ID A0A164Z3T8_9CRUS Unreviewed; 1330 AA.
AC A0A164Z3T8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=APZ42_018316 {ECO:0000313|EMBL:KZS15911.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS15911.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS15911.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS15911.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS15911.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS15911.1}.
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DR EMBL; LRGB01000781; KZS15911.1; -; Genomic_DNA.
DR STRING; 35525.A0A164Z3T8; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd06263; MAM; 1.
DR CDD; cd05036; PTKc_ALK_LTK; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF604; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF12810; Gly_rich; 1.
DR Pfam; PF00629; MAM; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50060; MAM_2; 1.
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|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Kinase {ECO:0000313|EMBL:KZS15911.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|RuleBase:RU000312, ECO:0000313|EMBL:KZS15911.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Transferase {ECO:0000313|EMBL:KZS15911.1};
KW Transmembrane {ECO:0000256|RuleBase:RU000312, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 745..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 155..333
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 829..1108
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 466..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 863
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 120..138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1330 AA; 143073 MW; 2C0E966DCCDD7643 CRC64;
MDNPKAIELS SPWYQESGPY CKLSVALHMN NMEDGNLKIV VETRNHTWVI VETLGNGLRE
WRTLTQSVGR ISQPFRLKLE FTDGKKIPSH AAVDNIRLLS CLTEIPPNGH CDSAKRAFRC
DDGRCLPRDQ VCDISKDCPG GEDEDQDCDQ VLEGSRCDFE RGWCGWVNTL RDDLDWRRHN
GSTPTPQTGP GHDNTYKNST GMYVYVDMSE TRQLGNAAVL QSTRFPPPPK YHSNPASPYF
NSCQIRFFYH LYGPHIGDLV VRIVEEDPRY GRDNKSTDIW RESRNMGDMW HRAAVPLPPI
KNWYTIQFIG KRGIRFRGDT AIDDISLSPE CSGIGVPKNE TAGWPPDPAH YDEPKFIRYV
LTSCGAKGRV GPHQNQCTNA YQDSVTQVQV LSQGRLSGVQ VWTAPVTGLY TIIAKGASGG
LGPGGSGPTG SPGLAGYGAR VRAVFPFTAG TQIYFLVGQE GIAAVRDKPK DNHNRNSTET
GGGGSSNGET RRGGALERVR GLHNASNGAH GSGNGGGGGG ATFVFQMDSQ GIPIPLMVAA
GGGGIAAIGR FSPRPADLSL VHGKGFNSFL PRPGMSGQGN FKGAGGGGGW NGSAETEAVG
FSLLEGGLGG FSCNSKAEWP TYGGFGGGGG GCTNGEGGGG GGYNGGNAVA NSSGEGGYSF
VSLLAIERLT DVEEGQNAGP GSLDVMPAIA EGCGCEQLCI VLDPSLEEKQ CVCPIASAGE
WPTEDNVTKC AGFNSETGLL GTPHLIGTVV AAILIFVIFS IICFCLYTRY QRQQLAALRR
KAMAAPELQL SRLRGPSSSM VSEYNPNYEF GSGAPCSVQG LKEIPRENLR LVRALGQGAF
GEVYQGYLRH VAGDTVEMPV AVKVLQTLPE LSSNQTEMDF LMEAIIMSKF HHANIVHFIG
ICFDKHPRFI VLELLSGGDL KTFLRESRPK PERPSTLTMR DLLKCALDVA KGCRYLEENH
FIHRDIAARN CLLTTKGPGR VVKIADFGMS RDIYRADYYR KGGKAMLPVK WMPPEAFLEG
VFTSKTDVWS FGVLLWEVMS LGYMPYPGRG NQEVMQLVTG GGRLEAPPGC PGPVYRIMVH
CWHTNPEERP SFVTVLERIG YCMQDPDVLA MPIPVFQRPL SQERDTTIVP TGPSSSTNTS
DYLIPLTNNR SSSADLVSDS TGSIDGARRP SGSDQCGYWE TSFTREGVKA IARGEVVPDS
NGSAGNLSLG DLRSGSTKRR SKGYATVPTF EAPTLSQSQS SQPLLDTPPD SPTATDDGPN
SSSLNGRASN GDVLGPLDAT TLCRQSYANV RIVNPAAATS SIGNSNSSTP SRATPPTKAE
RSVKQNEISC
//
