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Database: UniProt
Entry: A0A1S3LPI0_SALSA
LinkDB: A0A1S3LPI0_SALSA
Original site: A0A1S3LPI0_SALSA 
ID   A0A1S3LPI0_SALSA        Unreviewed;       436 AA.
AC   A0A1S3LPI0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   31-JUL-2019, entry version 15.
DE   SubName: Full=G protein-activated inward rectifier potassium channel 2-like isoform X1 {ECO:0000313|RefSeq:XP_013992735.1};
GN   Name=LOC106567685 {ECO:0000313|RefSeq:XP_013992735.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Salmoniformes; Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013992735.1};
RN   [1] {ECO:0000313|RefSeq:XP_013992735.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013992735.1};
RG   RefSeq;
RL   Submitted (JUN-2017) 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   RefSeq; XP_013992735.1; XM_014137260.1.
DR   GeneID; 106567685; -.
DR   KEGG; sasa:106567685; -.
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   Complete proteome {ECO:0000313|Proteomes:UP000087266};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|RefSeq:XP_013992735.1};
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,
KW   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,
KW   ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM     96    117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    171    194       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       60    199       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      206    375       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION        1     24       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      397    436       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     15       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    398    436       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        185    185       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   436 AA;  49771 MW;  299028D50F7C7FA8 CRC64;
     MNKSGVYQQG LTPSKAPMEQ DVESPAITIR KPKLPKQACE DLPKQLVDQV RAKRKIQRYV
     RKDGKCNVHH GNVQETYRYL TDIFTTLVDL KWRFNLFIFV LVYTVTWLLF GFAWWLIAYV
     RGDLEHIGDN QWTPCVNNLN GFVSAFLFSI ETETTIGYGY RVITDQCPEG ILLLLIQSVL
     GSIVNAFMVG CMFVKISQPK KRAETLVFST NAVISVRDGR LCLMFRVGDL RNSHIVEASI
     RAKLIKSKQT KEGEFIPLNQ TDMNVGYDTG DDRLFLVSPL IICHEINQNS PFWEISQAHL
     DKEDLEIVVI LEGMVEATGM TCQARSSYVT SEIKWGYRFM PVLTLEDGFY EVDYNSFHDI
     HETNTPSCSA RELAEINCRI RLPFTWSVAS KLSQQGVLEP ESREKKHTTL VTQEEGLEEQ
     TERNGDIANI ESESKV
//
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