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Database: UniProt
Entry: Q4S3E4_TETNG
LinkDB: Q4S3E4_TETNG
Original site: Q4S3E4_TETNG 
ID   Q4S3E4_TETNG            Unreviewed;       850 AA.
AC   Q4S3E4;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=(spotted green pufferfish) hypothetical protein {ECO:0000313|EMBL:CAG04838.1};
DE   Flags: Fragment;
GN   ORFNames=GSTENG00024683001 {ECO:0000313|EMBL:CAG04838.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG04838.1};
RN   [1] {ECO:0000313|EMBL:CAG04838.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAG04838.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) 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:CAG04838.1}.
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DR   EMBL; CAAE01014751; CAG04838.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4S3E4; -.
DR   KEGG; tng:GSTEN00024683G001; -.
DR   HOGENOM; CLU_008873_2_0_1; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:UniProt.
DR   GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd05095; PTKc_DDR2; 1.
DR   Gene3D; 2.60.120.1190; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR048525; DDR1-2_DS-like.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
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:SF295; DISCOIDIN DOMAIN-CONTAINING RECEPTOR 2; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF21114; DDR1-2_DS-like; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..850
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004243306"
FT   TRANSMEM        396..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..180
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          560..848
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAG04838.1"
FT   NON_TER         850
FT                   /evidence="ECO:0000313|EMBL:CAG04838.1"
SQ   SEQUENCE   850 AA;  96250 MW;  22146B65D4E23007 CRC64;
     RLYLLPLVLL HLFAAVRPQV NTGVCRYPLG MSGGQIQDED ISASSQWSES TAARYGRLDF
     EEGDGAWCPE TTVEPDSLKE FLQIDLRSLH FITLVGTQGR HAGGIGNEFA QMYKIKYSRD
     GSRWISWRNR QGEQVIEGNR NTYDIVLKDL EPPIIARFVR FMPVTDHSMN VCMRVELYGC
     EWLDGLVSYN APAGEQMNLP SFLVYVNDSV YDGAVTHSMT EGLGQLTDGV FGLDDFTNSC
     VYKAWPGYDY VGWSNESFPS GYVEIMFEFD RIRNFTTMKV HCNNMFSNHV KVFRQVLCHF
     RSESDWEPSP LLFSPAADEK NPSARFVTVS LANHMASAIK CQFYFADTWM LFSEITFQSD
     TAMYNTTLAP PKTGLPPNTP PGEDPTHKVD DSNTRILIGC LVAIIFILVA IIVIMLWRQV
     WQKMLEKASR RMLDDELITS LSIQSETFVY NHNQSSGASE QESSSTYERI FPLGPDYQEP
     SRFICKLPEF APSLEEPGST AASKSTTSTV AQDGVPHYAE ADVVNLQGVT GSNTYAIPAV
     TMDLLSGKDV AVEEFPRKML TFKEKLGEGQ FGEVHLCEAE GMHKFMDKEF LFDVPEDQPV
     LVAVKMLRSD ANKNARSDFL KEIKIMSRLK DPNIIRLLAV CICSDPLCMI TEYMENGDLN
     QFLSRHEPEG QLALISNAST VSFSNLCYMA AQIASGMKYL SSLNFVHRDL ATRNCLVGKN
     FTIKIADFGM SRNLYSGDYY RIQGRAVLPI RWMSWESILL GKFTTASDVW AFGVTLWEIL
     NFCKEQPYSQ LTDEQVIENT GEFFRDQKRQ IYLPQPGLCP DSLYKVMLSC WRRNAKERPS
     FQEIHTTLLE
//
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