ID M3Y133_MUSPF Unreviewed; 974 AA.
AC M3Y133;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=FLT3 {ECO:0000313|Ensembl:ENSMPUP00000005034.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000005034.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000005034.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, 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}.
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DR EMBL; AEYP01084857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01084858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004774881.1; XM_004774824.2.
DR RefSeq; XP_012902448.1; XM_013046994.1.
DR RefSeq; XP_012902449.1; XM_013046995.1.
DR AlphaFoldDB; M3Y133; -.
DR STRING; 9669.ENSMPUP00000005034; -.
DR Ensembl; ENSMPUT00000005119.1; ENSMPUP00000005034.1; ENSMPUG00000005073.1.
DR KEGG; mpuf:101685779; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000160575; -.
DR HOGENOM; CLU_000288_49_1_1; -.
DR InParanoid; M3Y133; -.
DR OMA; NSQGESC; -.
DR OrthoDB; 1614410at2759; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR PANTHER; PTHR24416:SF356; RECEPTOR-TYPE TYROSINE-PROTEIN KINASE FLT3; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|RuleBase:RU000311};
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
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}.
FT TRANSMEM 523..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 654..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 234..324
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 591..924
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 792
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 598..605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 673..679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 796
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 797
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 810
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 974 AA; 110782 MW; EBE53D8C4C0CEA02 CRC64;
MIFETITNQD LPVIKCVLIN HKNNDSSLGI SSSYPMASET PEDLGCALKS ESTEAVYGAA
TVEVDMLASI TLQVLVNTPG NISCLWVFKH SSLNCQPHFD LQNRGVVSMV ILKMTETQAG
EYLLFIQTEA TNYTILFTVS IRNTLLYTLR RPYFRKMENQ DALVCISESI PEPTVEWVFC
NAQSESCKGE SAAVVTKEES VLYELFGTDI RCCARNELGR ECTKLFTIDL NQTPQTTPPQ
LFLKVGEPLW IRCKAVHVNH GFGLSWELEN KALGEGSSFE MSTYSTNRTM IRILFAFVSS
VGRNDTGYYT CSSSEHPSKS ALVTILEKGF INGSKSSEDY EIDQYEEFCF SVRFKAYPQI
RCTWTFSRKS FPCEQRGLDD GSSISKFCNH KHQPGEYIFH AENDDAEFTK MFTLNIRRKP
QVLAKTSASQ ASCSSDGYPL PSWTWKKCSD KSPNCTEEIT EGIWNKKANR KVFGQWLSSS
TLNMSEAVKG FLVKCCAYNS LGTSCETILL NSPGPFPFIQ DNISFYATVG LCLPFIAILT
MLICHKYKKQ FRYESQLQMV QVTGSLDNEY FYVDFREYEY DIKWEFPREN LEFGKVLGSG
AFGKVMNATA YGISKTGVSI QVAVKMLKEK ADSSEREALM SELKMMTHLG NHENIVNLLG
ACTLSGPIYL IFEYCCYGDL LNYLRNKREK FHRTWTEIFK EHNFSFYPTF QSHPSSSMPG
SREVQLHQDS DHISGFNGNS FQSEDEIEYE NQKRLEEEED LNVLTFEDLL CFAYQVAKGM
EFLEFKSCVH RDLAARNVLV THGKVVKICD FGLARDIMSD SNYVIRGNAR LPVKWMAPES
LFQGIYTIKS DVWSYGILLW EIFSLGVNPY PGIPVDANFY KLIQSGFKMD QPFYATEEIY
FIMQSCWAFD SRKRPSFPNL TSFLGCQLAD AEEAMYQNME GHVSDRSSVY QNRRPYSREV
DSGLLPPQAH DEDS
//
