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Database: UniProt
Entry: A0A4Y0BMB8_ANOFN
LinkDB: A0A4Y0BMB8_ANOFN
Original site: A0A4Y0BMB8_ANOFN 
ID   A0A4Y0BMB8_ANOFN        Unreviewed;      1145 AA.
AC   A0A4Y0BMB8;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN020655-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN020655-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN020655-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A4Y0BMB8; -.
DR   STRING; 62324.A0A4Y0BMB8; -.
DR   EnsemblMetazoa; AFUN020655-RA; AFUN020655-PA; AFUN020655.
DR   VEuPathDB; VectorBase:AFUN020655; -.
DR   VEuPathDB; VectorBase:AFUN2_005466; -.
DR   Proteomes; UP000075900; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR   CDD; cd10319; EphR_LBD; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05033; PTKc_EphR; 1.
DR   Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR   InterPro; IPR027936; Eph_TM.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_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; IPR001426; Tyr_kinase_rcpt_V_CS.
DR   PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR   PANTHER; PTHR46877:SF14; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS51550; EPH_LBD; 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; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Signal {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}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1145
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5021285492"
FT   TRANSMEM        595..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..207
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          330..430
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          489..582
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          697..964
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1088..1144
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          1013..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         731
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1145 AA;  126621 MW;  009FB88F0AE98344 CRC64;
     MERFLSLLLL CYVLYQKFNG VVSDQVVLLD TTKEATLEWT RYPYGPQAQT PGWVEESFTN
     FVKGINWRSY VVCDVAYNNV NNWLWSPFID RGPANRLYIE IHFTIRDCSL FPGNALSCKE
     TFSLLFYEFD AATREPPPWQ PESYKLIGRI AAGEGRFNQN SDVDINVEVK SIAVTKKGVY
     FAFRDQGACI SVLAVKVYYI TCPAVTVNFA HFNETPTGRE VTIIEQQMGV CVENAEAYET
     PTYLCKGDGK WTILTGGCRC KVGYEPDADK QTCNVCPVGK FRSAEVRTCT ICPLNSKTNK
     VGSPFCPCLS GHYRHPRDGK HMPCYKPPGP PTNLTLLFID QTSAILSWNA PQRAADEQLD
     SKFRSDIVFR VRCAACTSNV VFNPSSETFN DTKLTLTNLE PVTTYTVQVH SQHGVSYPIV
     TPDGAHGAGG YENGSVVSGA AAGGYHATEP PMVMVNARAG GSGSSSDLDD IKTEFAEITF
     TTESAILSTV FNVKVVQITN KDVDLVWDKP IHSDSPIEYY EVRWFPKSEV DAMNKSVLST
     KESKIHIGDL LENTEYGFQV RCKTLNGWGT FSNIVYAQTH QSVSPVYDDS FQMRIVAGTT
     VTVVFILVLV IVITVVFLRS KNHDEIDKKT NNHLPLPLDY ASNEVHAMDT TPIVKTMKSN
     VTTPLFGTSR SYVDPHTYED PNQAIREFAR EIDASYITIE AIIGGGEFGD VCRGRLKVPP
     NFVQEIDVAI KTLKPGSSEK ARCDFLTEAS IMGQFEHPNV IFLQGVVTRS NPVMIITEYM
     ENGSLDTFLR ANDGKFQTIQ LIGMLRGIAA GMTYLSDMNY VHRDLAARNV LVNSLLVCKI
     ADFGLSREIE NASDAYTTRG GKIPVRWTAP EAIAFRKFTS ASDVWSYGVV LWEVMSFGER
     PYWNWSNQDV IKSIEKGYRL PAPMDCPEAL YQLMLDCWQK QRTHRPTFAS ITQTLDNLAR
     QPQVLLTTRN SPDNPVARMG TAGVPDDLTQ EMLAASAGGG VVVGVLGGSS QQQQQQQQQQ
     QQQQQQRAAT LMMGGGSGTT ERVLNNGSST TNVPGSMGTL GSTVGGLSNT GTMSGTGNPG
     IFISTDLWLE GIKMSRYSQH FKEAGLVTAQ QLSRLTAQQL SDMGITLVGH QKKILHQARQ
     IDTII
//
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