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Database: UniProt
Entry: A0A3Q3BJC8_KRYMA
LinkDB: A0A3Q3BJC8_KRYMA
Original site: A0A3Q3BJC8_KRYMA 
ID   A0A3Q3BJC8_KRYMA        Unreviewed;      1367 AA.
AC   A0A3Q3BJC8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029985.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000029985.1}
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         ECO:0000256|RuleBase:RU000312};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000312}.
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DR   RefSeq; XP_017262483.1; XM_017406994.1.
DR   STRING; 37003.ENSKMAP00000029985; -.
DR   Ensembl; ENSKMAT00000030355.1; ENSKMAP00000029985.1; ENSKMAG00000022163.1.
DR   GeneID; 108230621; -.
DR   KEGG; kmr:108230621; -.
DR   CTD; 245700; -.
DR   GeneTree; ENSGT00940000155404; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043009; P:chordate embryonic development; IEA:Ensembl.
DR   GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR   GO; GO:0006096; P:glycolytic process; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05061; PTKc_InsR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040969; Insulin_TMD.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-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; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF17870; Insulin_TMD; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00261; FU; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; 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:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000312};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        943..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          624..724
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          842..939
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1007..1283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1308..1367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1144
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         1017
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1041
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1088..1094
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1148..1149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1367 AA;  154124 MW;  7AADCCA94B562B92 CRC64;
     MRRLTLKLRS QMVFFIICTC IICHCGLITG EICQSKDIRN NVTNLQSLEN CTIIEGHLKI
     LLMFKTKTED FQGLSYPKLR VVTDYVLLFR VYGLETLTDL FPNLTVIRGN NLFFNYALVI
     YEMLQLKEMG LHSLMNITRG AVRIEKNPDL CYLATLDWSK VLDSVEDNYI VSNKNERECG
     DVCPGTAQGQ TICISTAING HFRGRCWSQN YCQKICHDKC KHGACSPEGH CCHDQCLGGC
     SETGNASSCV ACRNLLHGNT CVEKCPPGYY VFNGWRCVSF SFCQDLHNQC ADIKKQQDQE
     AGCSKYVIHN GACIPECPSG YSSLNSTRLM CEPCAGPCPK ECKGNMTIDS VTSAQALRGC
     TIIEGNMIIK IRGGTNIAAE LEASLGQIEI IKGYLSIRRA YALVSLSFLR KLRLIKGEQL
     ELEFYAFHAL DNQNLHQLWD WSKHNLTIER GRMFFHYNSK LCMAEITKME EVTGTKERNQ
     KNDIALRTNG DQASCETKTL NFTSVKPSHN MIILRWTSFW PTDFRDLLGF MVLYKEAPYR
     NVTEFDGQDA CGSNSWVIVD VDPPPRGTDN KKGEDPAYLI RPLKPWTQYA IMVKTQLSAP
     DERQVYGAKS KIIYVRTNAF SPSVPLDPIS SSNSSSQIIL KWKPPNSPNG NITHYRVICR
     QQPEDSDLYK FDYCLQGMKP PSRIPTHLDI EEEQKWNHTD DSTSEGKCCT CPLTKSQIEK
     EQQEIEYRKT FENYLHNEVF ERRLTRDRRS VDYPGPTGSS VLFTTIPSLH LGSTSASSTH
     EDKNDKVELN VTSESAVISN LQHFTSYKIE IIACNHPEDP KRCSLATFVS ARTMPEVKAD
     DIPGPVTHEV QTGEAPSVLI KWNAPPSPNG LIILYEVFYR KVGDTEVHTS CVSRPAYSRA
     GGTKLHLVHH GNYSVRVRAT SLAGNGSFTE TVYFFMPNSD PGLVWIVIGP VICFVLLLIA
     ASGVFYIIRK KQIEGPLGDL ITSPNPEYFS ASDMYVPDEW EVPRDKITLL RELGQGSFGM
     VYEGIAQDIV KGEPETRVAI KTVNESASLR ERIEFLNEAS VMKAFSCHHV VRLLGVVSKG
     QPTLVVMELM IHGDLKSYLR SLRPDSENNP TGSPPPTLKD MLQMAAEIAD GMAYLNAKKF
     VHRDLAARNC MVAEDFTVKI GDFGMTRDIY ETDYYRKGGK GLLPVRWMAP ESLKDGVFTA
     HSDCWSFGVV LWEISTLAEQ PYQGLSNEQV LKFVMDGGYL DRPDNCPERI HNLMQMSWQY
     NPKMRPTFLE IIEMLRDDLH PSFQEVSFFY SEENKVPETE DFDLDLDNME SIPLDPSSYS
     QREESLGRDS GPSVALRGNY EEHVPYTHMN GGKKNGRILS LPRSSPS
//
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