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Database: UniProt
Entry: G3PU46_GASAC
LinkDB: G3PU46_GASAC
Original site: G3PU46_GASAC 
ID   G3PU46_GASAC            Unreviewed;       385 AA.
AC   G3PU46;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   31-JUL-2019, entry version 41.
DE   SubName: Full=Potassium voltage-gated channel subfamily J member 4 {ECO:0000313|Ensembl:ENSGACP00000021133};
GN   Name=KCNJ4 {ECO:0000313|Ensembl:ENSGACP00000021133};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021133};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000021133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000021133}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) 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; ENSGACT00000021173; ENSGACP00000021133; ENSGACG00000016015.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   Proteomes; UP000007635; 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; IPR003273; K_chnl_inward-rec_Kir2.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF53; PTHR11767:SF53; 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:UP000007635};
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:UP000007635};
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     40     66       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    129    154       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        5    159       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      166    337       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      345    385       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    357    371       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        145    145       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   385 AA;  43797 MW;  F9AAB0830B344AE8 CRC64;
     RSRFVKKNGQ CNVVFNNMED KPRRYLADIF TTCVDIRWRY LLLIFTTTFL LSWLLFAVVF
     WGVALIHGDF SLRVPAKEGD PGANGEDAKD EWRPCILHIQ GFIGAFLFSI ETQTTIGYGF
     RCVTEECPVA VVTVVVQSIV GCIIDSFMIG TIMAKMVRPK KRAQTLLFSH YAVIALRDGK
     LCLMWRLGNM RKSHIVEAHV RAQLIKPHVT AEGEYLPLEQ TDIDVGYDDG LDRLFLVSPL
     VVVHEINKTS PLYDVSRSDL LKEDFEIVVI LEGMVEATAM TTQARSSYLS KEILWGHRFE
     PVVFEKGDRY QVDYSRFHKS YEVPSTPHCS ARELNQMMGR GALTDYSPPY RYTSAESQGN
     KREKQSSHEH QQEALKSAQL QRGGG
//
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