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Database: UniProt
Entry: I3KCZ3_ORENI
LinkDB: I3KCZ3_ORENI
Original site: I3KCZ3_ORENI 
ID   I3KCZ3_ORENI            Unreviewed;       475 AA.
AC   I3KCZ3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   18-SEP-2019, entry version 49.
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 9 {ECO:0000313|Ensembl:ENSONIP00000018988};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000018988, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Ensembl:ENSONIP00000018988}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2012) to UniProtKB.
RN   [2] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J.,
RA   Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J.,
RA   Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A.,
RA   Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O.,
RA   Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R.,
RA   Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T.,
RA   Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S.,
RA   Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D.,
RA   Rakotomanga M., Renn S.C.P., Ribeiro F.J., Ron M., Salzburger W.,
RA   Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R.,
RA   Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D.,
RA   Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A.,
RA   Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid
RT   fish.";
RL   Nature 513:375-381(2014).
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   EMBL; AERX01017769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 8128.ENSONIP00000018988; -.
DR   Ensembl; ENSONIT00000019005; ENSONIP00000018988; ENSONIG00000015087.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193368; -.
DR   InParanoid; I3KCZ3; -.
DR   OMA; DYASFHQ; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000005207; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated 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; IPR003276; K_chnl_inward-rec_Kir3.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF17; PTHR11767:SF17; 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:UP000005207};
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:UP000005207};
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    146    167       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    224    244       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      110    249       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      256    424       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION       76     97       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      447    475       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        235    235       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   475 AA;  53462 MW;  E7B99545C3643196 CRC64;
     MALENSIFPS RPDSLSLPVE EKVESEEVEV ATEVTASTGV FNVSEELGHV VTTETTSSLP
     NSAPVKRSFQ SKLAEREANA NQHRKKTQGT EKERGRFGWA RTRRKRQRYV EKNGRCNVQH
     GNMRETYRYL TDIFTTLVDL NWRCSLFVFV MAYAVTWLFF GAIWYLIAYC RGDLDHLEDE
     TWTPCVNNVN GFISAFLFSI ETETTIGYGH RVITDQCPVG TMLLLLQAIL GSMVNAFMVG
     CMFVKISQPN KRAETLVFSK HAVISPRDDK LCLMFRVGDL RSSHIVGANI RAKLIKSKQT
     QEGEFIPLDQ TDISVGFETG DDRLFLVSPL VISHEIDARS PFWDMSHAQL EKEDFEIVVI
     LEGMVEATGM TCQARSSYLA EEVLWGHRFS PMMSLAEGFF DVDYGAFHHT FEVDTPSCSA
     RELSLAAARL DAHLYWSISS RLDEEPTLAN QAAKQPDRLG ELNGSVATDQ SESEA
//
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