ID A0A1S3GX26_DIPOR Unreviewed; 426 AA.
AC A0A1S3GX26;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Inward rectifier potassium channel 16 {ECO:0000313|RefSeq:XP_012893341.1, ECO:0000313|RefSeq:XP_012893342.1};
GN Name=Kcnj16 {ECO:0000313|RefSeq:XP_012893341.1,
GN ECO:0000313|RefSeq:XP_012893342.1, ECO:0000313|RefSeq:XP_012893344.1,
GN ECO:0000313|RefSeq:XP_012893345.1, ECO:0000313|RefSeq:XP_012893346.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012893341.1};
RN [1] {ECO:0000313|RefSeq:XP_012893341.1, ECO:0000313|RefSeq:XP_012893342.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012893341.1,
RC ECO:0000313|RefSeq:XP_012893342.1};
RG RefSeq;
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 RefSeq; XP_012893341.1; XM_013037887.1.
DR RefSeq; XP_012893342.1; XM_013037888.1.
DR RefSeq; XP_012893344.1; XM_013037890.1.
DR RefSeq; XP_012893345.1; XM_013037891.1.
DR RefSeq; XP_012893346.1; XM_013037892.1.
DR STRING; 10020.ENSDORP00000027643; -.
DR GeneID; 106003110; -.
DR KEGG; dord:106003110; -.
DR CTD; 3773; -.
DR OMA; CVFEVRS; -.
DR OrthoDB; 4126787at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IPR008061; K_chnl_inward-rec_Kir5.
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:SF24; INWARD RECTIFIER POTASSIUM CHANNEL 16; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01678; KIR5CHANNEL.
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:UP000081671};
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 74..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..174
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 182..348
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT REGION 356..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 161
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 426 AA; 48555 MW; CC6BEFAFB3CD7598 CRC64;
MSYYGSSYRV VNVDSKYPGF PPEQAMAEKR RARRRLLHKD GSCNVYFKHI FGEWGSYVVD
IFTTLVDTKW RHMFVIFSLS YVLSWLIFGS IFWVIAWHHG DLSSPPDLTP CVDNVHSFTA
AFLFSLETQT TIGYGYRCVT EECSVAVLTV ILQSILSCII NTFIIGAALA KMATARKRAQ
TIRFSYFALI GMRDGKLCLM WRIGDFRPNH VVEGTVRAQL LRYAEDSEGR MTMAFRDLKL
VNDQIILVTP VTIVHEIDHD SPLYALDRKA VAKDNFEILV TFIYTGDSTG TSHQSRSSYV
PREILWGHRF HDVLEVKRKY YKVNCLQFEG SVEVYAPFCS AKQLDWKDQQ LLHVQKTTPV
ASPPPGPCAS DPKVRRRSFS AVAVVNSKGE NPEEDSTGYD PLDEYKETPY QKAVLTLNRI
SVESQM
//