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Database: UniProt
Entry: W5NMU3_LEPOC
LinkDB: W5NMU3_LEPOC
Original site: W5NMU3_LEPOC 
ID   W5NMU3_LEPOC            Unreviewed;       455 AA.
AC   W5NMU3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   16-OCT-2019, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLOCP00000021952};
GN   Name=KCNJ4 {ECO:0000313|Ensembl:ENSLOCP00000021952};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000021952, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Ensembl:ENSLOCP00000021952, ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000021952}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2014) 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; AHAT01036248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000021952; -.
DR   Ensembl; ENSLOCT00000021991; ENSLOCP00000021952; ENSLOCG00000017849.
DR   GeneTree; ENSGT00960000186595; -.
DR   OMA; GHNRNGQ; -.
DR   Proteomes; UP000018468; Linkage group LG12.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
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:UP000018468};
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:UP000018468};
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     55     79       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    177       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      184    354       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   COILED      393    413       {ECO:0000256|SAM:Coils}.
FT   SITE        163    163       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   455 AA;  51251 MW;  673C4537927BEE13 CRC64;
     GQGGSKVSTM GPGRLRSRFV KKNGQCNVVF TNMQDKPRRY LADIFTTCVD IRWRYMLAIF
     SAAFLASWLL FGLVFWGVAL AHGDLDLGRG LGSHLGGGPG GGRKEEEEEW KPCILHVHSF
     VGAFLFSIET QTTIGYGFRC VTEECPVAVA TVVVQSIVGC IIDSFMIGTI MAKMARPKKR
     AQTLLFSHHA VVALRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPYMTAE GEYLPLEQTD
     LNVGYDAGLD RLFLVSPLVI VHEIDEQSPL YGLSKEDLET EDFEIVVILE GMVEATAMTT
     QARSSYLARE ILWGHRFEPV VFEDKHRYQV DYSRFHKTYE VPSTPQCSAR ELSDASFKMT
     SPSLSLPPPS PPPAMLPLPT SAFCYENEVA LHCREEEEEE EERGREMEEL RDRAGDFRAP
     DDVLRVLDVE SRLEFDRLQA AIPLDPLSFR RESEI
//
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