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   24-JAN-2024, entry version 128.
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 4 dpc
CC       to 16 dpc, with the highest level detected between 12 dpc and 16 dpc.
CC       Expression rapidly decreases after hatching.
CC       {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   GlyCosmos; Q9I946; 1 site, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000015259; -.
DR   Ensembl; ENSGALT00000015275; ENSGALP00000015259; ENSGALG00000009378.
DR   Ensembl; ENSGALT00010019578.1; ENSGALP00010011126.1; ENSGALG00010008185.1.
DR   Ensembl; ENSGALT00015006471; ENSGALP00015004024; ENSGALG00015002880.
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; MCVVIQT; -.
DR   OrthoDB; 3908391at2759; -.
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 cell types or 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:0005161; F:platelet-derived growth factor receptor binding; IBA:GO_Central.
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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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; Cystine-knot cytokines; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR000072; PDGF/VEGF_dom.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR11633; PLATELET-DERIVED GROWTH FACTOR; 1.
DR   PANTHER; PTHR11633:SF5; PLATELET-DERIVED GROWTH FACTOR C; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00341; PDGF; 1.
DR   SMART; SM00042; CUB; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 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
//