GenomeNet

Database: UniProt
Entry: W5NNI2_LEPOC
LinkDB: W5NNI2_LEPOC
Original site: W5NNI2_LEPOC 
ID   W5NNI2_LEPOC            Unreviewed;       429 AA.
AC   W5NNI2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   18-SEP-2019, entry version 36.
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 12b {ECO:0000313|Ensembl:ENSLOCP00000022191};
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:ENSLOCP00000022191, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Ensembl:ENSLOCP00000022191, 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:ENSLOCP00000022191}
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AHAT01031975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000022191; -.
DR   Ensembl; ENSLOCT00000022232; ENSLOCP00000022191; ENSLOCG00000018090.
DR   GeneTree; ENSGT00960000186595; -.
DR   OMA; DCFMIGA; -.
DR   Proteomes; UP000018468; Linkage group LG13.
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; IPR003272; K_chnl_inward-rec_Kir2.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF14; PTHR11767:SF14; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   Pfam; PF08466; IRK_N; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01325; KIR22CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
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     82    108       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    183       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        2     46       IRK_N. {ECO:0000259|Pfam:PF08466}.
FT   DOMAIN       47    188       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      195    366       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        174    174       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   429 AA;  48985 MW;  0D6BA506A74C8643 CRC64;
     GMSAGRINRY SIVSSEEDGL RLATMPGVNG FGNGKIHTRR KCRNRFVKKN GQCNVQFANM
     DDKSQRYIAD IFTTCVDIRW RYMLLIFSLA FLVSWLAFGL AFWLIALIHG DLENPTGDEN
     FKPCVLQVNG FVAAFLFSIE TQTTIGYGFR CVTEECPIAV FLVVFQSIVG CIIDSFMIGA
     IMAKMARPKK RAQTLLFSHN AVIAMRDGKL CLMWRVGNLR RSHIVEAHVR AQLIKPRITE
     EGEYIPLDQI DINVGFDKGL DRIFLVSPIT ILHEIDEESP LFGISKQDLE TADFEIVVIL
     EGMVEATAMT TQARSSYLAA EILWGHRFEP VLFEEKNQYK VDYSHFHKTY EVPSTPRCSA
     KDMVENKFLV PSTNSFCYEN ELAFMSRDEE EDEDSRVLDD LSPDSRHDFD RLQATIALDQ
     RSYRRESEI
//
DBGET integrated database retrieval system