UniProt: A0A7L3J7W5

Database: UniProt
Entry: A0A7L3J7W5_THACH

LinkDB:  A0A7L3J7W5_THACH 
Original site:  A0A7L3J7W5_THACH

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (28)   
   InterPro (15)   
   Pfam (5)   
   PROSITE (5)   
   SMART (3)   
All databases (40)   

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ID   A0A7L3J7W5_THACH        Unreviewed;      1093 AA.
AC   A0A7L3J7W5;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, entry version 22.
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};
DE   Flags: Fragment;
GN   Name=Pdgfra {ECO:0000313|EMBL:NXU24931.1};
GN   ORFNames=THACHL_R03271 {ECO:0000313|EMBL:NXU24931.1};
OS   Thalassarche chlororhynchos (Atlantic yellow-nosed albatross) (Diomedea
OS   chlororhynchos).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Procellariiformes;
OC   Diomedeidae; Thalassarche.
OX   NCBI_TaxID=54017 {ECO:0000313|EMBL:NXU24931.1, ECO:0000313|Proteomes:UP000556761};
RN   [1] {ECO:0000313|EMBL:NXU24931.1, ECO:0000313|Proteomes:UP000556761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-DU-029-24 {ECO:0000313|EMBL:NXU24931.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXU24931.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-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       Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Golgi
CC       apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC       {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC       {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:NXU24931.1}.
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DR   EMBL; VZTW01018368; NXU24931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7L3J7W5; -.
DR   OrthoDB; 9936425at2759; -.
DR   Proteomes; UP000556761; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:TreeGrafter.
DR   CDD; cd05859; Ig4_PDGFR; 1.
DR   FunFam; 1.10.510.10:FF:002211; -; 1.
DR   FunFam; 2.60.40.10:FF:000720; Platelet-derived growth factor receptor alpha; 1.
DR   FunFam; 2.60.40.10:FF:000725; Platelet-derived growth factor receptor alpha; 1.
DR   FunFam; 2.60.40.10:FF:000776; Platelet-derived growth factor receptor alpha; 1.
DR   FunFam; 2.60.40.10:FF:000832; Platelet-derived growth factor receptor alpha; 1.
DR   FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR   FunFam; 2.60.40.10:FF:000223; Platelet-derived growth factor receptor beta; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
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; 2.
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; 4.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
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   Cell projection {ECO:0000256|ARBA:ARBA00023273};
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   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000556761};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..1093
FT                   /note="Platelet-derived growth factor receptor alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5029734788"
FT   TRANSMEM        525..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        878..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          215..306
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          593..983
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1023..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        818
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         572
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         599..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT   BINDING         600..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         675..681
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         822
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         823
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         836
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   DISULFID        49..99
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   DISULFID        149..189
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   DISULFID        235..290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   DISULFID        435..501
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXU24931.1"
FT   NON_TER         1093
FT                   /evidence="ECO:0000313|EMBL:NXU24931.1"
SQ   SEQUENCE   1093 AA;  123700 MW;  8E163D599691DD0F CRC64;
     MGTSPRTFLI LGCFLTGPFL TFCQLPLPTI VPNRNEMVVQ LNSNFTLKCS GDSEVSWQYP
     VTEGSHRIDI RHEENNSGLF VTVLEVGNAS AAHTGLYVCY YNHTQVEDGE VEGKDIYIYV
     PDPDMPFVPS IPEDQFILVE EGDPTVIPCR TSDPNAQVTL INSLDKAVYA FYDSKQGFIG
     NFPAGSYTCK TMVKGVEFKS DEFLIYILRA TSQLPVEIEA LKTVYKTGET IVVTCVVFDN
     EVVNLQWNYP GKVKEKGLIK LDDIKVPSQK LVYTLTIPEA SVKDTGDYEC TARHATKEVK
     ENKKVVITVH DKGFIHLEPQ FSPLEAVNLH EVKNFVVDVQ AYPAPKMYWL KDNVTLIENL
     TEIVTSSNRV QETRFQSILK LIRAKEEDSG YYTLVVENED EIKRYTFSLL IQVPALILDL
     VDDHHGSAGG QTVRCLAEGT PLPDVEWLVC KDIKKCSNDT SWTLLTNNIS DIHMEAHLDE
     KNMVESQVTF QKVEETLAVR CVARNDLGAV TRELKLVAPT LRSELTVAAA VLVLLVIVII
     SLIVLVIIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG
     SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL
     LGACTKSGPI YIITEYCFYG DLVNYLHKNR DNFLSRHPEK PKKDLDIFGM NPADESTRSY
     VILSFENTGE YMDMKQADTT QYVPMLERKE GSKYSDIQRS VYDRPASYKK KSMSESEVKN
     LLSDDSSEGL SLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA
     RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGMYLIKLFQ
     FKLFYVKYFK FYSKNICVKS AVSYSSIWGF GSQLAGLKQS LHIHLQKSLI FSGLMNHSYP
     FEERQPYYEK IHLDFLKSDH PAVTRMRGDC DNAYIGVTYK NEDKLKDRES GFDEQRLSAD
     SGYIIPLPDI DPVSEDELGK RNRHSSQTSE ESAIETGSSS STFIKREDET IEDIDMMDDI
     GIDSSDLVED SFL
//

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