8WCC4; -.
DR SMR; A8WCC4; -.
DR GeneID; 107126248; -.
DR KEGG; gja:107126248; -.
DR CTD; 56034; -.
DR OrthoDB; 962163at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:InterPro.
DR GO; GO:0048568; P:embryonic organ development; IEA:InterPro.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:InterPro.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR029817; PDGF-C.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR11633:SF5; PTHR11633:SF5; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00341; PDGF; 1.
DR SMART; SM00042; CUB; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW Glycoprotein; Growth factor; Mitogen; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..345
FT /note="Platelet-derived growth factor C, latent form"
FT /id="PRO_0000343879"
FT CHAIN ?..345
FT /note="Platelet-derived growth factor C, receptor-binding
FT form"
FT /id="PRO_0000343880"
FT DOMAIN 46..163
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT SITE 225..226
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 231..232
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 234..235
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 250..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 274
FT /note="Interchain (with C-286)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 280..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 286
FT /note="Interchain (with C-274)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 287..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 345 AA; 39065 MW; 01EB501770291799 CRC64;
MLLFGFLLLT FALVSQRQGA EAESNLSSKF QFSSAKEQNG VQEPQHEKII TVSANGSIHS
PKFPYTYPRN TVLVWRLVAI EENVLIQLTF DERFGLEDPE DDICKYDFVE VEEPSDGSIL
GRWCGSTAVP GKQISKGNQI RIRFVSDEYF PSEPGFCIHY TLLTPHQTES ASPTVLPPSA
FSLDLLNNAV AGFSTVEELI RYLEPDRWQL DLEDLYKPAW QLLGKAYIHG RKSRVVDLNL
LKEEVRMYSC TPRNFSVSLR EELKRTDTIF WPLCLLVKRC GGNCACCQHS CSECQCIPTK
VTKKYHEVLQ LKPRSGVRGL HKSLTDVPLE HHEECECVCK GNAEG
