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Database: UniProt
Entry: A0A2I3SPB0_PANTR
LinkDB: A0A2I3SPB0_PANTR
Original site: A0A2I3SPB0_PANTR 
ID   A0A2I3SPB0_PANTR        Unreviewed;      1351 AA.
AC   A0A2I3SPB0; A0A2J8P970;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-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:ENSPTRP00000078837.1,
GN   ECO:0000313|VGNC:VGNC:2431};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000078837.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000078837.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000078837.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   EMBL; AACZ04000317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016796611.1; XM_016941122.1.
DR   Ensembl; ENSPTRT00000096985.1; ENSPTRP00000078837.1; ENSPTRG00000014941.4.
DR   GeneID; 744480; -.
DR   CTD; 4486; -.
DR   VGNC; VGNC:2431; MST1R.
DR   GeneTree; ENSGT00940000157842; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000002277; Chromosome 3.
DR   Bgee; ENSPTRG00000014941; Expressed in thymus and 11 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|PIRSR:PIRSR000617-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
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:UP000002277};
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..1351
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015081652"
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          1033..1296
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1318..1351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT   BINDING         1039..1047
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT   BINDING         1065
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1112..1115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT   BINDING         1163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT   MOD_RES         1189
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT   MOD_RES         1190
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT   MOD_RES         1304
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT   MOD_RES         1311
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   1351 AA;  147282 MW;  155BBA4D21955B57 CRC64;
     MELLPPLPQS FLLLLLLPAK PAAGEDWQCP RTPYAASRDF DVKYVVPSFS AGGLVQAMVT
     YEGDRNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG CQTCAACGPG PHGPPGDTDT
     KVLVLDPALP ALVSCGSSLQ GRCFLHDLEP QGTAVHLAAP ACLFSAHHNR PDDCPDCVAS
     PLGTRVTVVE QGQASYFYVA SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK
     HLVSYSIEYV HSFHTGAFVY FLTVQPASVT DDPSALHTRL ARLSATEPEL GDYRELVLDC
     RFAPKRRRRG APEGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF VTGKDGGPGV
     GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF FQSPSFCPNP PGLEALSPNT
     SCRHFPLLVS SSFSRVDLFN GLLGPVQVTA LYVTRLDNVT VAHMGTMDGR ILQVELVRSL
     NYLLYVSNFS LGDSGQPVQR DVSRLGDHLL FASGDQVFQV PIRGPGCRHF LTCGRCLRAW
     HFMGCGWCGN MCSQQKECPG SWQQDHCPPK LTEFHPHSGP LRGSTRLTLC GSNFYLHPSG
     LVPEGTHQVT VGQSPCRPLP KDSSKLRPVP RKDFVEEFEC ELEPLGTQAV GPTNVSLTVT
     NMPPGKHFRV DGTSVLRGFS FMEPVLIAVQ PLFGPRAGGT CLTLEGQSLS VGTSRAVLVN
     GTECLLERVS EGQLLCATPP GATVASVPLS LQVGGAQVPG SWTFQYREDP VVLSISPNCG
     YINSHITICG QHLTSAWHLV LSFHDGLRAV ESRCERQLPE QQLCRLPEYV VRDPQGWVAG
     NLSARGDGAA GFTLPGFRFL PPPHPPSANL VPLKPEEHAI KFEVCVDGEC HILGRVVRPG
     PDGVPQSTLL GILLPLLLLV AALATALVFS YWWRRKQLVL PPNLNDLASL DQTAGATPLP
     ILYSGSDYRS GLALPAIDGL DSTTCVHGAS FSDSEDESCV PLLWKESIQL RDLDSALLAE
     VKDVLIPHER VVTHSDRVIG KGHFGVVYHG EYIDQAQNRI QCAIKSLSRI TEMQQVEAFL
     REGLLMRGLN HLNVLALIGI MLPPEGLPHV LLPYMCHGDL LQFIRSPQRN PTVKDLISFG
     LQVARGMEYL AEQKFVHRDL AARNCMLDES FTVKVADFGL ARDILDREYY SVQQHRHARL
     PVKWMALESL QTYRFTTKSD VWSFGVLLWE LLTRGAPPYR HIDPFDLTHF LAQGRRLPQP
     EYCPDSLYQV MQQCWEADPA VRPTFGVLVG EVEQIVSALL GDHYVQLPAT YMNLGPSTSH
     EMNVRPEQPQ FSPMPGNVRR PRPLSEPPQP T
//
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