ID A0A3B5B451_9TELE Unreviewed; 390 AA.
AC A0A3B5B451;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=G protein-activated inward rectifier potassium channel 1 {ECO:0000256|ARBA:ARBA00015495};
DE AltName: Full=Inward rectifier K(+) channel Kir3.1 {ECO:0000256|ARBA:ARBA00032145};
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 3 {ECO:0000256|ARBA:ARBA00031390};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000028363.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000028363.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: This potassium channel is controlled by G proteins. Inward
CC rectifier potassium channels are characterized by a greater tendency to
CC allow potassium to flow into the cell rather than out of it. Their
CC voltage dependence is regulated by the concentration of extracellular
CC potassium; as external potassium is raised, the voltage range of the
CC channel opening shifts to more positive voltages. The inward
CC rectification is mainly due to the blockage of outward current by
CC internal magnesium. This receptor plays a crucial role in regulating
CC the heartbeat. {ECO:0000256|ARBA:ARBA00024877}.
CC -!- SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein
CC activated heteromultimer pore-forming unit. The resulting inward
CC current is much larger. {ECO:0000256|ARBA:ARBA00025883}.
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. KCNJ3 subfamily. {ECO:0000256|ARBA:ARBA00009002}.
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DR AlphaFoldDB; A0A3B5B451; -.
DR Ensembl; ENSSPAT00000028823.1; ENSSPAP00000028363.1; ENSSPAG00000021334.1.
DR GeneTree; ENSGT01080000257365; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0015467; F:G-protein activated 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; IPR003274; K_chnl_inward-rec_Kir3.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767:SF99; G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 1; 1.
DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01327; KIR31CHANNEL.
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 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 72..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..176
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 183..354
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT REGION 343..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 162
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 390 AA; 44166 MW; 8FACFBE5BE909760 CRC64;
MAALRRKFGE DYQVVNTNRS MTFSAPVKRK RQRFVEKNGR CNVQHGNLGG ETSRYISDLF
TTLVDLKWRW NLLIFILTYT VAWLVMASMW WVIAYIRGDL SHGGHDSSYT PCVANVYNFP
SAFLFFIETE ATIGYGYRYI TEKCPEGIIL FLFQSLLGSI VDAFLIGCMF IKMSQPKKRA
ETLMFSQDAV ISQRDGKLCL MFRVGNLRNS HMVSAQIRCK LIKSRQTPEG EFLPLDQCEL
DVGFGTGADQ LFLVSPLTIC HEINTNSPFF DLSQRSLMNE QFEIVVILEG IVETTGMTCQ
ARTSYTEDEV LWGHRFLPVM SLEEGFFRVD YSQFHNTFEV PTPPYSVKEQ EEKSSLTSPN
PLPVAPTPSS PLLGNGVSAL AKITMHGKPV
//
