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Protein

Calcium-gated potassium channel MthK

Gene

mthK

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-gated potassium channel.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi184 – 1841Calcium
Metal bindingi210 – 2101Calcium
Metal bindingi212 – 2121Calcium

GO - Molecular functioni

  • cation transmembrane transporter activity Source: InterPro
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Calcium, Metal-binding, Potassium

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-1522-MONOMER.

Protein family/group databases

TCDBi1.A.1.13.2. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-gated potassium channel MthK
Gene namesi
Name:mthK
Ordered Locus Names:MTH_1520
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicAdd
BLAST
Transmembranei21 – 4121Helical; Name=Outer helix M1Add
BLAST
Topological domaini42 – 487Extracellular
Intramembranei49 – 5810Helical; Pore-formingSequence analysis
Intramembranei59 – 646Pore-formingSequence analysis
Topological domaini65 – 695Extracellular
Transmembranei70 – 9526Helical; Name=Inner helix M2Add
BLAST
Topological domaini96 – 10611CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071M → I: Elimination of the 26 kDa product and reduced levels of channel expression. 1 Publication
Mutagenesisi184 – 1841D → N: At high calcium concentration, mean open time is short and mean closed time is long compared with wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Calcium-gated potassium channel MthKPRO_0000035777Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1101987,EBI-1101987

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-37842N.
STRINGi187420.MTH1520.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 4223Combined sources
Helixi46 – 5712Combined sources
Beta strandi63 – 653Combined sources
Helixi70 – 9829Combined sources
Beta strandi117 – 1226Combined sources
Helixi125 – 1339Combined sources
Turni134 – 1363Combined sources
Beta strandi137 – 1448Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 1546Combined sources
Beta strandi158 – 1625Combined sources
Helixi167 – 1726Combined sources
Beta strandi179 – 1835Combined sources
Helixi188 – 20114Combined sources
Beta strandi203 – 2108Combined sources
Helixi214 – 2163Combined sources
Helixi217 – 2237Combined sources
Beta strandi226 – 2294Combined sources
Helixi231 – 24111Combined sources
Turni242 – 2454Combined sources
Helixi247 – 25610Combined sources
Beta strandi257 – 2615Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi271 – 2733Combined sources
Turni274 – 2774Combined sources
Helixi280 – 2834Combined sources
Helixi285 – 2895Combined sources
Beta strandi292 – 2987Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi317 – 3226Combined sources
Helixi324 – 33411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNQX-ray3.30A/B/C/D/E/F/G/H1-336[»]
2AEFX-ray1.70A/B107-336[»]
2AEJX-ray2.10A/B107-336[»]
2AEMX-ray2.80A107-336[»]
2FY8X-ray2.79A/B/C/D/E/F/G/H107-336[»]
2OGUX-ray3.23A107-336[»]
3KXDX-ray2.20A/B116-336[»]
3LDCX-ray1.45A18-99[»]
3LDDX-ray1.45A18-99[»]
3LDEX-ray2.21A18-99[»]
3OUSX-ray1.75A18-99[»]
3R65X-ray1.80A18-99[»]
3RBXX-ray2.80A/B/C/D/E/F107-336[»]
3RBZX-ray3.40A/B/C/D1-336[»]
4EI2X-ray3.11A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P107-336[»]
4HYOX-ray1.65A/B/C/D/E/F/G/H11-101[»]
4HZ3X-ray1.70A/B/C/D/E/F/G/H11-101[»]
4L73X-ray2.50A/B107-336[»]
4L74X-ray1.84A/B107-336[»]
4L75X-ray2.39A/B/C/D/E/F107-336[»]
4L76X-ray2.99A/B/C/D/E/F107-336[»]
4QE7X-ray2.40A19-99[»]
4QE9X-ray2.15A18-100[»]
4RO0X-ray3.18A/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/j107-336[»]
ProteinModelPortaliO27564.
SMRiO27564. Positions 19-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO27564.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 237121RCK N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini252 – 33685RCK C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 646Selectivity filter

Domaini

The channel is composed of 4 repeated units, each containing a transmembrane pore part and a gating ring part. The gating ring is composed of eight identical RCK (Regulators of K conductance) domains, in an alternating arrangement of one domain from each of the four subunits and four from the intracellular solution. Two protein interfaces between dimers of RCK domains from the pore-forming subunit and from the intracellular solution hold the ring together. One is called the fixed interface and the other the flexible interface. The flexible interface forms a cleft where calcium binds. Upon calcium binding the gating ring undergoes a conformational change that enables it to pull open the inner helices of the pore, allowing ion conduction.

Sequence similaritiesi

Contains 1 RCK C-terminal domain.PROSITE-ProRule annotation
Contains 1 RCK N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG01958. Archaea.
COG1226. LUCA.
KOiK10716.
OMAiIYAFGTK.

Family and domain databases

Gene3Di3.30.70.1450. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR013099. K_chnl_dom.
IPR016040. NAD(P)-bd_dom.
IPR006037. RCK_C.
IPR003148. RCK_N.
[Graphical view]
PfamiPF07885. Ion_trans_2. 1 hit.
PF02080. TrkA_C. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
SUPFAMiSSF116726. SSF116726. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS51202. RCK_C. 1 hit.
PS51201. RCK_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: O27564-1) [UniParc]FASTAAdd to basket

Also known as: Calcium-gated potassium channel

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVLVIEIIRK HLPRVLKVPA TRILLLVLAV IIYGTAGFHF IEGESWTVSL
60 70 80 90 100
YWTFVTIATV GYGDYSPSTP LGMYFTVTLI VLGIGTFAVA VERLLEFLIN
110 120 130 140 150
REQMKLMGLI DVAKSRHVVI CGWSESTLEC LRELRGSEVF VLAEDENVRK
160 170 180 190 200
KVLRSGANFV HGDPTRVSDL EKANVRGARA VIVDLESDSE TIHCILGIRK
210 220 230 240 250
IDESVRIIAE AERYENIEQL RMAGADQVIS PFVISGRLMS RSIDDGYEAM
260 270 280 290 300
FVQDVLAEES TRRMVEVPIP EGSKLEGVSV LDADIHDVTG VIIIGVGRGD
310 320 330
ELIIDPPRDY SFRAGDIILG IGKPEEIERL KNYISA
Length:336
Mass (Da):37,314
Last modified:January 1, 1998 - v1
Checksum:i31FDC5811CB79253
GO
Isoform Soluble (identifier: O27564-2) [UniParc]FASTAAdd to basket

Also known as: RCK domain

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Note: No experimental confirmation available.
Show »
Length:230
Mass (Da):25,416
Checksum:i90462DA6E2BC1649
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 106106Missing in isoform Soluble. CuratedVSP_018901Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85995.1.
PIRiH69069.
RefSeqiWP_010877130.1. NC_000916.1. [O27564-1]

Genome annotation databases

EnsemblBacteriaiAAB85995; AAB85995; MTH_1520.
GeneIDi1471789.
KEGGimth:MTH1520.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85995.1.
PIRiH69069.
RefSeqiWP_010877130.1. NC_000916.1. [O27564-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNQX-ray3.30A/B/C/D/E/F/G/H1-336[»]
2AEFX-ray1.70A/B107-336[»]
2AEJX-ray2.10A/B107-336[»]
2AEMX-ray2.80A107-336[»]
2FY8X-ray2.79A/B/C/D/E/F/G/H107-336[»]
2OGUX-ray3.23A107-336[»]
3KXDX-ray2.20A/B116-336[»]
3LDCX-ray1.45A18-99[»]
3LDDX-ray1.45A18-99[»]
3LDEX-ray2.21A18-99[»]
3OUSX-ray1.75A18-99[»]
3R65X-ray1.80A18-99[»]
3RBXX-ray2.80A/B/C/D/E/F107-336[»]
3RBZX-ray3.40A/B/C/D1-336[»]
4EI2X-ray3.11A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P107-336[»]
4HYOX-ray1.65A/B/C/D/E/F/G/H11-101[»]
4HZ3X-ray1.70A/B/C/D/E/F/G/H11-101[»]
4L73X-ray2.50A/B107-336[»]
4L74X-ray1.84A/B107-336[»]
4L75X-ray2.39A/B/C/D/E/F107-336[»]
4L76X-ray2.99A/B/C/D/E/F107-336[»]
4QE7X-ray2.40A19-99[»]
4QE9X-ray2.15A18-100[»]
4RO0X-ray3.18A/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/j107-336[»]
ProteinModelPortaliO27564.
SMRiO27564. Positions 19-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37842N.
STRINGi187420.MTH1520.

Protein family/group databases

TCDBi1.A.1.13.2. the voltage-gated ion channel (vic) superfamily.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85995; AAB85995; MTH_1520.
GeneIDi1471789.
KEGGimth:MTH1520.

Phylogenomic databases

eggNOGiarCOG01958. Archaea.
COG1226. LUCA.
KOiK10716.
OMAiIYAFGTK.

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-1522-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO27564.

Family and domain databases

Gene3Di3.30.70.1450. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR013099. K_chnl_dom.
IPR016040. NAD(P)-bd_dom.
IPR006037. RCK_C.
IPR003148. RCK_N.
[Graphical view]
PfamiPF07885. Ion_trans_2. 1 hit.
PF02080. TrkA_C. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
SUPFAMiSSF116726. SSF116726. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS51202. RCK_C. 1 hit.
PS51201. RCK_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  2. "Crystal structure and mechanism of a calcium-gated potassium channel."
    Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R.
    Nature 417:515-522(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), MUTAGENESIS OF MET-107 AND ASP-184.

Entry informationi

Entry nameiMTHK_METTH
AccessioniPrimary (citable) accession number: O27564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: April 13, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

It is not known whether calcium is the physiological ligand.
Inhibited by charybdotoxin (CTX), a protein from scorpion venom.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.