IRK10_MAGMG
ID IRK10_MAGMG Reviewed; 295 AA.
AC D9N164; D9N165; D9N166;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Inward rectifier potassium channel Kirbac3.1;
OS Magnetospirillum magnetotacticum (Aquaspirillum magnetotacticum).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=188;
RN [1]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-75; ALA-78; PHE-88;
RP THR-93; GLY-98; LEU-118; MET-121; GLY-123; ALA-125; SER-129; ILE-150;
RP VAL-181 AND SER-205.
RX PubMed=20876570; DOI=10.1074/jbc.m110.175687;
RA Paynter J.J., Andres-Enguix I., Fowler P.W., Tottey S., Cheng W.,
RA Enkvetchakul D., Bavro V.N., Kusakabe Y., Sansom M.S., Robinson N.J.,
RA Nichols C.G., Tucker S.J.;
RT "Functional complementation and genetic deletion studies of KirBac
RT channels: activatory mutations highlight gating-sensitive domains.";
RL J. Biol. Chem. 285:40754-40761(2010).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (9 ANGSTROMS), SUBCELLULAR LOCATION,
RP TOPOLOGY, AND SUBUNIT.
RX PubMed=16216578; DOI=10.1016/j.str.2005.07.011;
RA Kuo A., Domene C., Johnson L.N., Doyle D.A., Venien-Bryan C.;
RT "Two different conformational states of the KirBac3.1 potassium channel
RT revealed by electron crystallography.";
RL Structure 13:1463-1472(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, DOMAIN,
RP POLYAMINE-BINDING, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=20564790; DOI=10.1016/j.cell.2010.05.003;
RA Clarke O.B., Caputo A.T., Hill A.P., Vandenberg J.I., Smith B.J.,
RA Gulbis J.M.;
RT "Domain reorientation and rotation of an intracellular assembly regulate
RT conduction in Kir potassium channels.";
RL Cell 141:1018-1029(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF MUTANT ARG-129, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF TYR-38 AND
RP SER-129.
RX PubMed=22231399; DOI=10.1038/nsmb.2208;
RA Bavro V.N., De Zorzi R., Schmidt M.R., Muniz J.R., Zubcevic L.,
RA Sansom M.S., Venien-Bryan C., Tucker S.J.;
RT "Structure of a KirBac potassium channel with an open bundle crossing
RT indicates a mechanism of channel gating.";
RL Nat. Struct. Mol. Biol. 19:158-163(2012).
CC -!- FUNCTION: Inward rectifier potassium channel that mediates potassium
CC uptake into the cell. Inward rectifier potassium channels are
CC characterized by a greater tendency to allow potassium to flow into the
CC cell rather than out of it. The inward rectification may be achieved by
CC the blockage of outward current by cytoplasmic divalent metal ions and
CC polyamines. Complements an E.coli mutant that is defective in K(+)
CC uptake. {ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570,
CC ECO:0000269|PubMed:22231399}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16216578,
CC ECO:0000269|PubMed:22231399}.
CC -!- INTERACTION:
CC D9N164; D9N164: -; NbExp=2; IntAct=EBI-15558188, EBI-15558188;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16216578,
CC ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570,
CC ECO:0000269|PubMed:22231399}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16216578, ECO:0000269|PubMed:20564790,
CC ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}.
CC -!- DOMAIN: A conformation change implying rotational movement of the
CC cytoplasmic domains plays an important role in channel opening and
CC closing. Release of polyamines from their binding sites on the
CC cytoplasmic domain may block the ion permeation pathway, preventing the
CC efflux of intracellular potassium ions. {ECO:0000269|PubMed:20564790}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ11 subfamily. {ECO:0000305}.
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DR PDB; 1XL6; X-ray; 2.85 A; A/B=1-295.
DR PDB; 2WLH; X-ray; 3.28 A; A=5-295.
DR PDB; 2WLI; X-ray; 3.09 A; A/B=5-295.
DR PDB; 2WLJ; X-ray; 2.60 A; A/B=1-295.
DR PDB; 2WLK; X-ray; 2.80 A; A/B=1-295.
DR PDB; 2WLM; X-ray; 3.61 A; A/B/C/D=5-295.
DR PDB; 2WLN; X-ray; 3.44 A; A/B/C/D/E/F/G/H=5-295.
DR PDB; 2WLO; X-ray; 4.04 A; A/B=1-295.
DR PDB; 2X6A; X-ray; 3.10 A; A=5-295.
DR PDB; 2X6B; X-ray; 3.30 A; A=5-295.
DR PDB; 2X6C; X-ray; 2.70 A; A=5-295.
DR PDB; 3ZRS; X-ray; 3.05 A; A=1-295.
DR PDB; 4LP8; X-ray; 2.46 A; A=1-295.
DR PDB; 6O9T; X-ray; 4.01 A; A=1-295.
DR PDB; 6O9U; X-ray; 2.00 A; A=1-295.
DR PDB; 6O9V; X-ray; 3.09 A; A/B=1-295.
DR PDB; 7ADI; X-ray; 2.80 A; A/B=1-295.
DR PDB; 7N9K; X-ray; 2.72 A; A=1-295.
DR PDB; 7N9L; X-ray; 2.40 A; A=1-295.
DR PDBsum; 1XL6; -.
DR PDBsum; 2WLH; -.
DR PDBsum; 2WLI; -.
DR PDBsum; 2WLJ; -.
DR PDBsum; 2WLK; -.
DR PDBsum; 2WLM; -.
DR PDBsum; 2WLN; -.
DR PDBsum; 2WLO; -.
DR PDBsum; 2X6A; -.
DR PDBsum; 2X6B; -.
DR PDBsum; 2X6C; -.
DR PDBsum; 3ZRS; -.
DR PDBsum; 4LP8; -.
DR PDBsum; 6O9T; -.
DR PDBsum; 6O9U; -.
DR PDBsum; 6O9V; -.
DR PDBsum; 7ADI; -.
DR PDBsum; 7N9K; -.
DR PDBsum; 7N9L; -.
DR AlphaFoldDB; D9N164; -.
DR SMR; D9N164; -.
DR DIP; DIP-59916N; -.
DR TCDB; 1.A.2.2.2; the inward rectifier k(+) channel (irk-c) family.
DR EvolutionaryTrace; D9N164; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IPR013099; K_chnl_dom.
DR InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..295
FT /note="Inward rectifier potassium channel Kirbac3.1"
FT /id="PRO_0000422432"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT TRANSMEM 48..69
FT /note="Helical"
FT TOPO_DOM 70..82
FT /note="Extracellular"
FT INTRAMEM 83..95
FT /note="Helical; Pore-forming"
FT TRANSMEM 107..131
FT /note="Helical"
FT TOPO_DOM 132..295
FT /note="Cytoplasmic"
FT MOTIF 96..100
FT /note="Selectivity filter"
FT MUTAGEN 38
FT /note="Y->F: Decreases channel activity."
FT /evidence="ECO:0000269|PubMed:22231399"
FT MUTAGEN 75
FT /note="I->S: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 78
FT /note="A->P: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 88
FT /note="F->L: Strongly increased channel conductance due to
FT defective gating."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 93
FT /note="T->I: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 98
FT /note="G->D: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 118
FT /note="L->Q: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 121
FT /note="M->K: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 123
FT /note="G->D: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 125
FT /note="A->E: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 129
FT /note="S->D,E,K,R: Promotes open channel conformation."
FT /evidence="ECO:0000269|PubMed:20876570,
FT ECO:0000269|PubMed:22231399"
FT MUTAGEN 150
FT /note="I->F: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 181
FT /note="V->I: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT MUTAGEN 205
FT /note="S->L: Increased channel conductance."
FT /evidence="ECO:0000269|PubMed:20876570"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2WLI"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2WLJ"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:6O9U"
FT HELIX 46..71
FT /evidence="ECO:0007829|PDB:6O9U"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6O9U"
FT HELIX 106..135
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 171..185
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2X6C"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:6O9U"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:6O9U"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:6O9U"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:6O9U"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:6O9U"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6O9U"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:2WLK"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6O9U"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6O9U"
SQ SEQUENCE 295 AA; 32915 MW; 516385C96C5F8BE2 CRC64;
MTGGMKPPAR KPRILNSDGS SNITRLGLEK RGWLDDHYHD LLTVSWPVFI TLITGLYLVT
NALFALAYLA CGDVIENARP GSFTDAFFFS VQTMATIGYG KLIPIGPLAN TLVTLEALCG
MLGLAVAASL IYARFTRPTA GVLFSSRMVI SDFEGKPTLM MRLANLRIEQ IIEADVHLVL
VRSEISQEGM VFRRFHDLTL TRSRSPIFSL SWTVMHPIDH HSPIYGETDE TLRNSHSEFL
VLFTGHHEAF AQNVHARHAY SCDEIIWGGH FVDVFTTLPD GRRALDLGKF HEIAQ
