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Database: UniProt
Entry: H3CWN9_TETNG
LinkDB: H3CWN9_TETNG
Original site: H3CWN9_TETNG 
ID   H3CWN9_TETNG            Unreviewed;       433 AA.
AC   H3CWN9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   16-OCT-2019, entry version 45.
DE   SubName: Full=Potassium voltage-gated channel subfamily J member 2 {ECO:0000313|Ensembl:ENSTNIP00000012673};
GN   Name=KCNJ2 {ECO:0000313|Ensembl:ENSTNIP00000012673};
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:ENSTNIP00000012673, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Ensembl:ENSTNIP00000012673}
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:ENSTNIP00000012673}
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; ENSTNIT00000012865; ENSTNIP00000012673; ENSTNIG00000009786.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   InParanoid; H3CWN9; -.
DR   OMA; VFSHYAT; -.
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; IPR003271; K_chnl_inward-rec_Kir2.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF43; PTHR11767:SF43; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   Pfam; PF08466; IRK_N; 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: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     83    107       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    154    179       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        6     47       IRK_N. {ECO:0000259|Pfam:PF08466}.
FT   DOMAIN       48    184       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      191    362       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        170    170       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   433 AA;  48802 MW;  463BCE56EA604E4A CRC64;
     GERADHRYSI VSSEEDGMKL AAVAVPNGYG NGNVDKGHAE RQHQSRFVRK GAHCNVQFIN
     MSEKGQRYLA DIFTTCVDIR WRWMLLVFCL SFLLSWLFFG LVFWMVALSY GDLDSKTQKC
     VSNVDSFTAA FLFSVETQTT IGYGYRYVTE ECPIAVFMVV FQSIVGCIID AFIIGAVMAK
     MAKPKKRNET LVFSYYATVA MRDSKLCLMW RVGNLRKSHL VEAHVRAQLL KSRTTAEGEY
     IPLDQVDIDV GFDSGLDRIF LVSPITIVHE IDEDSPFYEM SKEDLQTSEF EIVVILEGMV
     EATAMTTQCR SSYVAGEILW GHRFEPVLFE EKNYYKVDYS RFDNTYEVPS TPVCSARELA
     EKMSNPSSSR NSFCYENEVA LEKVELEDEE SGAARGDEVG AFEDTAAGVV LDSECNLDSV
     SLESRPLTAE SEI
//
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