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Database: UniProt
Entry: H2TBH2_TAKRU
LinkDB: H2TBH2_TAKRU
Original site: H2TBH2_TAKRU 
ID   H2TBH2_TAKRU            Unreviewed;       432 AA.
AC   H2TBH2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   16-OCT-2019, entry version 51.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000022013};
GN   Name=LOC101064149 {ECO:0000313|Ensembl:ENSTRUP00000022013};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000022013};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000022013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A.,
RA   Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu
RT   facilitates insights into distinct features of genome evolution in
RT   teleosts and mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000022013}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003822};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. {ECO:0000256|RuleBase:RU003822,
CC       ECO:0000256|SAAS:SAAS00549381}.
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DR   STRING; 31033.ENSTRUP00000022013; -.
DR   Ensembl; ENSTRUT00000022103; ENSTRUP00000022013; ENSTRUG00000008764.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186620; -.
DR   InParanoid; H2TBH2; -.
DR   OMA; EWADPEL; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1400; -; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR003269; K_chnl_inward-rec_Kir1.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF21; PTHR11767:SF21; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005226};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609};
KW   Ion transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434639};
KW   Membrane {ECO:0000256|SAAS:SAAS00434581, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434575};
KW   Potassium transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Transmembrane {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434543, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00036756,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM     94    115       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    168    193       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       58    198       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      205    372       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION        1     49       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     40       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        184    184       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium.
FT                                {ECO:0000256|PIRSR:PIRSR005465-1}.
SQ   SEQUENCE   432 AA;  48099 MW;  3A5B5D868A1970D6 CRC64;
     MTSATPPSSG SSSPQKVCHS QTQTDVSKPL LGSQETNGGS AMGAGGPGAL RRRRRVLSKD
     GRSNVLIEHV SGRGALYLRD LWTTFLDMQW RYKFFLFSAT FAGTWFVFGV LWYLVAMVHG
     DLQEFNPPSN HTPCVMEVKT LTGAFLFSLE SQTTIGYGFR CITEECPVAI VLLIFQLVIT
     MVLEIFITGT FLAKVARPKK RGETVKFSHH AVVSHHEGLP CLMIRVANMR KSLLLDCQVT
     GKLLQTSMTK EGETVRLDQR NVPFQVDTAS DSPFLIIPLT FYHIIDDSSP LREWAATGSE
     WADPELADFE LLVILSATIE PTSATCQVRT SYLPDEILWG YEFPPVVSLS PSGKYVADFA
     FFDKVAKTKT SPLFKKTLST IPVSQGSHYQ AKEGNGMDTE KMRLEESYRG EDRGKERRIR
     DSSPLCVRIS NV
//
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