ID A0A5N5LAW1_PANHP Unreviewed; 1465 AA.
AC A0A5N5LAW1;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Platelet-derived growth factor receptor alpha {ECO:0000256|ARBA:ARBA00016938};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=Alpha platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00030503};
DE AltName: Full=Alpha-type platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00029782};
GN ORFNames=PHYPO_G00092030 {ECO:0000313|EMBL:KAB5539700.1};
OS Pangasianodon hypophthalmus (Striped catfish) (Helicophagus hypophthalmus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Pangasiidae; Pangasianodon.
OX NCBI_TaxID=310915 {ECO:0000313|EMBL:KAB5539700.1, ECO:0000313|Proteomes:UP000327468};
RN [1] {ECO:0000313|EMBL:KAB5539700.1, ECO:0000313|Proteomes:UP000327468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indonesia {ECO:0000313|EMBL:KAB5539700.1,
RC ECO:0000313|Proteomes:UP000327468};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB5539700.1};
RA Wen M., Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Avarre J.-C., Campet M., Ha T.T.T., Dugue R., Lampietro C., Louis A.,
RA Herpin A., Echchiki A., Berthelot C., Parey E., Roest-Crollius H.,
RA Braasch I., Postlethwait J., Bobe J., Montfort J., Bouchez O., Begum T.,
RA Schartl M., Guiguen Y.;
RT "A chromosome-scale genome assembly of the striped catfish, Pangasianodon
RT hypophthalmus.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- SUBUNIT: Interacts with homodimeric pdgfa, pdgfb and pdgfc, and with
CC heterodimers formed by pdgfa and pdgfb. Monomer in the absence of bound
CC ligand. Interaction with dimeric pdgfa, pdgfb and/or pdgfc leads to
CC receptor dimerization, where both pdgfra homodimers and heterodimers
CC with pdgfrb are observed. {ECO:0000256|ARBA:ARBA00064866}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC protein {ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB5539700.1}.
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DR EMBL; VFJC01000020; KAB5539700.1; -; Genomic_DNA.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP000327468; Chromosome 19.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IEA:InterPro.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:TreeGrafter.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:TreeGrafter.
DR CDD; cd00096; Ig; 1.
DR FunFam; 2.60.40.10:FF:000720; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 1.10.510.10:FF:000140; Platelet-derived growth factor receptor beta; 1.
DR FunFam; 2.60.40.10:FF:000223; Platelet-derived growth factor receptor beta; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027290; PDGFRA.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR050122; RTK.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR PANTHER; PTHR24416:SF52; PLATELET-DERIVED GROWTH FACTOR RECEPTOR ALPHA; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR500950-52};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000615-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000327468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1465
FT /note="Platelet-derived growth factor receptor alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024337230"
FT TRANSMEM 905..929
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..298
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 608..687
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 698..789
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 973..1331
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1382..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1195
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 952
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 979..987
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 980..987
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1007
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1055..1061
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1339
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 437..482
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 528..569
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 615..669
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 814..881
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
SQ SEQUENCE 1465 AA; 164020 MW; 53EE38A6207AA526 CRC64;
MWILKTHLLL GVVLFGILQN GACELPPPII VSDRGEFVLE LHSVFNISCT GNKSVVWEEP
LPVNTHVLPG YYTTTLLIDG AAAHHTGEYT CIYNDSDEEQ PNINNMASIY IFVPDPEVPF
VPDDPTEASQ FNIPCRITDP QSTVILRSLP SGDVVPYEYE EKYGFLGSFV PGQYVCETVV
NGEVVRSMVY PVTDRPNGSD MFNVMENDFS VKLTASQEEI KEGEAFNLTC TVPPGSLYVQ
KWLHPSKEAV GAIQKKETYP DKVLYILSIP HASTNDTGFY ECSVTEQSSG KTHSSQVTIT
VHESSFVTLD HSGIGAVETI SLLEEAEFTI YIHSDAVPKV TWFKDDNVLN TNYITAKTTL
LADKRYESVL VLRHPVEEDS GTYKILASAG SKSKEFSFKL YVKAGEPQII QSMLAPVIWP
REETMVVFLH SMFRLTCRGQ AEVVWEGPIP LDKQKLDDKR GLFVSTVTVD NAEATHTGEY
TCLYKNENQT EESSIYIFVP DPNIPFVAPP LPFGHHVLKS PEEMEVPCRV SDPSAQVTLF
HVETQQAVPA TYDSKKGFLG NFTPGTYVCQ ALVNGEEHES EEYIVHGWTG GSGLHVEMKA
EKKALLVGET LIVNCVAKGS DLLDQQWKYP GKMADRAKMT LKENKKDQEI YYTLTVSDAR
TKDSGNYACS ITDIMSNESQ TKELTITVYE REFVSLAPMF APVETAKLND VREFQVDIEA
LPAPKVTWLK DGIVLGDTAA EFTTSLRTIS ETRYQSTLAL IRAKAEDSGN YTVRAQIGNQ
SASHSFNLQV KVPAVIVDLM DLHHGSETGQ AVVCVAGGSP VPEVEWYICK NIKQCSNDSN
EWSPLQTNTT GITIDTHIDQ DNQLESQVIF GHLENTLAVR CLARNEMVAV SREIKLVANG
PHSELTVAAA VLVLLVIVII SLIVLVIIWK QKPRYEIRWR VIESVSPDGH EYIYVDPMQL
PYDTRWEFPR DGLVLGRILG SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA
LMSELKIMTH LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DTFLSRQGEK
GKKDLDIFGI NPADESSRSY VILSFEEKGD YMDMKQADTM QYVPMLERSN ASKYFDLQRD
DYDHPPSHKH INDSEVEKLL SDDSERLTTM DLLSFTYQVA RGMEFLASKN CVHRDLAARN
VLLSQGKIVK ICDFGLARDI MHDNNYVSKG STFLPVKWMA PESIFDNLYT TLSDVWSYGI
LLWEIFSLGG TPYPGMVVDS SFYNKIKSGY RMAKPEHASS DVYELMVKCW NNEPEKRPSF
HSLSESVATL LPCGYKRSYE RVNNDFLKSD HPAVTRVQCV QSDETYLGVA YKNQCKMRER
ESGFEEQRLS SDSGYIIPLP DLDPLSDEEY TKRNRHSSQT SEESAIETGS SSSTLPKREV
ETLEDITLLD EMCLDSGDLV EDSFL
//
