ID A0A2K5YGQ4_MANLE Unreviewed; 1403 AA.
AC A0A2K5YGQ4;
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:ENSMLEP00000014705.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000014705.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000014705.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 9568.ENSMLEP00000014705; -.
DR Ensembl; ENSMLET00000038156.1; ENSMLEP00000014705.1; ENSMLEG00000031418.1.
DR GeneTree; ENSGT00940000157842; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IEA:UniProtKB-EC.
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; 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; 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: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:UP000233140};
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..1403
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014363973"
FT TRANSMEM 962..986
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..526
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT DOMAIN 1085..1348
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1368..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT BINDING 1091..1099
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1164..1167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT MOD_RES 1241
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1242
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1356
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1363
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 531..549
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 537..571
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 540..556
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 552..562
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
SQ SEQUENCE 1403 AA; 152435 MW; D93F1A3535B62E4E CRC64;
MELLPPLPQS FLLLLLLPAK PAAAKEWQCP RTPYAASRDF NVKYMVPSFS AGGLVQAMVT
YQGDKNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG CQTCAACGPG PHGPSGDTDT
KVLVLEPALP ALVSCGSSLQ GRCFLHDLDP QGTAVHLAAP ACLFSAHHNQ PDDCPDCVAS
PLGTRVTVVE QGQASYFYVA SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK
HLVSYSIEYV HSFHTGAFVY FLTVQPASVT DAPGALHTRL ARLSATEPEL GDYRELVLDC
RFAPKRRRRG APKGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF VAGKDSGPGV
GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF FQSPSFCPNP PGLEAPSPNT
SCRHFPLLVS SSFSRVDLFN GLLGTVEVTA LYVTRLDNVT VAHMGTADGR ILQVELARSL
NYLLYVSNFS LGDSGQPVQR DVSRLGDHLF FVRWAGAGPG VFQVPIQGPG CRHFLTCGRC
LRAQRFMGCG WCGNMCGRQK ECPGSWQQDH CPPKLTEFHP HSGPLRGSTR LTLCGSNFYL
HPSGLVPEGT HQITVGQSPC RPLPKDSSKL RPVPRKDFVE EFECELEPLG TQAVGPTNVS
LTVTNMPPGK HFRVDGTSML RGFFFMEPVL ISVQPLFGPR AGGTRLTLEG QSLSVGTSRA
VLVNGTDCLL ARVSEGQLLC ATPPGAMVAS VPLSLQVGGA QVPGSWTFHY REDPVVLSIS
PNCGYSNSHI TICGQHLTSA WHLVLSFHDG LRAVESRCER QLPEQQLCRL PEYVVRDPQG
WVAGNLSAWG DGAAGFTLPG FRFLTPPHPP SANLIPLKPE EHAIKFEYIG LAAVTNCVGV
NVTVGGESCQ HEFRGDMVVC PLPPSLQLGK DGAPLQVCVD GECRILGRVV WPGPDGVPQS
TLLGILLPLL LLVAALATAL VFSYWWQRKQ LVLPPNLDDL ASLDQTAGAT PLPILYSDSD
YRSGLARPAT DGLDSTCVHG ASFSNSEDES CVPLLRKESI QLRDLDSVLL AEVKDVLIPH
ERVVTHSDRV IGKGHFGVVY HGEYIDQAQN RIQCAIKSLS RITEMQQVEA FLREGLLMRG
LNHPNVLALI GIMLPPEGLP HVLLPYMCHG DLLQFIRSPQ RNPTVKDLIS FGLQVAHGME
YLAEQKFVHR DLAARNCMLD ESFTVKVADF GLARDILDKE YYSVRQHRHA RLPVKWMALE
SLQTYRFTTK SDVWSFGVLL WELLTRGAPP YPHIDPFDLT HFLAQGRRLP QPEYCPNSLY
QVMQQCWEAD PAARPTFGVL VGEVEQIVSA LLGDHYVQLP ATYMNLGPST SHEMNVHPEQ
QQSSPMPGSA HRPRPLSEPP RPT
//
