ID A0A8J5ZRP9_GALPY Unreviewed; 1280 AA.
AC A0A8J5ZRP9;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Fragment;
GN ORFNames=J0S82_017527 {ECO:0000313|EMBL:KAG8504942.1};
OS Galemys pyrenaicus (Iberian desman) (Pyrenean desman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Talpidae; Galemys.
OX NCBI_TaxID=202257 {ECO:0000313|EMBL:KAG8504942.1, ECO:0000313|Proteomes:UP000700334};
RN [1] {ECO:0000313|EMBL:KAG8504942.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBE-C5619 {ECO:0000313|EMBL:KAG8504942.1};
RX PubMed=34295371;
RA Escoda L., Castresana J.;
RT "The genome of the Pyrenean desman and the effects of bottlenecks and
RT inbreeding on the genomic landscape of an endangered species.";
RL Evol. Appl. 14:1898-1913(2021).
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}.
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:KAG8504942.1}.
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DR EMBL; JAGFMF010012279; KAG8504942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J5ZRP9; -.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP000700334; 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:TreeGrafter.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:TreeGrafter.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:TreeGrafter.
DR CDD; cd05859; Ig4_PDGFR; 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; 2.60.40.10:FF:000223; Platelet-derived growth factor receptor beta; 1.
DR FunFam; 1.10.510.10:FF:001927; Receptor protein-tyrosine kinase; 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; 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 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; 2.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW 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:0000313|EMBL:KAG8504942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000700334};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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}.
FT TRANSMEM 680..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..268
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 383..461
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 748..1145
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1280
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 958
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 755..762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 782
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 793..799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 962
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 963
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 976
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1153
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG8504942.1"
SQ SEQUENCE 1280 AA; 143638 MW; F736C77BB3CDF3AB CRC64;
PGPQERKELQ KKHAKVLSGT RIWAPHPEKI RSQIGSLSIV NGWSVPSRQS GGSVGAHGLA
HISRRDAKGL KWSSGGKKEE EEETMSTKLC KVSAENNANA QRRAWGAAAA AALSPECGGL
GRGTPERAPR SDLAAEARLT PVTSTPVVPF LPLFVDFSET RDLSPTVFPF TGPSLILCQL
SFPSILPNEN EKVVQLNSSF SLRCFGESEV SWQYPTSEEE NPNVEVRNEE NNSGLFVSVL
EVVGAVAAHT GLYTCYYNHT QTEEGEIEGR NIYIYVPDPE IAFVPLKLTD YLVLAEDDDS
AVIPCRTTDP ETPVTLLNGD GVVQASYDSR QGFNGTFTVG PYICEATVKG RKFQTITFNV
YALKATSELD LEMEALKTVY KSGEKIVVTC VVFNNEVVDL QWAYPGQVKG KGIHKLEEIK
VPFIKLVYTL MVPDATVKDS GEYECAARQA TKEVKEMKKV TISVHEKGFI EIKPTFSQLE
TVNLHEVKHF VVDVQAYPPP RISWLKDNLT LIENLTEITT DVEKIQEIRY RSKLKLIRAK
EEDSGHYTII VQNEDDVKSY TFQLLTQVPS SILDLVDDHH ASTGGQTVRC TAEGTPLPEI
EWMICKDIKK CNNETSWTVL SNNISNIVTE LHARDRSTVE GQVMFAKVEE TIAVRCLARN
PLGTENRELK LVAPSLRSEL TVAAAVLVLL VIVIISLIVL VVIWKQKPRY EIRWRVIESI
SPDGHEYIYV DPMQLPYDSR WEFPRDGLVL GRILGSGAFG KVVEGTAYGL SRSQPVMKVA
VKMLKRPIYI ITEYCFYGDL VNYLHKNRDS FLSHHPEKPK KELDIFGLNP TDESTRSYVI
LSFENNGDYM DMKQADTTQY VPMLERKEVS KYSDIQRSLY DRPASYKKKS LLGNCLHSLR
GRCDLGLQDA GDADDSEVKN LLSDENSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA
ARNVLLAQGK IVKICDFGLA RDIMHDSNYV SKGSGTGQVL SDLGRRVTEE SWSPRRLFQA
FIALYIREDT AGVPTGFNFF PPSLQTFLPV KWMAPESIFD NLYTTLSDVW SYGILLWEIF
SLGGTPYPGM MVDSTFYNKI KSGYRMAKPD HATSEVYEIM VKCWNSEPEK RPSFYHLSEI
VENLLPGQYK KSYEKIHLDF LKSDHPAVAR MRVDPDNAYI GVTYKNEEDK LKDWEGGLDE
QRLSADSGYI IPLPDIDPVP EEEDLGKRNR HSSQTSEESA IETGSSSSTF IKREDETIED
IDMMDDIGID SSDLVEDSFL
//
