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Database: UniProt
Entry: A0A1S3RDZ1_SALSA
LinkDB: A0A1S3RDZ1_SALSA
Original site: A0A1S3RDZ1_SALSA 
ID   A0A1S3RDZ1_SALSA        Unreviewed;       459 AA.
AC   A0A1S3RDZ1;
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=inward rectifier potassium channel 2-like isoform X1 {ECO:0000313|RefSeq:XP_014049983.1, ECO:0000313|RefSeq:XP_014049984.1};
GN   Name=LOC106602059 {ECO:0000313|RefSeq:XP_014049983.1,
GN   ECO:0000313|RefSeq:XP_014049984.1};
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_014049984.1};
RN   [1] {ECO:0000313|RefSeq:XP_014049983.1, ECO:0000313|RefSeq:XP_014049984.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014049983.1,
RC   ECO:0000313|RefSeq:XP_014049984.1};
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_014049983.1; XM_014194508.1.
DR   RefSeq; XP_014049984.1; XM_014194509.1.
DR   GeneID; 106602059; -.
DR   KEGG; sasa:106602059; -.
DR   KO; K04996; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000087266; Genome assembly.
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: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; IPR003271; K_chnl_inward-rec_Kir2.1.
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:SF43; PTHR11767:SF43; 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; PR01324; KIR21CHANNEL.
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_014049983.1,
KW   ECO:0000313|RefSeq:XP_014049984.1};
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     86    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    157    182       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1     50       IRK_N. {ECO:0000259|Pfam:PF08466}.
FT   DOMAIN       51    187       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      194    366       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      390    409       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      418    459       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    390    405       Acidic. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    420    446       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        173    173       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   459 AA;  52263 MW;  E07F425AA00C63D1 CRC64;
     MGSVRSHRYS IVSSEEDGMK LAAIAAVPNG YANGTVAKVH AAQQQAVSRF VQKDGHCNVQ
     FINMSEKGQR YLADLFTTCV DIRWRWMLII FCLSFLLSWL FFGFVFWLVA LSYGDLENET
     QMCVSNVNSF TAAFLFSVET QTTIGYGYRY VTEECPVAVF MVVFQSIFGC IIDAFIIGAV
     MAKMAKPKKR NETLLFSHYA TVAMRDSKLC LMWRVGNLRK SHLVEAHVRA HLLRSRTTAE
     GEYIPLDQMD IDVGFDSGVD RVFLVSPITI VHEIDEDSPL YEMSKQELET SQFEMVVILE
     GMVEATAMTT QCRSSYVASE VLWGHRFEPV LFEENNYYKV DYSRFEKTYE VSSTPQCSAR
     ELAENKSLVS CSNSFCYENE VALEKVEMEE TFDEEKEEDG EEKEEVKMED QGAIENGIEN
     ATLEETNTDT VSVHSEHNQD TRSLTMPSEA RPLRRESEI
//
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