ID E1BCZ6_BOVIN Unreviewed; 1401 AA.
AC E1BCZ6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=MST1R {ECO:0000313|Ensembl:ENSBTAP00000020028.4,
GN ECO:0000313|VGNC:VGNC:31708};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000020028.4, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000020028.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020028.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000020028.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020028.4};
RG Ensembl;
RL Submitted (NOV-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}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the plexin family.
CC {ECO:0000256|ARBA:ARBA00010297}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR SMR; E1BCZ6; -.
DR STRING; 9913.ENSBTAP00000020028; -.
DR PaxDb; 9913-ENSBTAP00000020028; -.
DR Ensembl; ENSBTAT00000020028.4; ENSBTAP00000020028.4; ENSBTAG00000015046.4.
DR VEuPathDB; HostDB:ENSBTAG00000015046; -.
DR VGNC; VGNC:31708; MST1R.
DR eggNOG; KOG1095; Eukaryota.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT00940000157842; -.
DR HOGENOM; CLU_005158_0_0_1; -.
DR InParanoid; E1BCZ6; -.
DR OMA; NISCRHF; -.
DR OrthoDB; 1614410at2759; -.
DR TreeFam; TF317402; -.
DR Reactome; R-BTA-8852405; Signaling by MST1.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000015046; Expressed in digestive system secreted substance and 84 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0005773; C:vacuole; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00102; IPT; 1.
DR CDD; cd01179; IPT_plexin_repeat2; 1.
DR CDD; cd05058; PTKc_Met_Ron; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR24416:SF113; MACROPHAGE-STIMULATING PROTEIN RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF81296; E set domains; 3.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000617-
KW 2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000617-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000617-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1401
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018763736"
FT TRANSMEM 961..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..525
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT DOMAIN 1083..1344
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1025..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1209
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT BINDING 1089..1097
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1162..1165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT MOD_RES 1239
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1240
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1354
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1361
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT DISULFID 105..108
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 111..166
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 139..147
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 177..180
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 303..370
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 388..410
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 389..425
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 530..548
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 536..570
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 539..555
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 551..561
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
SQ SEQUENCE 1401 AA; 151790 MW; F395DA31C067A84A CRC64;
MELHPPLFQP FLLLLLLLPT LPAVPETGGS WQCPRIPYAA SRDFAVEYSV PSFSAGGPVQ
AVATYEGGRE GSAVFVATRN RLHVLGPDLQ PVESLATGPA GAPGCQTCAA CGPGPHGPPG
DTDTQVLVLE PALPALISCG SSLRGRCFLH ELEPGGTALH LAPPVCLFSE HNRPEDCPDC
VASPLGTLVT VVEQGQASYL YVASSLDSAV AASFSPLSVS IRRLKADGSG FAAGFAALSV
LPQHLDSYRI EYVYSFHAGA FVYFLTVQPA DVAAAPGTLH TRLARLSAVE TDLGDYRELV
LHCHFAPKRR RRAAHEGGQP YPVLRAAHAA PVGGHLAAEL SIPEGQEVLF GVFSASRDSS
PGADPNSVVC AFPVHLLDTL IEKGVEHCCE PPVPPGLRRG LDFFQLPSFC PDAPGLGASS
PNISCRHFPL LVSGNLLRVD LFNGLLGPVE VTALYVTRLD NVTVAHMGTA DGRILQVELA
RSLNYLLYVS NFSLGSNGQP VHRDVRRLGD HLLFASGDQV FQVPIRGPGC RHFLTCGRCL
RAQRFMGCGW CGGMCGRQKE CPGSWQQDYC PPVLTEFYPR SGPLRGSTRL TLCGSNFYLY
PSGLVPEGTH QVTVGRSPCR LLPKGNSDLS RLPRKDFIED FECELEPLST QVAGPANVSL
TVTNMPLGRH FRVEGTSMLG GFSFMEPVLT AVRPFFGPRA GGTCLTLEGR GLSIGTSQTV
LVNGTECPLK QVSEGQLLCT TPPGAATASV PIRLQVGGAE VPGSWNFHYR EDPIVLGISP
KCGYTGSHVT IRGQHLTSAW HLTLSFHDGV RAVENRCEGQ LPEQHRCRLP EYVVRGRRGW
VTGNLSVRGD GAPGYTLPGF RFLPPPHPPS KDLAPLKPEE HAIKFEYIGL GTVADCVAVN
VTVSGKSCQH ELRGDVVVCP LPPSLQLGKD GAPLQVCVDG RCYTLGKVVR PGLEGVPQST
LLGVLLALLL LVAVLAAILV FSYRWRKQLV LSSNLEDLAS LDRTPGAMPL PLLRSGSDYR
NGLAPPITGQ DSSTQVHRIS SSDSGDGSRV PLLRKGSIQL GDLDSVLLSE VKDVLIPHER
VVTHADRVIG KGHFGVVYHG EYKDEAQNRI HCAIKSLSRI TEVQEVEAFL REGLLMRRLH
HPNVLALIGI VLPPEGLPRV LLPYMRHGDL LQFIRSPQRN PTVKDLISFG LQVAHGMEYL
AEQKFVHRDL AARNCMLDES FTVKVADFGL ARDVLDKEYY SVQQHRHARL PVKWMALESL
QTYRFTTKSD VWSYGVLLWE LLTRGAPPYP HIDPFDLTHF LAQGRRLPQP EYCPDSLYTV
MQHCWAADPM ARPTFGELAG EVALVVAALR GDHYVQLPVA YVNVGPGAPD KAIMPLEQSP
SPTVHRSPGR PRPLSEPLRP T
//
