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Database: UniProt
Entry: A0A3Q3E828_9LABR
LinkDB: A0A3Q3E828_9LABR
Original site: A0A3Q3E828_9LABR 
ID   A0A3Q3E828_9LABR        Unreviewed;       409 AA.
AC   A0A3Q3E828;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Potassium inwardly rectifying channel subfamily J member 4 {ECO:0008006|Google:ProtNLM};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000003218.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000003218.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC       1.A.2.1) family. {ECO:0000256|RuleBase:RU003822}.
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DR   AlphaFoldDB; A0A3Q3E828; -.
DR   Ensembl; ENSLBET00000003389.1; ENSLBEP00000003218.1; ENSLBEG00000002240.1.
DR   GeneTree; ENSGT01030000234586; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR   PANTHER; PTHR11767:SF53; INWARD RECTIFIER POTASSIUM CHANNEL 4; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU003822};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU003822};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU003822};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW   ECO:0000256|RuleBase:RU003822};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003822};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003822};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003822}.
FT   TRANSMEM        79..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..180
FT                   /note="Potassium channel inwardly rectifying transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          187..358
FT                   /note="Inward rectifier potassium channel C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          386..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            166
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   409 AA;  46857 MW;  C5BC3993564FA9F6 CRC64;
     FSSVRTYSIV SDILPEEERQ KIFGGMNNGK ILTRGSSQLR SRFVKKNGQC NVLFTNMAEK
     RQRYLADIFT TCVDIRWRYL LLLFCCSFLL SWLFFGIIFY TVSLAHGDFE RSRMPCVLHV
     QGFVGALLFS METQTTIGYG WRCVTEECPV AIVTVVIQSI VGCIIDSFMI GTIMAKMARP
     KKRNQTLVFS KNAVIALRDG KLCLMWRVGN LRRSHIVEAH VRAQLIRSYV TAEGEFIPLE
     QTDLNVGYDE GTDRLFLVSP LVIVHEIDRD SPLYSLSRAD LETDHFEIVV ILEGMVEATA
     MTTQFRSSYI AREILWGHRF EPVIYEDRDC YKVDYARFHK TYEVPSTTQL SARELDEADL
     IPRSVSTFCY ENEAVLSCEE EDDVFTSSHA GGTEWSEERR TSEVNTLSK
//
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