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Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)

 M3WAV8_FELCA            Unreviewed;      1089 AA.
M3WAV8;
01-MAY-2013, integrated into UniProtKB/TrEMBL.
28-FEB-2018, sequence version 2.
10-OCT-2018, entry version 52.
RecName: Full=Platelet-derived growth factor receptor alpha {ECO:0000256|PIRNR:PIRNR500950};
Short=PDGF-R-alpha {ECO:0000256|PIRNR:PIRNR500950};
Short=PDGFR-alpha {ECO:0000256|PIRNR:PIRNR500950};
EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500950};
AltName: Full=Alpha platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500950};
AltName: Full=Alpha-type platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500950};
Name=PDGFRA {ECO:0000313|Ensembl:ENSFCAP00000008478};
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000008478, ECO:0000313|Proteomes:UP000011712};
[1] {ECO:0000313|Ensembl:ENSFCAP00000008478, ECO:0000313|Proteomes:UP000011712}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008478,
ECO:0000313|Proteomes:UP000011712};
PubMed=17975172; DOI=10.1101/gr.6380007;
Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N.,
Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U.,
Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N.,
Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.;
"Initial sequence and comparative analysis of the cat genome.";
Genome Res. 17:1675-1689(2007).
[2] {ECO:0000313|Ensembl:ENSFCAP00000008478}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008478};
Hillier L.W., Warren W., Obrien S., Wilson R.K.;
"Sequence assembly of the Felis catus genome version 6.2.";
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Ensembl:ENSFCAP00000008478}
IDENTIFICATION.
STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008478};
Ensembl;
Submitted (MAR-2013) to UniProtKB.
-!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface
receptor for PDGFA, PDGFB and PDGFC and plays an essential role in
the regulation of embryonic development, cell proliferation,
survival and chemotaxis. Depending on the context, promotes or
inhibits cell proliferation and cell migration. Plays an important
role in the differentiation of bone marrow-derived mesenchymal
stem cells. Required for normal skeleton development.
{ECO:0000256|PIRNR:PIRNR500950}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00701269}.
-!- ACTIVITY REGULATION: Present in an inactive conformation in the
absence of bound ligand. Binding of PDGFA and/or PDGFB leads to
dimerization and activation by autophosphorylation on tyrosine
residues. {ECO:0000256|PIRNR:PIRNR500950}.
-!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and
with heterodimers formed by PDGFA and PDGFB. Monomer in the
absence of bound ligand. {ECO:0000256|PIRNR:PIRNR500950}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000256|PIRNR:PIRNR500950}; Single-pass type I membrane
protein {ECO:0000256|PIRNR:PIRNR500950}. Membrane
{ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
protein {ECO:0000256|RuleBase:RU000311}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000256|PIRNR:PIRNR500950, ECO:0000256|RuleBase:RU000311}.
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EMBL; AANG04001605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_003985426.1; XM_003985377.3.
RefSeq; XP_006931182.1; XM_006931120.2.
RefSeq; XP_019685048.1; XM_019829489.1.
RefSeq; XP_019685049.1; XM_019829490.1.
RefSeq; XP_019685050.1; XM_019829491.1.
STRING; 9685.ENSFCAP00000008478; -.
Ensembl; ENSFCAT00000009145; ENSFCAP00000008478; ENSFCAG00000009141.
GeneID; 101090765; -.
KEGG; fca:101090765; -.
CTD; 5156; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
InParanoid; M3WAV8; -.
KO; K04363; -.
OMA; CKDIKKC; -.
OrthoDB; EOG091G01TL; -.
Proteomes; UP000011712; Chromosome B1.
Bgee; ENSFCAG00000009141; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IEA:Ensembl.
GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0001553; P:luteinization; IEA:Ensembl.
GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
GO; GO:0072277; P:metanephric glomerular capillary formation; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IEA:Ensembl.
GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027290; PDGFRA.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF07679; I-set; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SMART; SM00220; S_TKc; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|PIRSR:PIRSR500950-51, ECO:0000256|SAAS:SAAS00708816};
Cell membrane {ECO:0000256|PIRNR:PIRNR500950};
Chemotaxis {ECO:0000256|PIRNR:PIRNR500950};
Complete proteome {ECO:0000313|Proteomes:UP000011712};
Developmental protein {ECO:0000256|PIRNR:PIRNR500950};
Disulfide bond {ECO:0000256|PIRSR:PIRSR500950-52,
ECO:0000256|SAAS:SAAS00916669};
Immunoglobulin domain {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00941986};
Kinase {ECO:0000256|PIRNR:PIRNR500950, ECO:0000256|SAAS:SAAS00582553};
Membrane {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|PIRSR:PIRSR500950-51, ECO:0000256|SAAS:SAAS00708816};
Receptor {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|RuleBase:RU000311, ECO:0000256|SAAS:SAAS00600436};
Reference proteome {ECO:0000313|Proteomes:UP000011712};
Repeat {ECO:0000256|SAAS:SAAS00457685};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00582553};
Transmembrane {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00582553}.
SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
CHAIN 24 1089 Platelet-derived growth factor receptor
alpha. {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5014191139.
TRANSMEM 525 549 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1 113 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 202 306 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 593 954 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
NP_BIND 599 607 ATP. {ECO:0000256|PIRSR:PIRSR500950-51}.
ACT_SITE 818 818 Proton acceptor.
{ECO:0000256|PIRSR:PIRSR500950-50}.
BINDING 627 627 ATP. {ECO:0000256|PIRSR:PIRSR500950-51}.
DISULFID 49 100 {ECO:0000256|PIRSR:PIRSR500950-52}.
DISULFID 150 189 {ECO:0000256|PIRSR:PIRSR500950-52}.
DISULFID 235 290 {ECO:0000256|PIRSR:PIRSR500950-52}.
DISULFID 435 501 {ECO:0000256|PIRSR:PIRSR500950-52}.
SEQUENCE 1089 AA; 122845 MW; 6BE390B6D6FF0599 CRC64;
MGTSHLALLV LVCLLTGPSL ISCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP
MSEEENPNVE VRNEENNSGL FVTVLEVVNA SAAHTGLYTC YYNHTQTDEN EIEGRRIYIY
VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPKTPVT LRSSDGVVHA SYDSRQGFNG
TFSVGPYICE ATVSGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN
EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATKEVK
EMKKVTISVH EKGFIEIKPN FSPLEAVDLH EVKHFVVDVQ AYPPPRISWL KDNLTLIENL
TEITTDIEKI QEVRYRSKLK LIRAKEEDSG HYTIVVQNED DVKSYTFELL TQVPSSILDL
VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTVLANNIS NIITEVHRRD
RSTVEGRVTF TRVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII
SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSRHPEK PKKELDIFGL NPADESTRSY
VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSTSDSEVKN
LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
VDSTFYNKIK NGYRMAKPDH ATSEVYEIMV KCWHSEPEKR PSFYHLSEIV ENLLPGQYKK
SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKHEEDKL KDWEGSLDEQ RLSADSGYII
PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFV KREDETIEDI DMMDDIGIDS
SDLVEDSFL


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