PDGFA_HUMAN
ID PDGFA_HUMAN Reviewed; 211 AA.
AC P04085; B5BU73;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 212.
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; Synonyms=PDGF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3422746; DOI=10.1073/pnas.85.5.1492;
RA Bonthron D.T., Morton C.C., Orkin S.H., Collins T.;
RT "Platelet-derived growth factor A chain: gene structure, chromosomal
RT location, and basis for alternative mRNA splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1492-1496(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832727; DOI=10.1128/mcb.8.2.571-577.1988;
RA Rorsman F., Bywater M., Knott T.J., Scott J., Betsholtz C.;
RT "Structural characterization of the human platelet-derived growth factor A-
RT chain cDNA and gene: alternative exon usage predicts two different
RT precursor proteins.";
RL Mol. Cell. Biol. 8:571-577(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3754619; DOI=10.1038/320695a0;
RA Betsholtz C., Johnsson A., Heldin C.H., Westermark B., Lind P., Urdea M.S.,
RA Eddy R., Shows T.B., Philpott K., Mellor A.L., Knott T.J., Scott J.;
RT "cDNA sequence and chromosomal localization of human platelet-derived
RT growth factor A-chain and its expression in tumour cell lines.";
RL Nature 320:695-699(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3666150; DOI=10.1016/0014-5793(87)80297-1;
RA Hoppe J., Schumacher L., Eichner W., Weich H.A.;
RT "The long 3'-untranslated regions of the PDGF-A and -B mRNAs are only
RT distantly related.";
RL FEBS Lett. 223:243-246(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
RX PubMed=8486521;
RA Takimoto Y., Li W.Y., Wang Z.Y., Tong B.D., Deuel T.F.;
RT "Nucleotide sequence of the 5' region of the human platelet-derived growth
RT factor A-chain gene.";
RL Hiroshima J. Med. Sci. 42:47-52(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-211.
RX PubMed=1612586; DOI=10.1016/0888-7543(92)90240-s;
RA Bonthron D., Collins T., Grzeschik K.H., van Roy N., Speleman F.;
RT "Platelet-derived growth factor A chain: confirmation of localization of
RT PDGFA to chromosome 7p22 and description of an unusual minisatellite.";
RL Genomics 13:257-263(1992).
RN [9]
RP ALTERNATIVE SPLICING.
RX PubMed=3614363; DOI=10.1038/328619a0;
RA Tong B.D., Auer D.E., Jaye M., Kaplow J.M., Ricca G., McConathy E.,
RA Drohan W., Deuel T.F.;
RT "cDNA clones reveal differences between human glial and endothelial cell
RT platelet-derived growth factor A-chains.";
RL Nature 328:619-621(1987).
RN [10]
RP ALTERNATIVE SPLICING.
RX PubMed=3614364; DOI=10.1038/328621a0;
RA Collins T., Bonthron D.T., Orkin S.H.;
RT "Alternative RNA splicing affects function of encoded platelet-derived
RT growth factor A chain.";
RL Nature 328:621-624(1987).
RN [11]
RP INTERCHAIN DISULFIDE BONDS.
RX PubMed=1317862; DOI=10.1016/s0021-9258(19)49905-5;
RA Andersson M., Oestman A., Baeckstroem G., Hellman U., George-Nascimento C.,
RA Westermark B., Heldin C.-H.;
RT "Assignment of interchain disulfide bonds in platelet-derived growth factor
RT (PDGF) and evidence for agonist activity of monomeric PDGF.";
RL J. Biol. Chem. 267:11260-11266(1992).
RN [12]
RP INTERACTION WITH CSPG4.
RX PubMed=10358027; DOI=10.1074/jbc.274.24.16831;
RA Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.;
RT "High-affinity binding of basic fibroblast growth factor and platelet-
RT derived growth factor-AA to the core protein of the NG2 proteoglycan.";
RL J. Biol. Chem. 274:16831-16837(1999).
RN [13]
RP REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE.
RX PubMed=18483217; DOI=10.1101/gad.1653708;
RA Andrae J., Gallini R., Betsholtz C.;
RT "Role of platelet-derived growth factors in physiology and medicine.";
RL Genes Dev. 22:1276-1312(2008).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-181, AND DISULFIDE BONDS.
RX PubMed=20534510; DOI=10.1073/pnas.1000806107;
RA Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.;
RT "Structures of a platelet-derived growth factor/propeptide complex and a
RT platelet-derived growth factor/receptor complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010).
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 Required for normal lung alveolar septum formation during
CC embryogenesis, normal development of the gastrointestinal tract, normal
CC development of Leydig cells and spermatogenesis. Required for normal
CC oligodendrocyte development and normal myelination in the spinal cord
CC and cerebellum. Plays an important role in wound healing. Signaling is
CC modulated by the formation of heterodimers with PDGFB (By similarity).
CC {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. Interacts with CSPG4. {ECO:0000269|PubMed:10358027,
CC ECO:0000269|PubMed:20534510}.
CC -!- INTERACTION:
CC P04085; P16234: PDGFRA; NbExp=6; IntAct=EBI-2881386, EBI-2861522;
CC P04085-1; P04085-1: PDGFA; NbExp=2; IntAct=EBI-15499388, EBI-15499388;
CC P04085-2; Q12797-6: ASPH; NbExp=5; IntAct=EBI-11995148, EBI-12092171;
CC P04085-2; O95983-2: MBD3; NbExp=3; IntAct=EBI-11995148, EBI-11978579;
CC P04085-2; Q99750: MDFI; NbExp=3; IntAct=EBI-11995148, EBI-724076;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon
CC wounding.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P04085-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P04085-2; Sequence=VSP_004602, VSP_004603;
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; X03795; CAA27421.1; -; mRNA.
DR EMBL; X06374; CAA29677.1; -; mRNA.
DR EMBL; M20494; AAA60045.1; -; Genomic_DNA.
DR EMBL; M20488; AAA60045.1; JOINED; Genomic_DNA.
DR EMBL; M20489; AAA60045.1; JOINED; Genomic_DNA.
DR EMBL; M20490; AAA60045.1; JOINED; Genomic_DNA.
DR EMBL; M20491; AAA60045.1; JOINED; Genomic_DNA.
DR EMBL; M20492; AAA60045.1; JOINED; Genomic_DNA.
DR EMBL; M20493; AAA60045.1; JOINED; Genomic_DNA.
DR EMBL; M19988; AAA60046.1; -; Genomic_DNA.
DR EMBL; M21571; AAA60046.1; JOINED; Genomic_DNA.
DR EMBL; M19984; AAA60046.1; JOINED; Genomic_DNA.
DR EMBL; M19985; AAA60046.1; JOINED; Genomic_DNA.
DR EMBL; M19986; AAA60046.1; JOINED; Genomic_DNA.
DR EMBL; M19987; AAA60046.1; JOINED; Genomic_DNA.
DR EMBL; M19989; AAA60047.1; -; Genomic_DNA.
DR EMBL; M21571; AAA60047.1; JOINED; Genomic_DNA.
DR EMBL; M19984; AAA60047.1; JOINED; Genomic_DNA.
DR EMBL; M19985; AAA60047.1; JOINED; Genomic_DNA.
DR EMBL; M19986; AAA60047.1; JOINED; Genomic_DNA.
DR EMBL; M19987; AAA60047.1; JOINED; Genomic_DNA.
DR EMBL; AB451309; BAG70123.1; -; mRNA.
DR EMBL; AB451439; BAG70253.1; -; mRNA.
DR EMBL; AC147651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S62078; AAB26566.1; -; Genomic_DNA.
DR CCDS; CCDS34578.1; -. [P04085-1]
DR CCDS; CCDS47524.1; -. [P04085-2]
DR PIR; A28964; PFHUG1.
DR PIR; B28964; B28964.
DR RefSeq; NP_002598.4; NM_002607.5. [P04085-1]
DR RefSeq; NP_148983.1; NM_033023.4. [P04085-2]
DR PDB; 3MJK; X-ray; 2.40 A; A/B/E/F/X/Y=21-181.
DR PDBsum; 3MJK; -.
DR AlphaFoldDB; P04085; -.
DR SMR; P04085; -.
DR BioGRID; 111180; 44.
DR ComplexPortal; CPX-1874; Platelet-derived growth factor AA complex.
DR ComplexPortal; CPX-1875; Platelet-derived growth factor AB complex.
DR ComplexPortal; CPX-2881; PDGF receptor alpha - PDGF-AA complex.
DR ComplexPortal; CPX-2885; PDGF receptor alpha - PDGF-AB complex.
DR ComplexPortal; CPX-2886; PDGF receptor beta - PDGF-AB complex.
DR ComplexPortal; CPX-2892; PDGF receptor alpha-beta - PDGF-AB complex.
DR DIP; DIP-5735N; -.
DR IntAct; P04085; 7.
DR STRING; 9606.ENSP00000346508; -.
DR BindingDB; P04085; -.
DR ChEMBL; CHEMBL3137294; -.
DR GlyGen; P04085; 1 site.
DR iPTMnet; P04085; -.
DR PhosphoSitePlus; P04085; -.
DR BioMuta; PDGFA; -.
DR EPD; P04085; -.
DR jPOST; P04085; -.
DR MassIVE; P04085; -.
DR PaxDb; P04085; -.
DR PeptideAtlas; P04085; -.
DR PRIDE; P04085; -.
DR ProteomicsDB; 51650; -. [P04085-1]
DR ProteomicsDB; 51651; -. [P04085-2]
DR Antibodypedia; 3957; 463 antibodies from 36 providers.
DR DNASU; 5154; -.
DR Ensembl; ENST00000354513.9; ENSP00000346508.5; ENSG00000197461.13. [P04085-1]
DR Ensembl; ENST00000402802.7; ENSP00000383889.3; ENSG00000197461.13. [P04085-2]
DR GeneID; 5154; -.
DR KEGG; hsa:5154; -.
DR MANE-Select; ENST00000402802.8; ENSP00000383889.3; NM_033023.5; NP_148983.1. [P04085-2]
DR UCSC; uc003sir.4; human. [P04085-1]
DR CTD; 5154; -.
DR DisGeNET; 5154; -.
DR GeneCards; PDGFA; -.
DR HGNC; HGNC:8799; PDGFA.
DR HPA; ENSG00000197461; Tissue enhanced (skeletal).
DR MIM; 173430; gene.
DR neXtProt; NX_P04085; -.
DR OpenTargets; ENSG00000197461; -.
DR PharmGKB; PA33144; -.
DR VEuPathDB; HostDB:ENSG00000197461; -.
DR eggNOG; ENOG502QVAU; Eukaryota.
DR GeneTree; ENSGT00940000159039; -.
DR HOGENOM; CLU_094438_1_0_1; -.
DR InParanoid; P04085; -.
DR OMA; HHKNSSH; -.
DR OrthoDB; 1439735at2759; -.
DR PhylomeDB; P04085; -.
DR TreeFam; TF319554; -.
DR PathwayCommons; P04085; -.
DR Reactome; R-HSA-114608; Platelet degranulation. [P04085-1]
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; P04085; -.
DR SIGNOR; P04085; -.
DR BioGRID-ORCS; 5154; 7 hits in 1079 CRISPR screens.
DR ChiTaRS; PDGFA; human.
DR EvolutionaryTrace; P04085; -.
DR GeneWiki; PDGFA; -.
DR GenomeRNAi; 5154; -.
DR Pharos; P04085; Tchem.
DR PRO; PR:P04085; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P04085; protein.
DR Bgee; ENSG00000197461; Expressed in buccal mucosa cell and 185 other tissues.
DR ExpressionAtlas; P04085; baseline and differential.
DR Genevisible; P04085; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:1990265; C:platelet-derived growth factor complex; IPI:ComplexPortal.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IPI:BHF-UCL.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; ISS:UniProtKB.
DR GO; GO:0001775; P:cell activation; TAS:BHF-UCL.
DR GO; GO:0030031; P:cell projection assembly; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:1990401; P:embryonic lung development; ISS:BHF-UCL.
DR GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0050919; P:negative chemotaxis; IDA:BHF-UCL.
DR GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0010544; P:negative regulation of platelet activation; IDA:BHF-UCL.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035790; P:platelet-derived growth factor receptor-alpha signaling pathway; IC:ComplexPortal.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IDA:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:BHF-UCL.
DR GO; GO:0060683; P:regulation of branching involved in salivary gland morphogenesis by epithelial-mesenchymal signaling; ISS:UniProtKB.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:BHF-UCL.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; TAS:BHF-UCL.
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 1: Evidence at protein level;
KW 3D-structure; 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..20
FT PROPEP 21..86
FT /note="Removed in mature form"
FT /id="PRO_0000023356"
FT CHAIN 87..211
FT /note="Platelet-derived growth factor subunit A"
FT /id="PRO_0000023357"
FT REGION 158..162
FT /note="Receptor binding site"
FT /evidence="ECO:0000255"
FT REGION 185..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..140
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 123
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 129..177
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 132
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:20534510"
FT DISULFID 133..179
FT /evidence="ECO:0000269|PubMed:20534510"
FT VAR_SEQ 194..196
FT /note="GRP -> DVR (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:19054851"
FT /id="VSP_004602"
FT VAR_SEQ 197..211
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:19054851"
FT /id="VSP_004603"
FT CONFLICT 64..66
FT /note="RAH -> TRD (in Ref. 2; AAA60045)"
FT /evidence="ECO:0000305"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:3MJK"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:3MJK"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3MJK"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3MJK"
FT STRAND 118..130
FT /evidence="ECO:0007829|PDB:3MJK"
FT STRAND 134..181
FT /evidence="ECO:0007829|PDB:3MJK"
SQ SEQUENCE 211 AA; 24043 MW; 48633DDE558EFA43 CRC64;
MRTLACLLLL GCGYLAHVLA EEAEIPREVI ERLARSQIHS IRDLQRLLEI DSVGSEDSLD
TSLRAHGVHA TKHVPEKRPL PIRRKRSIEE AVPAVCKTRT VIYEIPRSQV DPTSANFLIW
PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV KVAKVEYVRK KPKLKEVQVR LEEHLECACA
TTSLNPDYRE EDTGRPRESG KKRKRKRLKP T
