ID A0A2K5VT19_MACFA Unreviewed; 1350 AA.
AC A0A2K5VT19;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:ENSMFAP00000027925.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000027925.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000027925.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000027925.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSMFAT00000002111.2; ENSMFAP00000027925.1; ENSMFAG00000045229.2.
DR VEuPathDB; HostDB:ENSMFAG00000045229; -.
DR GeneTree; ENSGT00940000157842; -.
DR Proteomes; UP000233100; Chromosome 2.
DR Bgee; ENSMFAG00000045229; Expressed in colon and 7 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00102; IPT; 1.
DR CDD; cd01180; IPT_plexin_repeat1; 1.
DR CDD; cd01179; IPT_plexin_repeat2; 1.
DR CDD; cd05058; PTKc_Met_Ron; 1.
DR CDD; cd11279; Sema_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; IPR039413; RON_Sema.
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; 2.
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:ARBA00023137};
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:UP000233100};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1350
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014323468"
FT TRANSMEM 909..933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..522
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT DOMAIN 1032..1295
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1315..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1158
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT BINDING 1038..1046
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1064
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1111..1114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT MOD_RES 1188
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1189
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1303
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1310
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT DISULFID 101..104
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 107..162
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 135..143
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 174..177
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 300..367
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 385..407
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 386..422
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 527..545
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 533..567
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 536..552
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 548..558
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
SQ SEQUENCE 1350 AA; 146918 MW; 503074C39C651E63 CRC64;
MELLPPLPQS FLLLLLLPAK PAAAKEWQCP RTPYAASRDF NVKYMVPSFS AGGLVQTMVT
YQGDKNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG CQTCAACGPG PHGPSGDTDT
KVLVLEPALP ALVSCGSSLQ GRCFLHDLDP QGTAVHLAAP ACLFSAHHNR PDDCPDCVAS
PLGTRVTVVE QGQASYFYVA SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK
HLVSYSIEYV HSFHTGAFVY FLTVQPASVT DAPGALHTRL ARLSATEPEL GDYRELVLDC
RFAPKRRRRG APEGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF VAGKDSGPGV
GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF FQSPSFCPNP PGLEAPSPNT
SCRHFPLLVS SSFSRVDLFN GLLGTVEVTA LYVTRLDNVT VAHMGTADGR ILQVELARSL
NYLLYVSNFS LGDSGQPVQR DVSRLGDHLF FASGDQVFQV PIQGPGCRHF LTCGRCLRAQ
RFMGCGWCGN MCGRQKECPG SWQQDHCPPK LTEFHPHSGP LRGSTRLTLC GSNFYLHPSG
LVPEGTHQIT VGQSPCRPLP KDSSKLRPVP RKDFVEEFEC ELEPLGTQAV GPTNVSLTVT
NMPPGKHFRV DGTSMLRGFF FMEPVLIAVQ PLFGPRAGGT CLTLEGQSLS VGTSRAVLVN
GTECLLARVS EGQLLCATPP GAMVASVPLS LQVGGAQVPG SWTFHYREDP VVLSISPNCG
YSNSHITICG QHLTSAWHLV LSFHDGLRAV ESRCERQLPE QQLCRLPEYV VQDPQGWVAG
NLSAWGDGAA GFTLPGFRFL TPPHPPSANL IPLKPEEHAI KFEVCVDGEC HILGRVVWPG
PDGVPQSTLL GILLPLLLLV AALATALVFS YWWQRKQLVL PPNLDDLASL DQTTGATPLP
ILYSGSDYRS GLARPATDGL DSTCVHGASF SNSEDESCVP LLRKESIQLR DLDSALLAEV
KDVLIPHERV VTHSDRVIGK GHFGVVYHGE YIDQAQNRIQ CAIKSLSRIT EMQQVEAFLR
EGLLMRGLNH PNVLALIGIM LPPEGLPHVL LPYMCHGDLL QFIRSPQRNP TVKDLISFGL
QVAHGMEYLA EQKFVHRDLA ARNCMLDESF TVKVADFGLA RDILDKEYYS VRQHRHARLP
VKWMALESLQ TYRFTTKSDV WSFGVLLWEL LTRGAPPYPH IDPFDLTHFL AQGRRLPQPE
YCPNSLYQVM QQCWEADPAA RPTFGVLVGE VEQIVSALLG DHYVQLPATY MNLGPSTSHE
MNVHPEQQQS SPMPGSAHRP RPLSEPPRPT
//
