PDGFD_RABIT
ID PDGFD_RABIT Reviewed; 300 AA.
AC Q6V9H4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Platelet-derived growth factor D;
DE Short=PDGF-D;
DE AltName: Full=Iris-expressed growth factor;
DE Contains:
DE RecName: Full=Platelet-derived growth factor D, latent form;
DE Short=PDGFD latent form;
DE Contains:
DE RecName: Full=Platelet-derived growth factor D, receptor-binding form;
DE Short=PDGFD receptor-binding form;
DE Flags: Precursor; Fragment;
GN Name=PDGFD; Synonyms=IEGF;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15611105; DOI=10.1074/jbc.m413570200;
RA Ray S., Gao C., Wyatt K., Fariss R.N., Bundek A., Zelenka P., Wistow G.;
RT "Platelet-derived growth factor D, tissue-specific expression in the eye,
RT and a key role in control of lens epithelial cell proliferation.";
RL J. Biol. Chem. 280:8494-8502(2005).
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 for cells of mesenchymal origin. Plays
CC an important role in wound healing. Induces macrophage recruitment,
CC increased interstitial pressure, and blood vessel maturation during
CC angiogenesis. Can initiate events that lead to a mesangial
CC proliferative glomerulonephritis, including influx of monocytes and
CC macrophages and production of extracellular matrix (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRB homodimers,
CC and with heterodimers formed by PDGFRA and PDGFRB (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released by
CC platelets upon wounding. {ECO:0000250}.
CC -!- PTM: Activated by proteolytic cleavage. Proteolytic removal of the N-
CC terminal CUB domain releasing the core domain is necessary for
CC unmasking the receptor-binding epitopes of the core domain. Cleavage
CC after Arg-191 or Arg-193 by urokinase plasminogen activator gives rise
CC to the active form (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; AY347260; AAQ24382.1; -; mRNA.
DR AlphaFoldDB; Q6V9H4; -.
DR SMR; Q6V9H4; -.
DR STRING; 9986.ENSOCUP00000013155; -.
DR eggNOG; ENOG502QPQY; Eukaryota.
DR InParanoid; Q6V9H4; -.
DR Proteomes; UP000001811; Unplaced.
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: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 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; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR027123; PDGFD.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR11633:SF4; PTHR11633:SF4; 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.
FT CHAIN <1..>300
FT /note="Platelet-derived growth factor D, latent form"
FT /id="PRO_0000250194"
FT CHAIN 194..>300
FT /note="Platelet-derived growth factor D, receptor-binding
FT form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250195"
FT DOMAIN <1..114
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT SITE 191..192
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 193..194
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 240
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT NON_TER 1
FT NON_TER 300
SQ SEQUENCE 300 AA; 34616 MW; 716C873C9C01C0C6 CRC64;
QVTGNGHVQS LAFPNSYPRN LLLTWRLHSQ EKTRIQLAFD HQFGLEEAEN DICRYDFVEV
EDISETSTVI RGRWCGHKEV PPRITSRTNQ IKITFKSDDY FVAKPGFKIY YSFVEDFQPA
AASETNWESV TSSISGVSYH NPSVTDPTLT ADALDKTIAE FDTVEDLLKH FNPESWQEDL
ENLYLDTPHY RGRSYHDRKS KVDLDRLNDD AKRYSCTPRN YSVNLREELK LTNVVFFPRC
LLVQRCGGNC GCGTVNWKSC TCSSGKTVKK YHEVLKFEPG HFKRRNRAKN MALVDIQLDH
