Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Two pore potassium channel protein sup-9

Gene

sup-9

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potassium channel involved in coordination of muscle contraction (PubMed:14534247). Activity is regulated by sup-18 (PubMed:24586202).2 Publications

GO - Molecular functioni

  • potassium channel activity Source: UniProtKB
  • potassium ion leak channel activity Source: GO_Central

GO - Biological processi

  • potassium ion transport Source: UniProtKB
  • regulation of muscle contraction Source: UniProtKB
  • stabilization of membrane potential Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiR-CEL-1299316. TWIK-releated acid-sensitive K+ channel (TASK).
R-CEL-5576886. Phase 4 - resting membrane potential.

Protein family/group databases

TCDBi1.A.1.9.7. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Two pore potassium channel protein sup-9
Alternative name(s):
Suppressor of unc-93 protein 9
n2P38
Gene namesi
Name:sup-9Imported
ORF Names:F34D6.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiF34D6.3; CE28297; WBGene00006318; sup-9.

Subcellular locationi

  • Membrane Curated; Multi-pass membrane protein Curated

  • Note: Associated with dense bodies.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysis
Transmembranei9 – 2921HelicalSequence analysisAdd
BLAST
Intramembranei80 – 10021Pore-forming; Name=Pore-forming 1Sequence analysisAdd
BLAST
Transmembranei108 – 12821HelicalSequence analysisAdd
BLAST
Topological domaini129 – 15729CytoplasmicSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Intramembranei186 – 20621Pore-forming; Name=Pore-forming 2Sequence analysisAdd
BLAST
Transmembranei220 – 24021HelicalSequence analysisAdd
BLAST
Topological domaini241 – 32989CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • muscle cell projection membrane Source: WormBase
  • striated muscle dense body Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → I in n2282; loss of function. 1 Publication
Mutagenesisi22 – 221G → E in n213; loss of function. 1 Publication
Mutagenesisi23 – 231A → V in lr129; loss of function. 1 Publication
Mutagenesisi27 – 271D → N in n4265 and n3975; loss of function. Not required for sup-18 mediated regulation. 1 Publication
Mutagenesisi41 – 411V → A in n1472; loss of function. 1 Publication
Mutagenesisi44 – 441V → E in n233; loss of function. 1 Publication
Mutagenesisi58 – 581D → V in n2291; loss of function. 1 Publication
Mutagenesisi61 – 611I → S in lr35; loss of function. 1 Publication
Mutagenesisi74 – 741A → V in n1025; loss of function. 1 Publication
Mutagenesisi94 – 941I → N in n1016; loss of function. 1 Publication
Mutagenesisi95 – 951G → D in n1020 and n2354; loss of function. 1 Publication
Mutagenesisi100 – 1001T → I in n3976; loss of function. Not required for sup-18 mediated regulation. 1 Publication
Mutagenesisi101 – 1011P → S in n190, n598, n2353 and n2356; loss of function. 1 Publication
Mutagenesisi103 – 1031T → I in n2347; loss of function. 1 Publication
Mutagenesisi106 – 1061G → E in n1009; loss of function. 1 Publication
Mutagenesisi106 – 1061G → R in n2351; loss of function. 1 Publication
Mutagenesisi109 – 1091F → S in lr45; loss of function. 1 Publication
Mutagenesisi119 – 1191P → S in n2281 and n2345; loss of function. 1 Publication
Mutagenesisi121 – 1211G → R in lr100; loss of function. 1 Publication
Mutagenesisi122 – 1221L → F in n264 and n3977; loss of function. Not required for sup-18 mediated regulation. 2 Publications
Mutagenesisi165 – 1651W → R in lr38; loss of function. 1 Publication
Mutagenesisi172 – 1721G → E in n219; loss of function. 1 Publication
Mutagenesisi172 – 1721G → R in n223 and n2355; loss of function. 1 Publication
Mutagenesisi173 – 1731G → E in n2288; partial loss of function. 1 Publication
Mutagenesisi173 – 1731G → R in n2294 and n2296; loss of function. 1 Publication
Mutagenesisi174 – 1741A → T in n2359; partial loss of function. 1 Publication
Mutagenesisi181 – 1811E → K in n2350; loss of function. 1 Publication
Mutagenesisi190 – 1901Y → F in n2352; loss of function. 1 Publication
Mutagenesisi195 – 1951T → I in n2278 and n2343; loss of function. 1 Publication
Mutagenesisi200 – 2001G → E in n191, n2283 and n2286; loss of function. 1 Publication
Mutagenesisi202 – 2021G → D in n2344; loss of function. 1 Publication
Mutagenesisi202 – 2021G → S in n1469; loss of function. 1 Publication
Mutagenesisi203 – 2031D → A in lr1; loss of function. 1 Publication
Mutagenesisi203 – 2031D → N in n2346 and n2349; loss of function. 1 Publication
Mutagenesisi226 – 2261F → S in n1557; loss of function. 1 Publication
Mutagenesisi230 – 2301G → E in n2176; loss of function. 1 Publication
Mutagenesisi230 – 2301G → R in n2348; loss of function. 1 Publication
Mutagenesisi235 – 2351S → F in n189 and n2358; loss of function. 1 Publication
Mutagenesisi236 – 2361A → M in n2360 and n2361; partial loss of function. 1 Publication
Mutagenesisi236 – 2361A → T in n1550, n3310, e2655 and 2661; gain of function, uncoordinated rubber band response in heterozygous mutants, inviable in homozygous mutants. 1 Publication
Mutagenesisi242 – 2421V → M in lr142; loss of function. 1 Publication
Mutagenesisi244 – 2441R → W in n3935; loss of function. 1 Publication
Mutagenesisi292 – 2921S → A in n4259; loss of function. 1 Publication
Mutagenesisi292 – 2921S → F in n1435, n3942, n4253 and n4254; loss of function. 1 Publication
Mutagenesisi293 – 2931C → A: Loss of function. 1 Publication
Mutagenesisi294 – 2941S → A in n4262; loss of function. 1 Publication
Mutagenesisi295 – 2951C → A: Loss of function. 1 Publication
Mutagenesisi296 – 2961Y → A: Loss of function. 1 Publication
Mutagenesisi303 – 3031L → P in n4269; loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Two pore potassium channel protein sup-9PRO_0000101770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence analysis
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO17185.
PRIDEiO17185.

Expressioni

Tissue specificityi

Low levels along surface of body-wall muscle cells, in vulval and intestinal muscles and, more weakly, in anal depressor and sphincter muscles. Also expressed in a subset of head neurons.2 Publications

Developmental stagei

Expressed in body wall muscles from 3.5-fold stage of embryogenesis with highest levels in late embryos and L1 stage larvae. Lower levels persist to adulthood.1 Publication

Gene expression databases

BgeeiWBGene00006318.

Interactioni

Subunit structurei

May form a complex with the regulatory subunits unc-93 and sup-10.1 Publication

Protein-protein interaction databases

STRINGi6239.F34D6.3.

Structurei

3D structure databases

ProteinModelPortaliO17185.
SMRiO17185. Positions 18-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni289 – 2968May be important for regulation by and/or interaction with sup-101 Publication

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi93 – 986Selectivity filterSequence analysis
Motifi198 – 2036Selectivity filterSequence analysis

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4404. Eukaryota.
ENOG410XRZJ. LUCA.
GeneTreeiENSGT00760000118858.
HOGENOMiHOG000231463.
InParanoidiO17185.
KOiK04919.
OMAiMTMNTED.
OrthoDBiEOG091G08DH.
PhylomeDBiO17185.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR003092. 2pore_dom_K_chnl_TASK.
IPR013099. K_chnl_dom.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PIRSFiPIRSF038061. K_channel_subfamily_K_type. 1 hit.
PRINTSiPR01333. 2POREKCHANEL.
PR01095. TASKCHANNEL.

Sequencei

Sequence statusi: Complete.

O17185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRQNIRTLS LIVCTLTYLL VGAAVFDALE TENEILQRKL VQRVREKLKT
60 70 80 90 100
KYNMSNADYE ILEATIVKSV PHKAGYQWKF SGAFYFATTV ITTIGYGHST
110 120 130 140 150
PMTDAGKVFC MLYALAGIPL GLIMFQSIGE RMNTFAAKLL RFIRRAAGKQ
160 170 180 190 200
PIVTSSDLII FCTGWGGLLI FGGAFMFSSY ENWTYFDAVY YCFVTLTTIG
210 220 230 240 250
FGDYVALQKR GSLQTQPEYV FFSLVFILFG LTVISAAMNL LVLRFLTMNT
260 270 280 290 300
EDERRDEQEA ILAAQGLVRV GDPTADDDFG RLPLSDNVSL ASCSCYQLPD
310 320
EKLRHRHRKH TEPHGGPPTF SGMTTRPKY
Length:329
Mass (Da):36,992
Last modified:October 1, 2001 - v2
Checksum:i338A6D9A577464CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY357729 mRNA. Translation: AAQ84518.1.
AF083652 mRNA. Translation: AAC32863.1.
FO081204 Genomic DNA. Translation: CCD69862.1.
PIRiT32347.
T43509.
RefSeqiNP_494333.1. NM_061932.3.
UniGeneiCel.14253.

Genome annotation databases

EnsemblMetazoaiF34D6.3; F34D6.3; WBGene00006318.
GeneIDi173613.
KEGGicel:CELE_F34D6.3.
UCSCiF34D6.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY357729 mRNA. Translation: AAQ84518.1.
AF083652 mRNA. Translation: AAC32863.1.
FO081204 Genomic DNA. Translation: CCD69862.1.
PIRiT32347.
T43509.
RefSeqiNP_494333.1. NM_061932.3.
UniGeneiCel.14253.

3D structure databases

ProteinModelPortaliO17185.
SMRiO17185. Positions 18-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F34D6.3.

Protein family/group databases

TCDBi1.A.1.9.7. the voltage-gated ion channel (vic) superfamily.

Proteomic databases

PaxDbiO17185.
PRIDEiO17185.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF34D6.3; F34D6.3; WBGene00006318.
GeneIDi173613.
KEGGicel:CELE_F34D6.3.
UCSCiF34D6.3. c. elegans.

Organism-specific databases

CTDi173613.
WormBaseiF34D6.3; CE28297; WBGene00006318; sup-9.

Phylogenomic databases

eggNOGiKOG4404. Eukaryota.
ENOG410XRZJ. LUCA.
GeneTreeiENSGT00760000118858.
HOGENOMiHOG000231463.
InParanoidiO17185.
KOiK04919.
OMAiMTMNTED.
OrthoDBiEOG091G08DH.
PhylomeDBiO17185.

Enzyme and pathway databases

ReactomeiR-CEL-1299316. TWIK-releated acid-sensitive K+ channel (TASK).
R-CEL-5576886. Phase 4 - resting membrane potential.

Miscellaneous databases

PROiO17185.

Gene expression databases

BgeeiWBGene00006318.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR003092. 2pore_dom_K_chnl_TASK.
IPR013099. K_chnl_dom.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PIRSFiPIRSF038061. K_channel_subfamily_K_type. 1 hit.
PRINTSiPR01333. 2POREKCHANEL.
PR01095. TASKCHANNEL.
ProtoNetiSearch...

Entry informationi

Entry nameiSUP9_CAEEL
AccessioniPrimary (citable) accession number: O17185
Secondary accession number(s): O76795
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: October 1, 2001
Last modified: September 7, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

Uncoordinated rubber band response is phenocopied by exposure to the unc-49 agonist muscimol.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.