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Database: UniProt
Entry: A0A267GG53_9PLAT
LinkDB: A0A267GG53_9PLAT
Original site: A0A267GG53_9PLAT 
ID   A0A267GG53_9PLAT        Unreviewed;      1489 AA.
AC   A0A267GG53;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   ORFNames=BOX15_Mlig002042g3 {ECO:0000313|EMBL:PAA85045.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA85045.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA85045.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA85045.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA85045.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:PAA85045.1}.
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DR   EMBL; NIVC01000350; PAA85045.1; -; Genomic_DNA.
DR   STRING; 282301.A0A267GG53; -.
DR   Proteomes; UP000215902; 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:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR   CDD; cd00064; FU; 4.
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; 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   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; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 6.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1489
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012108316"
FT   DOMAIN          926..1196
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1200..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1295..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1449..1489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1302..1327
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1352..1375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1403..1424
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1466..1480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         960
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1489 AA;  162109 MW;  D6278C7EDF9DB685 CRC64;
     MLMHLMALCL LLPLSAAIDT AAVNASSEYV VCTGTLEAEQ TNEDSVRKFK ALRDRLSGCQ
     FVIGDIHLTR IKQEHFDEQD EVLDFGFLNT IKEVTGCVKL VDSCFSSPLE FESLQVIRGT
     GCGNSSLLLQ FDSNCALQTP YVAFPNLRHI GGGIILYNVS SCYIERHVSF SELFAYPMAP
     VVSRIGQCRD LDNACHSNCT EWPEDGQQHC WGPELRHCQP RTRCRHLSTR DCPYQRCFVD
     SQGGERCCHE QCLGGCFGPL AQHCLGCRNF DRNGTCVQKC ELENYYHPGA AQNLSPVEGK
     MLPHGPVCVT KCPGSYFTED GSCVKKCMSE RKPDADGVCV AVDESRVCEI EVGALSTICH
     SGNPLMQGLT NASMLCTEFH GSVTVNPDCF SDEPKPGKVT VEQLYTMFSR LRVVRGEIQL
     LLFGYNQLRN LTFLSHLERV DDRPGEKKSG RIMIVAPEIH FFGLASLRFI NKYIMFLALP
     NGSSVSLCTG FIPKQDAVNE SLIQLGASTT SNWLRSPEGL DNIRVRSICP IKPDSCDPQC
     EPRFGCWGPG PTNCVRCRSV KAGRICLQSC ESSPGWFLVN STKLLEKQGN TTLELMCSRC
     HHSCAKCDGP GPSNCTACLN GTFLDGSVCV AKCNPETQFE DVSARACQPC PKICTSLGNG
     KPTCTGNKTL VGPGGCQFCQ HVVVTQQSEA DFTPLLKCGP SSCPAGFYTA LVDFGSNQFN
     NFSDFLAVKR TVDLPVTMCA KCAPHCMTCK GASNKCTACR HYSIEPVLTD EFECETRAEP
     ACRDGFYADH GNQTCRPCAP PCSTCSGPGE GDCLRCVAPK YLVLAESEDG PVDVENSTSF
     CTDTCPEDRP RLIASKRGLI CTAALSTSMI GVLIGAAGFA VSLAALLSFC CIWRRRRSVM
     LPEEEKEELE PMLNRGYLAT ISENELARGP EVGSGAFGTV FKGEWTPADG DGRKTTVAIK
     ILADSGDNGL SSELLEESRI MASVDHPHCV RLVGICMTQP LQLVTQFMPL GNLRDFLRAR
     REPGQIGAAQ MLRYAAQIAS GMAHLERCNI IHRDLACRNV LVSSSRCVRI TDFGLAKALD
     TASQEYQASG GKLPVKWLAL ESLISRRFTH KSDVWSYGIT LWEIFTFGEP PYPNVKPQDL
     AEYLEKGERL PQPAVCMLDV YMLMIKCWML DEHHRPTFDE LEANFTKMCS QPERYVYNRG
     VRHPSHCSSS RVSGNSRGGS GGGGPKSPRH SNNNRQSLDE LDDAYVAMED EVAESDLDND
     VFVVDQSTLN TSTTSTACRR LPLSPQPLLY PSVHQNQHRQ LLPSAPPPPE QQLSQPPPPP
     PPLMKPPQRS FSVTSGGRRR AAGPPPPLVS SSPQNQYTMD PCQPGPSNSD YYLQPVCLSA
     GSRRENPLPL PPRLSPVATH PLATTPTRPP LPPPLPPPLL PPLLQSAGSP GAVANPEYFF
     HYSGASTATA AADAPSGGAA NAATAAATPN PASSNDSGIA SPKFEFGHD
//
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