PDGFC_CHICK
ID PDGFC_CHICK Reviewed; 345 AA.
AC Q9I946;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Platelet-derived growth factor C;
DE Short=PDGF-C;
DE AltName: Full=Spinal cord-derived growth factor;
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; Synonyms=SCDGF;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=White leghorn; TISSUE=Spinal cord;
RX PubMed=10858496; DOI=10.1016/s0014-5793(00)01640-9;
RA Hamada T., Ui-Tei K., Miyata Y.;
RT "A novel gene derived from developing spinal cords, SCDGF, is a unique
RT member of the PDGF/VEGF family.";
RL FEBS Lett. 475:97-102(2000).
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, ECO:0000269|PubMed:10858496}.
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|UniProtKB:Q9NRA1}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in the spinal cord from E4 to
CC E16, with the highest level detected between E12 and E16. Expression
CC rapidly decreases after hatching. {ECO:0000269|PubMed:10858496}.
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; AB033829; BAB03265.1; -; mRNA.
DR RefSeq; NP_990052.1; NM_204721.2.
DR AlphaFoldDB; Q9I946; -.
DR SMR; Q9I946; -.
DR STRING; 9031.ENSGALP00000015259; -.
DR PaxDb; Q9I946; -.
DR Ensembl; ENSGALT00000015275; ENSGALP00000015259; ENSGALG00000009378.
DR GeneID; 395469; -.
DR KEGG; gga:395469; -.
DR CTD; 56034; -.
DR VEuPathDB; HostDB:geneid_395469; -.
DR eggNOG; ENOG502QUUR; Eukaryota.
DR GeneTree; ENSGT00940000158645; -.
DR HOGENOM; CLU_037859_0_0_1; -.
DR InParanoid; Q9I946; -.
DR OMA; LDENVWI; -.
DR OrthoDB; 962163at2759; -.
DR PhylomeDB; Q9I946; -.
DR TreeFam; TF332130; -.
DR Reactome; R-GGA-186797; Signaling by PDGF.
DR PRO; PR:Q9I946; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000009378; Expressed in heart and 10 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0048568; P:embryonic organ development; IEA:InterPro.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IBA:GO_Central.
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; Reference proteome; 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_0000343877"
FT CHAIN ?..345
FT /note="Platelet-derived growth factor C, receptor-binding
FT form"
FT /id="PRO_0000343878"
FT DOMAIN 46..163
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT SITE 225..226
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT SITE 231..232
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 234..235
FT /note="Cleavage"
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; 38940 MW; 97ACEA992BF5128C CRC64;
MLLLGLLLLT SALAGRRHGA AAESDLSSKF SFPGAKEQNG VQDPQHEKII TVTSNGSIHS
PKFPHTYPRN TVLVWRLVAV DENVWIQLTF DERFGLEDPE DDICKYDFVE VEEPSDGTVL
GRWCGSSSVP SRQISKGNQI RIRFVSDEYF PSQPGFCIHY TLLVPHHTEA PSPSSLPPSA
LPLDVLNNAV AGFSTVEELI RYLEPDRWQL DLEDLYRPTW QLLGKAYIHG RKSRVVDLNL
LKEEVRLYSC TPRNFSVSLR EELKRTDTIF WPLCLLVKRC GGNCACCHQN CNECQCIPTK
VTKKYHEVLQ LKPRSGVRGL HKSLTDVPLE HHEECDCVCK GNSEG
