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Database: UniProt
Entry: H3CDP5_TETNG
LinkDB: H3CDP5_TETNG
Original site: H3CDP5_TETNG 
ID   H3CDP5_TETNG            Unreviewed;       382 AA.
AC   H3CDP5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   16-OCT-2019, entry version 43.
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 1b {ECO:0000313|Ensembl:ENSTNIP00000006368};
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:ENSTNIP00000006368, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Ensembl:ENSTNIP00000006368}
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:ENSTNIP00000006368}
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; ENSTNIT00000006517; ENSTNIP00000006368; ENSTNIG00000003768.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193347; -.
DR   InParanoid; H3CDP5; -.
DR   OMA; LWYWIAK; -.
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; 1.
DR   PANTHER; PTHR11767:SF6; PTHR11767:SF6; 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: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     58     81       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    136    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       22    164       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      171    340       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        150    150       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   382 AA;  43026 MW;  9B9E9E26C84B581F CRC64;
     MFQLLQRHIQ PAGQQSRTTR LVTKDGHCNI EFGNIEYSNH FAYLLDFWTT FVEIRWRFVL
     LFFVASFTGS WFFFSLLWYW IAKSNGDLTG QNRTDEHVRC VDNVNGLTTA FLYSLETQTT
     IGYGGRALTG HCAGTVALII VQSLIGVFIN CFMCGVILAK ISLPKKRAKT VTFSDQAVIC
     LKEGSLCLLI RVANLRKTLL IGSQIYGKLL RTTSTADGET IILEQVDIDF MVDAGKDHLF
     FVCPLTLYHV INRSSPFYEL SADSLPHQDF ELVVFLEGTA ESTSSACQVR TSYIPQEIQW
     GYTFLPIISC IQTGKYRVDF SNFSKSVRVS TPHCVHCCEA DSDQRNHNGH DTDNHHVHGK
     VGIDNLGFQV VDIQESVAIT KM
//
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