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MTHK_METTH
ID   MTHK_METTH              Reviewed;         336 AA.
AC   O27564;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Calcium-gated potassium channel MthK;
GN   Name=mthK; OrderedLocusNames=MTH_1520;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), AND MUTAGENESIS OF MET-107 AND
RP   ASP-184.
RX   PubMed=12037559; DOI=10.1038/417515a;
RA   Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R.;
RT   "Crystal structure and mechanism of a calcium-gated potassium channel.";
RL   Nature 417:515-522(2002).
CC   -!- FUNCTION: Calcium-gated potassium channel.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       O27564; O27564: mthK; NbExp=3; IntAct=EBI-1101987, EBI-1101987;
CC       O27564-1; O27564-1: mthK; NbExp=11; IntAct=EBI-15621899, EBI-15621899;
CC       O27564-2; O27564-2: mthK; NbExp=2; IntAct=EBI-15737903, EBI-15737903;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=Calcium-gated potassium channel;
CC         IsoId=O27564-1; Sequence=Displayed;
CC       Name=Soluble; Synonyms=RCK domain;
CC         IsoId=O27564-2; Sequence=VSP_018901;
CC   -!- DOMAIN: The channel is composed of 4 repeated units, each containing a
CC       transmembrane pore part and a gating ring part. The gating ring is
CC       composed of eight identical RCK (Regulators of K conductance) domains,
CC       in an alternating arrangement of one domain from each of the four
CC       subunits and four from the intracellular solution. Two protein
CC       interfaces between dimers of RCK domains from the pore-forming subunit
CC       and from the intracellular solution hold the ring together. One is
CC       called the fixed interface and the other the flexible interface. The
CC       flexible interface forms a cleft where calcium binds. Upon calcium
CC       binding the gating ring undergoes a conformational change that enables
CC       it to pull open the inner helices of the pore, allowing ion conduction.
CC   -!- MISCELLANEOUS: It is not known whether calcium is the physiological
CC       ligand.
CC   -!- MISCELLANEOUS: Inhibited by charybdotoxin (CTX), a protein from
CC       scorpion venom.
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DR   EMBL; AE000666; AAB85995.1; -; Genomic_DNA.
DR   PIR; H69069; H69069.
DR   RefSeq; WP_010877130.1; NC_000916.1.
DR   PDB; 1LNQ; X-ray; 3.30 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 2AEF; X-ray; 1.70 A; A/B=107-336.
DR   PDB; 2AEJ; X-ray; 2.10 A; A/B=107-336.
DR   PDB; 2AEM; X-ray; 2.80 A; A=107-336.
DR   PDB; 2FY8; X-ray; 2.79 A; A/B/C/D/E/F/G/H=107-336.
DR   PDB; 2OGU; X-ray; 3.23 A; A=107-336.
DR   PDB; 3KXD; X-ray; 2.20 A; A/B=116-336.
DR   PDB; 3LDC; X-ray; 1.45 A; A=18-99.
DR   PDB; 3LDD; X-ray; 1.45 A; A=18-99.
DR   PDB; 3LDE; X-ray; 2.21 A; A=18-99.
DR   PDB; 3OUS; X-ray; 1.75 A; A=18-99.
DR   PDB; 3R65; X-ray; 1.80 A; A=18-99.
DR   PDB; 3RBX; X-ray; 2.80 A; A/B/C/D/E/F=107-336.
DR   PDB; 3RBZ; X-ray; 3.40 A; A/B/C/D=1-336.
DR   PDB; 4EI2; X-ray; 3.11 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=107-336.
DR   PDB; 4HYO; X-ray; 1.65 A; A/B/C/D/E/F/G/H=11-101.
DR   PDB; 4HZ3; X-ray; 1.70 A; A/B/C/D/E/F/G/H=11-101.
DR   PDB; 4L73; X-ray; 2.50 A; A/B=107-336.
DR   PDB; 4L74; X-ray; 1.84 A; A/B=107-336.
DR   PDB; 4L75; X-ray; 2.39 A; A/B/C/D/E/F=107-336.
DR   PDB; 4L76; X-ray; 2.99 A; A/B/C/D/E/F=107-336.
DR   PDB; 4QE7; X-ray; 2.40 A; A=19-99.
DR   PDB; 4QE9; X-ray; 2.15 A; A=18-100.
DR   PDB; 4RO0; X-ray; 3.18 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/a/b/c/d/e/f/g/h/i/j=107-336.
DR   PDB; 6OLY; X-ray; 3.11 A; A/B/C/D=1-336.
DR   PDB; 6U5N; EM; 3.20 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6U5P; EM; 3.30 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6U5R; EM; 3.60 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6U68; EM; 4.50 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6U6D; EM; 3.60 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6U6E; EM; 6.30 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6U6H; EM; 5.00 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6U9P; X-ray; 1.65 A; A=18-99.
DR   PDB; 6U9T; X-ray; 1.55 A; A=18-99.
DR   PDB; 6U9Y; X-ray; 1.80 A; A=18-99.
DR   PDB; 6U9Z; X-ray; 1.95 A; A=18-99.
DR   PDB; 6UWN; EM; 3.50 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6UX4; EM; 3.50 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6UX7; EM; 6.70 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6UXA; EM; 4.50 A; A/B/C/D/E/F/G/H=1-336.
DR   PDB; 6UXB; EM; 4.90 A; A/B/C/D/E/F/G/H=1-336.
DR   PDBsum; 1LNQ; -.
DR   PDBsum; 2AEF; -.
DR   PDBsum; 2AEJ; -.
DR   PDBsum; 2AEM; -.
DR   PDBsum; 2FY8; -.
DR   PDBsum; 2OGU; -.
DR   PDBsum; 3KXD; -.
DR   PDBsum; 3LDC; -.
DR   PDBsum; 3LDD; -.
DR   PDBsum; 3LDE; -.
DR   PDBsum; 3OUS; -.
DR   PDBsum; 3R65; -.
DR   PDBsum; 3RBX; -.
DR   PDBsum; 3RBZ; -.
DR   PDBsum; 4EI2; -.
DR   PDBsum; 4HYO; -.
DR   PDBsum; 4HZ3; -.
DR   PDBsum; 4L73; -.
DR   PDBsum; 4L74; -.
DR   PDBsum; 4L75; -.
DR   PDBsum; 4L76; -.
DR   PDBsum; 4QE7; -.
DR   PDBsum; 4QE9; -.
DR   PDBsum; 4RO0; -.
DR   PDBsum; 6OLY; -.
DR   PDBsum; 6U5N; -.
DR   PDBsum; 6U5P; -.
DR   PDBsum; 6U5R; -.
DR   PDBsum; 6U68; -.
DR   PDBsum; 6U6D; -.
DR   PDBsum; 6U6E; -.
DR   PDBsum; 6U6H; -.
DR   PDBsum; 6U9P; -.
DR   PDBsum; 6U9T; -.
DR   PDBsum; 6U9Y; -.
DR   PDBsum; 6U9Z; -.
DR   PDBsum; 6UWN; -.
DR   PDBsum; 6UX4; -.
DR   PDBsum; 6UX7; -.
DR   PDBsum; 6UXA; -.
DR   PDBsum; 6UXB; -.
DR   AlphaFoldDB; O27564; -.
DR   SMR; O27564; -.
DR   DIP; DIP-37842N; -.
DR   TCDB; 1.A.1.13.2; the voltage-gated ion channel (vic) superfamily.
DR   EnsemblBacteria; AAB85995; AAB85995; MTH_1520.
DR   GeneID; 1471789; -.
DR   KEGG; mth:MTH_1520; -.
DR   PATRIC; fig|187420.15.peg.1483; -.
DR   HOGENOM; CLU_050982_1_0_2; -.
DR   OMA; VFEGIWW; -.
DR   EvolutionaryTrace; O27564; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1450; -; 1.
DR   InterPro; IPR013099; K_chnl_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006037; RCK_C.
DR   InterPro; IPR036721; RCK_C_sf.
DR   InterPro; IPR003148; RCK_N.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   Pfam; PF02080; TrkA_C; 1.
DR   Pfam; PF02254; TrkA_N; 1.
DR   SUPFAM; SSF116726; SSF116726; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51202; RCK_C; 1.
DR   PROSITE; PS51201; RCK_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Calcium; Cell membrane; Ion channel;
KW   Ion transport; Membrane; Metal-binding; Potassium; Potassium transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..336
FT                   /note="Calcium-gated potassium channel MthK"
FT                   /id="PRO_0000035777"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT   TRANSMEM        21..41
FT                   /note="Helical; Name=Outer helix M1"
FT   TOPO_DOM        42..48
FT                   /note="Extracellular"
FT   INTRAMEM        49..58
FT                   /note="Helical; Pore-forming"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        59..64
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..69
FT                   /note="Extracellular"
FT   TRANSMEM        70..95
FT                   /note="Helical; Name=Inner helix M2"
FT   TOPO_DOM        96..106
FT                   /note="Cytoplasmic"
FT   DOMAIN          117..237
FT                   /note="RCK N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT   DOMAIN          252..336
FT                   /note="RCK C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   MOTIF           59..64
FT                   /note="Selectivity filter"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   VAR_SEQ         1..106
FT                   /note="Missing (in isoform Soluble)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018901"
FT   MUTAGEN         107
FT                   /note="M->I: Elimination of the 26 kDa product and reduced
FT                   levels of channel expression."
FT                   /evidence="ECO:0000269|PubMed:12037559"
FT   MUTAGEN         184
FT                   /note="D->N: At high calcium concentration, mean open time
FT                   is short and mean closed time is long compared with wild-
FT                   type."
FT                   /evidence="ECO:0000269|PubMed:12037559"
FT   HELIX           20..42
FT                   /evidence="ECO:0007829|PDB:3LDC"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:3LDC"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:3LDD"
FT   HELIX           70..98
FT                   /evidence="ECO:0007829|PDB:3LDC"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:6OLY"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:4L75"
FT   STRAND          137..144
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           149..154
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          158..162
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           167..172
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           188..201
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          203..210
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           217..223
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           231..241
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   TURN            242..245
FT                   /evidence="ECO:0007829|PDB:2FY8"
FT   HELIX           247..256
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          257..261
FT                   /evidence="ECO:0007829|PDB:2OGU"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          271..273
FT                   /evidence="ECO:0007829|PDB:2FY8"
FT   TURN            274..277
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           280..283
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           285..289
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          292..298
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:2AEF"
FT   HELIX           324..334
FT                   /evidence="ECO:0007829|PDB:2AEF"
SQ   SEQUENCE   336 AA;  37314 MW;  31FDC5811CB79253 CRC64;
     MVLVIEIIRK HLPRVLKVPA TRILLLVLAV IIYGTAGFHF IEGESWTVSL YWTFVTIATV
     GYGDYSPSTP LGMYFTVTLI VLGIGTFAVA VERLLEFLIN REQMKLMGLI DVAKSRHVVI
     CGWSESTLEC LRELRGSEVF VLAEDENVRK KVLRSGANFV HGDPTRVSDL EKANVRGARA
     VIVDLESDSE TIHCILGIRK IDESVRIIAE AERYENIEQL RMAGADQVIS PFVISGRLMS
     RSIDDGYEAM FVQDVLAEES TRRMVEVPIP EGSKLEGVSV LDADIHDVTG VIIIGVGRGD
     ELIIDPPRDY SFRAGDIILG IGKPEEIERL KNYISA
 
 
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