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Database: UniProt
Entry: H3CY88_TETNG
LinkDB: H3CY88_TETNG
Original site: H3CY88_TETNG 
ID   H3CY88_TETNG            Unreviewed;       342 AA.
AC   H3CY88;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   16-OCT-2019, entry version 46.
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 1a, tandem duplicate 6 {ECO:0000313|Ensembl:ENSTNIP00000013223};
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;
OC   Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000013223, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Ensembl:ENSTNIP00000013223}
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.,
RA   Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B.,
RA   Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S.,
RA   Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B.,
RA   Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V.,
RA   Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J.,
RA   Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S.,
RA   Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J.,
RA   Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M.,
RA   Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C.,
RA   Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals
RT   the early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000013223}
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   Ensembl; ENSTNIT00000013415; ENSTNIP00000013223; ENSTNIG00000010319.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193347; -.
DR   OMA; IINCFWC; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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; IPR003268; K_chnl_inward-rec_Kir1.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 2.
DR   PANTHER; PTHR11767:SF6; PTHR11767:SF6; 2.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 2.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007303};
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:UP000007303};
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     60     83       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    137    160       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       24    166       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      174    310       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      318    342       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        152    152       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   342 AA;  38999 MW;  7F7ADDE49B439E92 CRC64;
     MFRFVSKCFR DCLAERRHRR TRLVTKDGRC NIEYGNIKYS NHFALLADFW TTFVEIRWRF
     VLFLFIAAFT LSWFLFGLLW YWIARTNGDL AWQNPPSNHT PCVDNVVGLT TAFLYSIETQ
     TTIGYGGRAL THLCPGAVSL LVIQSLIGAI INCFMCGVIL SKISLPTQNP DDGSQIYGKL
     LRTTNTPDGE TIIMDQVNIE FMVDAGKDNL FFVCPLTLYH VIDKSSPFFD MAVDTLHKQE
     FELVVFLDGT AESTSSSCQV RTSFIPQEIM WGYNFLPIIS RSKEGRYRVD FSNFSKVVPV
     ATAHCAYCFH NIKGHHHHSR DGHDNKGFEV IEIQDPPSVT KM
//
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