PDGFA_XENLA
ID PDGFA_XENLA Reviewed; 226 AA.
AC P13698;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Platelet-derived growth factor subunit A;
DE Short=PDGF subunit A;
DE AltName: Full=PDGF-1;
DE AltName: Full=Platelet-derived growth factor A chain;
DE AltName: Full=Platelet-derived growth factor alpha polypeptide;
DE Flags: Precursor;
GN Name=pdgfa;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=3413486; DOI=10.1126/science.3413486;
RA Mercola M., Melton D.A., Stiles C.D.;
RT "Platelet-derived growth factor A chain is maternally encoded in Xenopus
RT embryos.";
RL Science 241:1223-1225(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=2308861; DOI=10.1093/nar/18.3.680;
RA Bejcek B.E., Li D.Y., Deuel T.F.;
RT "Nucleotide sequence of a cDNA clone of Xenopus platelet-derived growth
RT factor A-chain.";
RL Nucleic Acids Res. 18:680-680(1990).
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.
CC Signaling is modulated by the formation of heterodimers with PDGFB (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; antiparallel disulfide-linked dimer. Heterodimer
CC with PDGFB; antiparallel disulfide-linked dimer. The PDGFA homodimer
CC interacts with PDGFRA homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB
CC interacts with PDGFRA homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P13698-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P13698-2; Sequence=VSP_004611, VSP_004612;
CC -!- DOMAIN: The long form contains a basic insert which acts as a cell
CC retention signal.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; M23237; AAA49927.1; -; mRNA.
DR EMBL; M23238; AAA49928.1; -; mRNA.
DR EMBL; X17545; CAA35583.1; -; mRNA.
DR PIR; I51550; I51550.
DR PIR; I51551; I51551.
DR PIR; S08220; S08220.
DR RefSeq; NP_001081304.1; NM_001087835.1. [P13698-1]
DR RefSeq; XP_018092793.1; XM_018237304.1.
DR RefSeq; XP_018092794.1; XM_018237305.1. [P13698-2]
DR AlphaFoldDB; P13698; -.
DR SMR; P13698; -.
DR PRIDE; P13698; -.
DR GeneID; 397765; -.
DR KEGG; xla:397765; -.
DR CTD; 397765; -.
DR Xenbase; XB-GENE-484499; pdgfa.S.
DR OMA; THTHFPP; -.
DR OrthoDB; 1439735at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 397765; Expressed in internal ear and 18 other tissues.
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:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR006782; PDGF_N.
DR Pfam; PF00341; PDGF; 1.
DR Pfam; PF04692; PDGF_N; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
KW Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT PROPEP 23..91
FT /note="Removed in mature form"
FT /id="PRO_0000023364"
FT CHAIN 92..226
FT /note="Platelet-derived growth factor subunit A"
FT /id="PRO_0000023365"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..145
FT /evidence="ECO:0000250"
FT DISULFID 128
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 134..182
FT /evidence="ECO:0000250"
FT DISULFID 137
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 138..184
FT /evidence="ECO:0000250"
FT VAR_SEQ 198..200
FT /note="GFF -> DVR (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_004611"
FT VAR_SEQ 201..226
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_004612"
FT CONFLICT 199..209
FT /note="Missing (in Ref. 2; CAA35583)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="Q -> R (in Ref. 2; CAA35583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25720 MW; E3E724FCF67C2FB2 CRC64;
MRIWAWILLL SVCCSYLSPS LGEEAEIPQE LIERLAHSEI RSISDLQRLL DIDSVGGGED
ASAANIRSQK HDFHHNRLVP EKRSVPSRRK RSVEEAVPAI CKTRTVIYEI PRSQIDPTSA
NFLIWPPCVE VKRCTGCCNT SSVKCQPSRI HHRSVKVAKV EYVRKKPKLK EVLVRLEEHL
ECTCTANSNS DYREEETGFF TSPALVLTGR TRETGKKQKR KKLKPT
