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Database: UniProt
Entry: A0A1I8M3W7_MUSDO
LinkDB: A0A1I8M3W7_MUSDO
Original site: A0A1I8M3W7_MUSDO 
ID   A0A1I8M3W7_MUSDO        Unreviewed;      1438 AA.
AC   A0A1I8M3W7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
GN   Name=101887261 {ECO:0000313|EnsemblMetazoa:MDOA000996-PA};
GN   Synonyms=LOC101887261 {ECO:0000313|RefSeq:XP_005174763.1};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA000996-PA};
RN   [1] {ECO:0000313|EnsemblMetazoa:MDOA000996-PA}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA000996-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005174763.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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 protein kinase superfamily. Tyr protein
CC       kinase family. EGF receptor subfamily. {ECO:0000256|PIRNR:PIRNR000619}.
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DR   RefSeq; XP_005174763.1; XM_005174706.3.
DR   STRING; 7370.A0A1I8M3W7; -.
DR   EnsemblMetazoa; MDOA000996-RA; MDOA000996-PA; MDOA000996.
DR   GeneID; 101887261; -.
DR   KEGG; mde:101887261; -.
DR   VEuPathDB; VectorBase:MDOA000996; -.
DR   eggNOG; KOG1025; Eukaryota.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000095301; Unassembled WGS sequence.
DR   Proteomes; UP000694905; Unplaced.
DR   GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
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:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR   GO; GO:0000003; P:reproduction; IEA:UniProt.
DR   CDD; cd00064; FU; 7.
DR   CDD; cd05057; PTKc_EGFR_like; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF566; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 7.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000619};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000619};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000619, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000619};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|PIRNR:PIRNR000619,
KW   ECO:0000313|RefSeq:XP_005174763.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000619}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1438
FT                   /note="Receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041080390"
FT   TRANSMEM        880..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1012..1031
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          396..427
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          950..1210
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          32..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1247..1306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1396..1438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1419..1438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1075
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT   BINDING         956..964
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   BINDING         983
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1438 AA;  160456 MW;  7B96397651376409 CRC64;
     MKGYNWLGAS LLLLIVLTHN FEPLLAQRAR NGRNSNKYNE DTNNNRSQRK RNNNNGNRSQ
     SSHRPRPSSQ HLISSLAAPS SLSSSSISGS SSSSTHHHLA EDQHTEFVKG KICIGTKSRL
     SVPSNREHHY RNLRDRYNNC TYVDGNLELT WLQDANLDLS FLENIREVTG YILISHVDIR
     QVVFPRLQII RGRTLFNLNV QDEQFALFVT YSKTFSLEMP ALRDILQGSV GFFNNFNLCH
     IKTLDWNEII SGPPDKYKYH YVYNFTVPER QCPKCHESCE GGCWGEGPNN CQKFSKINCS
     PQCAQGRCFG PRPRECCHLF CAGGCTGPTQ RECIACKNFY DDGVCKEECP PMQKYNPTNY
     LWEANPEGKY AYGATCVKEC PEHLLKDNGA CVRSCPAFKM AKDGECIPCN GPCPKTCPGR
     AVLHSGNIDS YKGCTVIEGS IRVLDQTFSG YQDIYKNYSL GPRYIAMHPD RMEVFSTVKE
     ITGYLDIEGV HPDFKNLSYF RNLEVIHGRQ LMESYFASLS IVKSSLQSLE LKSLKRINAG
     SVVIQHNDKI CYVNDIDWSK LQKSGEHGFV VEMNRNKEDC KKNGLVCSDQ CNSSGCWGSG
     PDQCLECKNF EFNGTCIADC RNITNAYQFD AKTCKQCHPE CRTCSGPDAE HCDECVHVRD
     ENRCVTVCPE NKFSDYGVCR TCHATCEGCT GPNNTIGPGG CKTCNLAIIN SDGDIERCLL
     KNDKCPDGYY WEYVNPREQG KLRPLAGKAI CRKCHPRCEL CSGYGFHEQV CQKCAGYKRG
     EQCDDECPTD HYADEVNREC FMCHPECKGC IGPGADECLA CRSFKIFGDG DPYDNSTVFN
     CTSKCPPELS HVIYQAPHLG TYCSSVPMKG SKLVAAVDNY IFLVIAVVAL VVVLGTLSVV
     TYVCRQKTKA KTEAVKMTMV LSGCEDSEPL RPSNIGANLS KLRIVKEAEL RKGGVLGMGA
     FGRVFKGVWV PEGENVKIPV AIKELLKSSG AESSEEFLRE AYIMASVEHP NLLKLLAVCL
     TSQMMLITQL MPLGCLLDYV RNNRDKIGSK ALLNWSTQIA KGMSYLEEKR LVHRDLAARN
     VLVQTPSCVK ITDFGLAKLL NNDSNEYKAA GGKMPIKWLA LECIRHRVFT SKSDVWAFGV
     TIWELLTFGQ RPHENIPAKD IPDLIEVGLK LEQPEICSLD IYCTLLSCWH LDAEMRPSFK
     QLVNVFAEFA RDPGRYLAIP GDKFTRLPAY TSQDEKDLIR KLAPSFEGSE GMAEPDDYLQ
     PKAAPGNHNQ EGSEDVPKLN RYCKDPMNKN SSNESDETDS NAREVGVGDL RLELPVDEDD
     YLMPTCQISS QTTLNNNNVT TSNAMSGAPG GYMDLIGVPA SVDNPEYLLN TSANLNGQEA
     PIPTQTLGIP VMVTRPPNPG PTMLDIPVTP SEPTSSDHEY YNDTQRELQP LHRNETRV
//
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