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Database: UniProt
Entry: G1SZ77_RABIT
LinkDB: G1SZ77_RABIT
Original site: G1SZ77_RABIT 
ID   G1SZ77_RABIT            Unreviewed;       419 AA.
AC   G1SZ77;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   16-OCT-2019, entry version 47.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOCUP00000008960};
GN   Name=KCNJ4 {ECO:0000313|Ensembl:ENSOCUP00000008960};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000008960, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000008960, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000008960}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000008960};
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   EMBL; AAGW02071791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9986.ENSOCUP00000008960; -.
DR   Ensembl; ENSOCUT00000010400; ENSOCUP00000008960; ENSOCUG00000010404.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   InParanoid; G1SZ77; -.
DR   OMA; GHNRNGQ; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000001811; Chromosome 4.
DR   Bgee; ENSOCUG00000010404; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
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:0030165; F:PDZ domain binding; IEA:Ensembl.
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; PR01326; KIR23CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001811};
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:UP000001811};
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     57     83       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     95    111       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    131    155       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       22    160       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      167    339       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   COILED      344    364       {ECO:0000256|SAM:Coils}.
FT   SITE        146    146       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   419 AA;  47412 MW;  0A9F79136DC7D8A8 CRC64;
     MHGHSRNGQA HVPRRKRRNR FVKKNGQCNV YFANLSNKSQ RYMADIFTTC VDTRWRYMLM
     IFSAAFLVSW LFFGLLFWCI AFFHGDLAAS AAPKPCIMHV NGFLGAFLFS VETQTTIGYG
     FRCVTEECPL AVIAVVVQSI VGCVIDSFMI GTIMAKMARP KKRAQTLLFS HHAVISVRDG
     KLCLMWRVGN LRKSHIVEAH VRAQLIKPYM TQEGEYLPLD QRDLNVGYDI GLDRIFLVSP
     IIIVHEIDED SPLYGMGKEE LESEDFEIVV ILEGMVEATA MTTQARSSYL ASEILWGHRF
     EPVVFEEKSH YKVDYSRFHK TYEVAGTPCC SARELQESKI TVRAFCYENE LALMSQEEEE
     MEEEAVAAAA VAAGLGLEAG SKEEAGIIHM LEFGSHLDLE RMQATLPLDN VSYRRESAI
//
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