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Database: UniProt
Entry: S7NB15_MYOBR
LinkDB: S7NB15_MYOBR
Original site: S7NB15_MYOBR 
ID   S7NB15_MYOBR            Unreviewed;      1344 AA.
AC   S7NB15;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
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   ORFNames=D623_10009165 {ECO:0000313|EMBL:EPQ14236.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ14236.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
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   EMBL; KE163877; EPQ14236.1; -; Genomic_DNA.
DR   eggNOG; KOG1025; Eukaryota.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:UniProtKB-UniRule.
DR   CDD; cd00064; FU; 3.
DR   CDD; cd05111; PTK_HER3; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF88; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 5.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 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|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000619};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
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   TRANSMEM        648..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          715..972
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1085..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1186..1220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1237..1259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         721..729
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   BINDING         748
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
SQ   SEQUENCE   1344 AA;  148113 MW;  569AF8E41672ED09 CRC64;
     MPKQCTLLGG PAGRGAETLV LVNVRWLEVV ILEKVCPGTL NGLSVTGDAE NQYQTLHKQY
     ERCEVVMGNL EIVLTGHNAD LSFLQWIREV TGYVLVAMNE FSTLPLPNLR VVRGTQVYDG
     KFAIFVMLNY NTNSSHALRQ LGFTQLTEIL SGGVYIEKND KLCHMDTIDW RDIVRDRDAE
     IVVKDNGRSC EPCHEVCKGR CWGPGPKDCQ TLTKTICAPQ CNGHCFGPDP NQCCHDECAG
     GCSGPQDTDC FACRLFNDSG ACVRQCPQPL VYNKLTFQLE PNPHTKYQYG GVCVASCPHN
     FVVDQTSCVR ACPPDKMEVD KNGLKICEPC GGLCPKACEG TGSGSRYQTV DSSNIDGFVN
     CTKILGNLDF LITGLNGDPW HKIPALDPEK LSVFRTVREI TGYLNIQSWP PHMHNFSVFS
     NLTTIGGRSL YNRGFSLLIM KNLNITSLGF RSLKEISAGR IYISANRQLC YHHSLNWTRL
     LRGPSEERLD IKHNRLRRDC VAEGKVCDPL CSGGCWGPGP GQCLSCRNYS RGGVCVTHCN
     FLNGEPREFA HEAECFPCHP ECQPMEGTAT CNGSGSDACA QCAHFRDGPH CVSSCPSGVL
     GAKGPIYKFP DAQNECRPCH ENCTQGCNGP DLQDCLGQTQ AMISKTHLAM ALAVVVGLVV
     IFVILGSTIL YLRGRRIQNK RAMRRYLERG ESIEPLDPSE KANKVLARVF KETELRKLKV
     LGSGVFGTVH KGVWIPEGES IKIPVCIKVI EDKSGRQSFQ AVTDHMLAIG SLDHAHIVRL
     LGLCPGSSLQ LVTQYLPLGS LLDHVRQHRG SLGPQLLLNW GVQIAKGMYY LEEHGMVHRN
     LAARNVLLKS TSQVQVADFG VADLLPPDDK QLLHSEAKTP IKWMALESIH FGKYTHQSDV
     WSYGVTVWEL MTFGAEPYAG LRLAEVPDLL EKGERLAQPQ ICTIDVYMVM VKCWMIDENI
     RPTFKELANE FTRMARDPPR YLVIKRESGP GIPPGAEPPA LTNKELEEVE LEPELDLDLD
     LEAEEDNLAT TLGSALSLPV GTLTWPRGSQ SLTSPSSGYM PMNQSNLGEA CQEPVVCGGE
     RCPRPASLHP MPRGRMVSES SEGHVTGSEA ELQEKVSMCR SRSRSPRPRG DSAYHSQRHS
     LLTPVTPLSP PGLEEEDVNG YVMPDAHLKG TPSSREGTLS SVGLSSVLGT EEEDEDEEYE
     YMNRRRRHSP PRPPRPGSLE ELGYEYMDVG SDLSASLGST QSCPLHPVPI IPTPGTTPDE
     DYEYMNKRRG GGGAGGDYAA MGACPAAEQG YEEMKAFQGP GHHAPQVHYT RLKTLRSLEA
     TDSAFDNPDY WHSRLFPKAN AQRT
//
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