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Database: UniProt
Entry: A0A1S3RLE7_SALSA
LinkDB: A0A1S3RLE7_SALSA
Original site: A0A1S3RLE7_SALSA 
ID   A0A1S3RLE7_SALSA        Unreviewed;       420 AA.
AC   A0A1S3RLE7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   11-DEC-2019, entry version 17.
DE   SubName: Full=G protein-activated inward rectifier potassium channel 2-like {ECO:0000313|RefSeq:XP_014052616.1, ECO:0000313|RefSeq:XP_014052617.1, ECO:0000313|RefSeq:XP_014052618.1};
GN   Name=LOC106603447 {ECO:0000313|RefSeq:XP_014052616.1,
GN   ECO:0000313|RefSeq:XP_014052617.1, ECO:0000313|RefSeq:XP_014052618.1,
GN   ECO:0000313|RefSeq:XP_014052619.1, ECO:0000313|RefSeq:XP_014052620.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014052619.1};
RN   [1] {ECO:0000313|RefSeq:XP_014052616.1, ECO:0000313|RefSeq:XP_014052617.1, ECO:0000313|RefSeq:XP_014052618.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014052616.1,
RC   ECO:0000313|RefSeq:XP_014052617.1};
RG   RefSeq;
RL   Submitted (JUN-2017) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003822}; Multi-
CC       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   RefSeq; XP_014052616.1; XM_014197141.1.
DR   RefSeq; XP_014052617.1; XM_014197142.1.
DR   RefSeq; XP_014052618.1; XM_014197143.1.
DR   RefSeq; XP_014052619.1; XM_014197144.1.
DR   RefSeq; XP_014052620.1; XM_014197145.1.
DR   GeneID; 106603447; -.
DR   KEGG; sasa:106603447; -.
DR   KO; K05000; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000087266; Genome assembly.
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; IPR003275; K_chnl_inward-rec_Kir3.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF19; PTHR11767:SF19; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01328; KIR32CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003822, ECO:0000256|SAAS:SAAS00434609,
KW   ECO:0000313|RefSeq:XP_014052616.1, ECO:0000313|RefSeq:XP_014052617.1};
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, ECO:0000256|SAAS:SAAS00434575};
KW   Potassium transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
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, ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM        79..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          43..182
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          189..359
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..420
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            168
FT                   /note="Role in the control of polyamine-mediated channel
FT                   gating and in the blocking by intracellular magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005465-1"
SQ   SEQUENCE   420 AA;  47924 MW;  E2B39ABC7420543D CRC64;
     MEQDVESPAV TTRKPKLPKQ AREDLPKQLV DQVRAKRKIQ RYVRKDGKCN VHHGNVQETY
     RYLTDIFTTL VDLKWRFNLF IFVLVYTVTW LLFGFAWWLI AYVRGDLEHI GDNQWTPCVN
     NLNGFVSAFL FSIETETTIG YGYRVITDQC PEGILLLLIQ SVLGSIVNAF MVGCMFVKIS
     QPKKRAETLV FSTSAVISVR DGRLCLMFRV GDLRNSHIVE ASIRAKLIKS KQTKEGEFIP
     LNQTDMNVGY DTGDDRLFLV SPLIICHEIN QNSPFWEISQ ADLDKEDLEI VVILEGMVEA
     TGMTCQARSS YVTSEIKWGY RFMPVLTLED GFYEVDYNSF HDIHETNTPS CSARELAEMN
     CRARLPLTWS VASKLSQQGV LEPEGREKKS TTTLVTQEEG LEEQTERNGD IANIESESKV
//
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