ID A0A6G1PLN5_CHAAH Unreviewed; 1628 AA.
AC A0A6G1PLN5;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
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=EXN66_Car006870 {ECO:0000313|EMBL:KAF3691195.1};
OS Channa argus (Northern snakehead) (Ophicephalus argus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Channoidei; Channidae; Channa.
OX NCBI_TaxID=215402 {ECO:0000313|EMBL:KAF3691195.1, ECO:0000313|Proteomes:UP000503349};
RN [1] {ECO:0000313|EMBL:KAF3691195.1, ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OARG1902GOOAL {ECO:0000313|EMBL:KAF3691195.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF3691195.1};
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus genome.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus Var Kimnra genome.";
RL Submitted (FEB-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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-
CC ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
CC -!- SIMILARITY: Belongs to the Antp homeobox family.
CC {ECO:0000256|ARBA:ARBA00009107}.
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DR EMBL; CM015717; KAF3691195.1; -; Genomic_DNA.
DR Proteomes; UP000503349; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
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:1990837; F:sequence-specific double-stranded DNA binding; IEA:TreeGrafter.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00086; homeodomain; 1.
DR FunFam; 1.10.10.60:FF:000147; GS homeobox 2; 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; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR042191; GSH1/2.
DR InterPro; IPR001356; HD.
DR InterPro; IPR020479; HD_metazoa.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR009057; Homeodomain-like_sf.
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; IPR013151; Immunoglobulin_dom.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR47421; GS HOMEOBOX 2; 1.
DR PANTHER; PTHR47421:SF1; GS HOMEOBOX 2; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
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|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KAF3691195.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000503349};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
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 TRANSMEM 1113..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..194
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 358..513
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 824..901
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 914..1001
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1181..1498
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 136..195
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 193..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1362
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 1160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1187..1195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 1188..1195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1226..1232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT DISULFID 652..697
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 744..785
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 831..885
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 1030..1089
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
SQ SEQUENCE 1628 AA; 181577 MW; 878E65AB174BE23E CRC64;
MSRSFYVDSL IIKDTVRPGP AEHPGQDFLI PISMHSPSVM TVTAPVCPSR KNGTFCVCPL
CVTSHIHSSR SGIPMLKNQF PGADTQYCQR IAHQQSPALA HPGHSPVCTP TFGVTDPRRY
HCLSIGASEN SHTQNGKRMR TAFTSTQLLE LEREFSTNMY LSRLRRIEIA TYLNLSEKQV
KIWFQNRRVK HKKEGKATQR SAHSGCKCST GHTDYSRSED EESLSPASTS EEKEARTSIG
MDGMQTCVVF GSMLVFLFSV TSALSPPTIE STKREFIVQP MSTFNISCSG KRKVVWDEPL
PKNSFVLPGY YTATLFLFNA SVENTGYYFC VYEKEEKQQE ALWEEPNEAE IYVFVPDPKV
PFVPETPENL VVAMDLKGVT ISCRVSNPNS SVILRSVPSG REMSAHYNNM MGFFGSLSPG
QYQCETTVKE QIVKSDIYTV QTEVPAQMED FSVEVKASEK TAVGAGQMKQ TFPDRVTYTL
SIPKATPQDS GTYECSITHD ISGEVRVSSV AVTVVEENSF VKLDHSGILA TGFVSPLEET
EFTILIEAYP PPKVTWLKDG KAISGNNYVH TKTRHIEGNR YESILTLQQP IEKDNGNYSI
MASSGSRSAT FSFTLKVKAP FTMALPPSSA PLLLPQLQEM VVPLHTSFTL TCRGEAKLAW
LIPFDAYEQM LEDNSGLFVT TITVDNATAM HTGYYTCYYN RNTTEEVESS IYIYVPDPEV
PFVPSPVPFG NHVLSDHEEM EIQCRVSDPS ANVTLINVDT QQPVPSVYDS KRGALGIFTA
GTYICKALIN GEEQYSSEYI VHGWTGGASL HVELTAKRTA LLVGDTITVT CIARGSEILE
DHWKYPGKQA NRAFKTVHEN KRDQEILYTL TISQASTKDS GIYSCSITDI ISNESQTKEL
AIRVFAGEFM SVKPLFGEYE SAELDEVREF KAEISSFPTA HVTWLKDGIP LSDVTAEIST
SLRQDSETSY VSVLTLIRAK EEDSGNYTLR VENGNQSQDI GIILEVKVPA AIVDLMDIHH
GSATGQSVVC ITRGQPTPAV ECCANDSSSW VPLTTNSTGI TLDSHIDEDN NLESQVMFGH
LENTLAVRCL ARNEMGAVSR EVKLVSSGPH PELTVAAAVL VLLVIVIISL IVLVVIWKQK
PRYEIRWRVI ESVSPDGHEY IYVDPMQLPY DSRWEFPRDR LVLGRILGSG AFGKVVEGTA
YGLSRSQPVM KVAVKMLKRP IYIITEYCFY GDLVNYLHKN RENFLSLNPE KNKKELDIFG
INPADESSRS YVILSFESKG DYMDMKQADN TQYVPMLEMS NASKYSDIQR PNYDHPPSQT
SSSEGEIDDK NEGLTTTDLL SFTYQVAKGM EFLASKNCVH RDLAARNVLL SQGKIVKICD
FGLARDIMHD NNYVSKGSTF LPVKWMAPES IFDNLYTTLS DVWSYGILLW EIFSLGGTPY
PGMVVDSSFY NKIKSGYRMS KPEHAPHDVY EMMMKCWNSE PEKRPSFLGL SDAVASLLPS
SYMRRVNREF LKSDHPAVTR VCMENDDAYI GITYKNQGKL KDRESGFDEQ RLSSDSGYII
PLPDLDPISD DEYGKRNRHS SQTSEESAIE TGSSSSTFAK REGETLEDIT LLEDMCLDCS
DLVEDSFL
//
