ID A0A2A3ESY9_APICC Unreviewed; 4096 AA.
AC A0A2A3ESY9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=APICC_02832 {ECO:0000313|EMBL:PBC34259.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC34259.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC34259.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC34259.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-2014) 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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 EMBL; KZ288192; PBC34259.1; -; Genomic_DNA.
DR STRING; 94128.A0A2A3ESY9; -.
DR Proteomes; UP000242457; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00992; PDZ_signaling; 3.
DR CDD; cd05032; PTKc_InsR_like; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_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; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF525; INSULIN-LIKE RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF13347; MFS_2; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00228; PDZ; 3.
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; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50106; PDZ; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000242457};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000312};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1254..1276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1146..1248
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1315..1608
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 3878..3963
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 4006..4078
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1759..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2079..2185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2222..2249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2343..2372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2400..2437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2461..2614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2630..2649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2735..2781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2918..2938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3040..3077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3241..3276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3290..3361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3378..3427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3512..3543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3568..3645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3684..3710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2093..2107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2222..2244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2348..2365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2400..2428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2467..2496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2512..2545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2556..2582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2753..2781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3241..3258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3303..3320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3321..3361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3568..3599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3690..3710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 4096 AA; 453897 MW; DED5D3F384B50F03 CRC64;
MPKRIFINHK KKTQSSIQLN VKTFFESYQD RKFGMESSKM ENAEEQSPLL ERKISTSTKI
AYALGHIFND LTAAMWFSYT LIYFQRVVLL EPIVAGALLL LGQIIDAFMT PVFGVLVDRY
LKKKIWHIIG SVMVTLSFPV IFGGFSKSSH VSIMLLYVAS IAVFQTGWAA VQISHLSMIP
ALTNSLLARA DLTAIRYSAQ VGSAVAVFVV TWIVLPTDEE AMGRLVEEDS YKFRNIVLTL
TSIGLMATIL FHVFLKENLL EDFESQKGNI EEARRLFDSS QSSRTSLVGT TILLRVAMLY
VASRLFITLA TVYLPLYIEE TDIDGKEALA TVPLVSYISS FVAALLLKYI NKSCGTKGCG
IPLEISNKRR GGNAKSNVWQ GHGASYPLSI AALIHAPIRI IKNSPTLPRP MCVVCQSIDI
RNTVRQFSRL KGCRLVEGFV QILLIDNAEP SEYTNISFPE LREITGYLLL YRVKGLRSIG
RLFPNLTVIR GHSLFINYAL VAFEMMNLQE IGLHSLTTIV RGSVRFEKNP ALCYVDTIDW
DLIAKAGKGE HVIAHRVTDV VTGESECRER CPNGSLEFMN HRCIDEERCL RMEKPKEVLK
NVKNFPYKPF NGSCVMECPP GYMDDEWNGR VSCKKCEGSC QKECAGANVD SIASAQKLRG
CTHITGSLEI QIRGGKNIVK ELEDGLSTIE EIDGYLKIVR SFPLISLNFL KNLRVIRGND
IDNSKYTLLV MDNQNLQELW DWSLHKEMRI LSKDGPGKIF FHLNPKLCLY KIEMLREKAG
LGPFTDYEVA PNSNGDKVAC NVTELKTRVG KKSPWGAVIE WEPFVHHDAR SLLGYVVYFI
EAPNRNVTMY DGRDACGGDG WKVDDVSAST NSTLMDSRQE KSVHTHYLSQ LKPYTQYAYY
VKTYTIATER SGAQSNLTYF RTMPEAPSSP RSLITWSNSS SELIMSWLPP LHNNGNLTHY
RIVGRWEPDD PNFIDQRNYC EEPMMLSDKK PITLAEEERK RMEEEKEQMV PETGTCECAD
RETDQSLREK EASSAIDFED ALHNQVYVKR KPRRKRDVSD ILFRKTKSLD QPVMNKKVNG
TYVIFEENVA STNRSFVMKD LRHFAAYNIE VQACRAQEMN DTYKKCSTKS MRTYRTLPLE
SADNIPPNTF KMSISGENNS LTMVTLQWDE PPQPNGLIIT YQIEYKRVDI QNYKPTVVCI
TRRDFTKAGN SYVLKELPAG NYSVKVRATS LAGNGAYTHV KYFYIEERNT MNTFWIVFWL
LFCAVLAIFS LAAFYACKRK FLRNVPNVTL IATVNPEYVS TPYVLDEWEV PREKIEMLRS
LGTGTFGMVY EGIAKDIVKG KSEVRCAVKT VNKDATDRER IEFLNEASVM KGFDAHHVVK
LLGVVTRGQP TLVIMELMVN GDLKRYLRSH RPCENMSNAP PKLDRILQMA IEIADGMAYL
STKKFVHRDL AARNCMVAED LTVKVGDFGM TRDIYERDYY RKGSKGLLPV RWMAPESLKD
GVFSSYSDVW SYGVVLWEMV TFASQPYQGL SNEQVLRFKS SFSPSRRDSR IVVPYRDRSL
QVLRYVIEGG VMERPENCPE LLYELMKRTW RHKATRRPTF MDIASMLLKH IDSDSFQEVS
FYHSPEGVEA RNQNRSNSPQ TNQHLELATL QDLQEEEAEG EEDSPLRQDF GDFASFEPAS
IKNSFGSRFR MDSYGENSKT TPNCHDMNSS NVPLKAGFDD FDGVSADSIA SVAKDALNLP
FVEESLKSVK SSPFINASRG NLSQLSTSNR SATSPKNPSG KRSFLGSPNS SKIAANPDYE
NGSPEILSAA EKRETVPLRL DFPSIDAIDI DNGMEKKEAL SPVEYVNKPE TLNNGKVRYI
VSKPYFSAFK ETRLTSLSAF NNRGGLHGVA SIPDCKDQRA CYGWNCSSTT IRKMDVAKSG
TEDFVTVVSV EGVHPQENFV TVLSIGSRRE EGEASSRLAE QGPLEEEVEV YRLPGERLGF
GLKFEGGNKT SERVRRLFVQ SCAEQSPASR ARCSWGTLGE GDELTDDFFT RSPVPQVLSI
DGVPVTHMTR LDCVRRLKES QLVIKLVVRC RGALRPEVVS AEKKSCPERD KVPPELPSAP
PPVPPRKLRL ARGLADGEAN PNPAKRSWSG GGSAARAQPG DARSSPTAAA EASRSTSYES
CESSPRSASG SSPRGPRSPE LAKQGVKQVS LPVFSVDCGL RQRSCFQEPP PEAMVYVDAR
SQCGSTHGST SDDTGSSMST PRPSKPSAVC PFEDDAYYAS NPPDYLLRRL ASSEAVTHVE
SRGEVEKITA VVAPNTVLIE ETITFQPPLS FQDAPLSYGH EARPDLFYTA DLAADSTTHF
RPIRDDVELP SSSSSASSLP ESRQTSFENE NEDEMCLETI AADQLDEATL ARACLESRAQ
LEQEKEEEEE GSKRGSSLDE RRNEETDDTE SMENFEVGEG YRTNKVLEII EIRKARAFPP
RRGANVPFST EDEDKRGRPL DGGEELGNEA KEAEAGDSGQ ESGGIGGAMD ESDEEQVTKF
NEPVDGSEKG EADLTSANRG EEAIMEDDTT SEESDEGDYY WQSNLATIGE EEETNSLEYA
NPNKEAAESE AIEAQGKTES AGKEDAFDAN EPPDSLSCLL SARNDEVDDA NRSANFPSSE
PPVENHHSGV IRFPSRSHEA KKDEVCVIGV DYQICRPTPK IQFDHDLIRD KKSNHSTPIE
TTNSGPMIYR FFLFALEYLP TYVQTVNGRM DNCGGGQRLP PDGDEFPAAY QEFGGNSGQQ
QQQQQQQQQQ QQRFATTGSA TARTATMNGR LVCDEGEPFM VVNEGYKLLE GNVATGIILQ
AENRITVPGA ESSPVCQEVV GKLEMAGSER ENVVRCQDAS SNTVSLLARE EAKDELVKKS
VYSAAAGCYG DGSVLVSERR IEITGYYHKD VGAVIEEDRR AEKDDTPPPL PLTGPPKIDR
AVCPTSYAAR NAAPLLDSTA RKFTSNGELW RQDDKSERSV RDKIAMFSSQ SSLDGPLFPS
ASMIAAAATN RRLSKYKSTE DVCSDERHCG QKERVSFLGD RTQSSFDLTD SGRNVGQEPG
RSYSVSGQNS PTKAGLASAA LSRATSFSGS SSAYGHQDRA STAADLAPTL AISRTSSLAS
TFKRPAEDSL RRNSLNQLIE QRKRSISKLR GLVIPEKETI TIDAPIVDLP EIKSRDSILL
HQVLAKASIQ DKWGSQSSLA SNASTASVPL RSAASFKMPA PQIHSKYSPA FKRKSLTVYA
TSSSKDPSST SAPVKTPSPV TPISAPPLCE PPKSLESICS PTRSDYSFEY ASTASSPEGL
RGSRPRAAHR KARMDYDDSD NDSAVSSSQS SISRGFSPPT SPVPSERSTI SSERSYVSTE
NNYQRRSLII DSLTRGYNQA RESDGSQRNG SQIPQRQLKR SNSTDTNCST SSTLTSGSQA
SAESLSRRVL KPQSVEAINR KNILASARCR SGRDLNGSPL IQRKFADDKG RSVIGENGEE
NGYQKSRGVK NSVSKDAVKI AYIEVTDPLG EEDPFRKASE RSDSPLKMSV APSVARPPSK
FEASIEPSND LKMWVRTEAK ALARSIEEKP VDKVEKKSAD IAASDPVDND QRRNNNKSVG
MEKQRYGSID LSSPSRRIQE NENESRLTRQ PRGLLPPNKP SEDQNDLLTI LTTKSRSRSA
IHVDEGSFAR SKSQMSLEDI LGAKAETKSA RGQSGETRTE KSNVFSNSQS NLGKSLWESR
DNRYIRRSSS TLNEYWNEDH KSFSKASTLE KSRLAESSAD EMMEVEKSKS ALSKIPTSRN
LGRRSVSVTD MKKAVEVNFT GAQSVGTGHN RFPSLDSSVD ENMSPVGIDM DTDRCCNEQF
GSISSLASTT SLISQQELAQ LVEEASLEET RGAHDVIVVL LHKENPTGSV GITLAGGADC
EIKEITIHRV LAHSIADKDG RVQRGDRILS INGRSTQGLT HRESIAVLKQ PRSEVVLVVS
RSRTEEGSCK LKSRTASVET IIEDFVLEGF ETNDAAEDTA WGPPSVVAVY KDGTGLGFSL
EGGRDSPLGD RPLLIKKIFT GGAAEKTGAL KAGDQLLQVN GYDVTRMSRI EAWSLMKKLH
DGEVNLLVRH PATKSS
//
