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Platelet-derived growth factor C (PDGF-C) (Spinal cord-derived growth factor) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)]

 PDGFC_CHICK             Reviewed;         345 AA.
Q9I946;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 106.
RecName: Full=Platelet-derived growth factor C;
Short=PDGF-C;
AltName: Full=Spinal cord-derived growth factor;
Contains:
RecName: Full=Platelet-derived growth factor C, latent form;
Short=PDGFC latent form;
Contains:
RecName: Full=Platelet-derived growth factor C, receptor-binding form;
Short=PDGFC receptor-binding form;
Flags: Precursor;
Name=PDGFC; Synonyms=SCDGF;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
STRAIN=White leghorn; TISSUE=Spinal cord;
PubMed=10858496; DOI=10.1016/S0014-5793(00)01640-9;
Hamada T., Ui-Tei K., Miyata Y.;
"A novel gene derived from developing spinal cords, SCDGF, is a unique
member of the PDGF/VEGF family.";
FEBS Lett. 475:97-102(2000).
-!- FUNCTION: Growth factor that plays an essential role in the
regulation of embryonic development, cell proliferation, cell
migration, survival and chemotaxis. Potent mitogen and
chemoattractant for cells of mesenchymal origin. Required for
normal skeleton formation during embryonic development. Required
for normal skin morphogenesis during embryonic development. Plays
an important role in wound healing, in angiogenesis and blood
vessel development (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10858496}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRA
homodimers, and with heterodimers formed by PDGFRA and PDGFRB (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NRA1}.
-!- DEVELOPMENTAL STAGE: Expression increases in the spinal cord from
E4 to E16, with the highest level detected between E12 and E16.
Expression rapidly decreases after hatching.
{ECO:0000269|PubMed:10858496}.
-!- PTM: Proteolytic removal of the N-terminal CUB domain releasing
the core domain is necessary for unmasking the receptor-binding
epitopes of the core domain. Cleavage after basic residues in the
hinge region (region connecting the CUB and growth factor domains)
gives rise to the receptor-binding form (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB033829; BAB03265.1; -; mRNA.
RefSeq; NP_990052.1; NM_204721.2.
UniGene; Gga.1907; -.
ProteinModelPortal; Q9I946; -.
SMR; Q9I946; -.
STRING; 9031.ENSGALP00000015259; -.
PaxDb; Q9I946; -.
PRIDE; Q9I946; -.
Ensembl; ENSGALT00000015275; ENSGALP00000015259; ENSGALG00000009378.
GeneID; 395469; -.
KEGG; gga:395469; -.
CTD; 56034; -.
eggNOG; ENOG410IETQ; Eukaryota.
eggNOG; ENOG410XQ91; LUCA.
GeneTree; ENSGT00390000005171; -.
HOGENOM; HOG000261610; -.
HOVERGEN; HBG057324; -.
InParanoid; Q9I946; -.
KO; K05450; -.
OMA; HTYPRNM; -.
OrthoDB; EOG091G0BFZ; -.
PhylomeDB; Q9I946; -.
TreeFam; TF332130; -.
Reactome; R-GGA-186797; Signaling by PDGF.
PRO; PR:Q9I946; -.
Proteomes; UP000000539; Chromosome 4.
Bgee; ENSGALG00000009378; -.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0009790; P:embryo development; IEA:InterPro.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; IBA:GO_Central.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IBA:GO_Central.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
CDD; cd00041; CUB; 1.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR000859; CUB_dom.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR029817; PDGF-C.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR035914; Sperma_CUB_dom_sf.
PANTHER; PTHR11633:SF5; PTHR11633:SF5; 1.
Pfam; PF00431; CUB; 1.
Pfam; PF00341; PDGF; 1.
SMART; SM00042; CUB; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS50278; PDGF_2; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Complete proteome;
Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
Mitogen; Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 345 Platelet-derived growth factor C, latent
form.
/FTId=PRO_0000343877.
CHAIN ? 345 Platelet-derived growth factor C,
receptor-binding form.
/FTId=PRO_0000343878.
DOMAIN 46 163 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
SITE 225 226 Cleavage. {ECO:0000305}.
SITE 231 232 Cleavage. {ECO:0000255}.
SITE 234 235 Cleavage. {ECO:0000255}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 104 124 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 250 294 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 274 274 Interchain (with C-286).
{ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 280 335 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 286 286 Interchain (with C-274).
{ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 287 337 {ECO:0000255|PROSITE-ProRule:PRU00059}.
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


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