Potassium voltage-gated channel subfamily H member 2

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O08962 (KCNH2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Potassium voltage-gated channel subfamily H member 2

Alternative name(s):
Ether-a-go-go-related gene potassium channel 1
Short name=ERG-1
Short name=Eag-related protein 1
Short name=Ether-a-go-go-related protein 1
Short name=RERG
Short name=r-ERG
Voltage-gated potassium channel subunit Kv11.1

Gene names

Name:	Kcnh2
Synonyms:	Erg

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) By similarity.
Subunit structure	The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits. Heteromultimer with KCNH6/ERG2 and KCNH7/ERG3. Heteromultimer with KCNE1 and KCNE2 By similarity. Interacts with ALG10B. Interacts with CANX By similarity. Ref.4 Ref.5
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Highly expressed in brain and testis, slightly less so in heart, adrenal, retina and thymus. Detected at lower levels in lung, soleus, tibialis, and at very low levels in cornea and lens. A shorter transcript is detected in skeletal muscle. Found in pituitary. Ref.3
Domain	The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
Post-translational modification	Phosphorylated on serine and threonine residues By similarity.
Sequence similarities	Belongs to the potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily. [View classification] Contains 1 cyclic nucleotide-binding domain. Contains 1 PAC (PAS-associated C-terminal) domain. Contains 1 PAS (PER-ARNT-SIM) domain.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein heterooligomerization Inferred from direct assay Ref.4. Source: RGD regulation of membrane potential Inferred from direct assay PubMed 11804849. Source: RGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	integral to plasma membrane Inferred from direct assay PubMed 11804849. Source: RGD
Molecular_function	inward rectifier potassium channel activity Inferred from direct assay PubMed 15677682. Source: RGD phosphorelay sensor kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1163

1163

Potassium voltage-gated channel subfamily H member 2

PRO_0000054003

Regions

Topological domain

1 – 405

405

Cytoplasmic Potential

Transmembrane

406 – 426

Helical; Name=Segment S1; Potential

Topological domain

427 – 452

Extracellular Potential

Transmembrane

453 – 473

Helical; Name=Segment S2; Potential

Topological domain

474 – 497

Cytoplasmic Potential

Transmembrane

498 – 518

Helical; Name=Segment S3; Potential

Topological domain

519 – 522

Extracellular Potential

Transmembrane

523 – 543

Helical; Voltage-sensor; Name=Segment S4; Potential

Topological domain

544 – 549

Cytoplasmic Potential

Transmembrane

550 – 570

Helical; Name=Segment S5; Potential

Topological domain

571 – 613

Extracellular Potential

Intramembrane

614 – 634

Pore-forming; Name=Segment H5; Potential

Topological domain

635 – 640

Extracellular Potential

Transmembrane

641 – 661

Helical; Name=Segment S6; Potential

Topological domain

662 – 1163

502

Cytoplasmic Potential

Domain

17 – 88

PAS

Domain

92 – 144

PAC

Nucleotide binding

744 – 861

118

cNMP

Motif

626 – 631

Selectivity filter By similarity

Amino acid modifications

Modified residue

322

Phosphoserine By similarity

Glycosylation

600

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

630

G → S: Dominant negative mutant; abolishes ERG current. Ref.4

Sequence conflict

411

V → A in AAC53160. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

O08962 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: F0D75B0B532D9EA2
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FASTA

1,163

126,952

        10         20         30         40         50         60 
MPVRRGHVAP QNTFLDTIIR KFEGQSRKFI IANARVENCA VIYCNDGFCE LCGYSRAEVM 

        70         80         90        100        110        120 
QRPCTCDFLH GPRTQRRAAA QIAQALLGAE ERKVEIAFYR KDGSCFLCLV DVVPVKNEDG 

       130        140        150        160        170        180 
AVIMFILNFE VVMEKDMVGS PAHDTNHRGP STSWLASGRA KTFRLKLPAL LALTARESPM 

       190        200        210        220        230        240 
RTGSTGSPGA PGAVVVDVDL TPAAPSSESL ALDEVSAMDN HVAGLGPAEE RRALVGPASA 

       250        260        270        280        290        300 
SPVASIPGPH PSPRAQSLNP DASGSSCSLA RTRSRESCAS VRRASSADDI EAMRAGALPL 

       310        320        330        340        350        360 
PPRHASTGAM HPLRSGLLNS TSDSDLVRYR TISKIPQITL NFVDLKGDPF LASPTSDREI 

       370        380        390        400        410        420 
IAPKIKERTH NVTEKVTQVL SLGADVLPEY KLQAPRIHRW TILHYSPFKA VWDWLILLLV 

       430        440        450        460        470        480 
IYTAVFTPYS AAFLLKETED GSQAPDCGYA CQPLAVVDLL VDIMFIVDIL INFRTTYVNA 

       490        500        510        520        530        540 
NEEVVSHPGR IAVHYFKGWF LIDMVAAIPF DLLIFGSGSE ELIGLLKTAR LLRLVRVARK 

       550        560        570        580        590        600 
LDRYSEYGAA VLFLLMCTFA LIAHWLACIW YAIGNMEQPH MDSHIGWLHN LGDQIGKPYN 

       610        620        630        640        650        660 
SSGLGGPSIK DKYVTALYFT FSSLTSVGFG NVSPNTNSEK IFSICVMLIG SLMYASIFGN 

       670        680        690        700        710        720 
VSAIIQRLYS GTARYHTQML RVREFIRFHQ IPNPLRQRLE EYFQHAWSYT NGIDMNAVLK 

       730        740        750        760        770        780 
GFPECLQADI CLHLNRSLLQ HCKPFRGATK GCLRALAMKF KTTHAPPGDT LVHAGDLLTA 

       790        800        810        820        830        840 
LYFISRGSIE ILRGDVVVAI LGKNDIFGEP LNLYARPGKS NGDVRALTYC DLHKIHRDDL 

       850        860        870        880        890        900 
LEVLDMYPEF SDHFWSSLEI TFNLRDTNMI PGSPSSAELE SGFNRQRKRK LSFRRRTDKD 

       910        920        930        940        950        960 
TEQPGEVSAL GQGPARVGPG PSCRGQPGGP WGESPSSGPS SPESSEDEGP GRSSSPLRLV 

       970        980        990       1000       1010       1020 
PFSSPRPPGD SPGGEPLTED GEKSSDTCNP LSGAFSGVSN IFSFWGDSRG RQYQELPRCP 

      1030       1040       1050       1060       1070       1080 
APAPSLLNIP LSSPGRRSRG DVESRLDALQ RQLNRLETRL SADMATVLQL LQRQMTLVPP 

      1090       1100       1110       1120       1130       1140 
AYSAVTTPGP GPTSTSPLLP VGPVPTLTLD SLSQVSQFVA FEELPAGAPE LPQDGPTRRL 

      1150       1160 
SLPGQLGALT SQPLHRHGSD PGS

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References

[1]	"RERG is a molecular correlate of the inward-rectifying K current in clonal rat pituitary cells." Bauer C.K., Engeland B., Wulfsen I., Ludwig J., Pongs O., Schwarz J.R. Recept. Channels 6:19-29(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain cortex.
[2]	"Tissue and species distribution of mRNA for the IKr-like K+ channel, erg." Wymore R.S., Gintant G.A., Wymore R.T., Dixon J.E., McKinnon D., Cohen I.S. Circ. Res. 80:261-268(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 409-568.
[3]	"Expression of mRNA for voltage-dependent and inward-rectifying K channels in GH3/B6 cells and rat pituitary." Wulfsen I., Hauber H.-P., Schiemann D., Bauer C.K., Schwarz J.R. J. Neuroendocrinol. 12:263-272(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Erg1, erg2 and erg3 K channel subunits are able to form heteromultimers." Wimmers S., Wulfsen I., Bauer C.K., Schwarz J.R. Pflugers Arch. 441:450-455(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNH6 AND KCNH7, MUTAGENESIS OF GLY-630.
[5]	"The IKr drug response is modulated by KCR1 in transfected cardiac and noncardiac cell lines." Kupershmidt S., Yang I.C.-H., Hayashi K., Wei J., Chanthaphaychith S., Petersen C.I., Johns D.C., George A.L. Jr., Roden D.M., Balser J.R. FASEB J. 17:2263-2265(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ALG10B.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z96106 mRNA. Translation: CAB09536.1. U75210 mRNA. Translation: AAC53160.1.
IPI	IPI00197531.
RefSeq	NP_446401.1. NM_053949.1.
UniGene	Rn.10970.
3D structure databases
ProteinModelPortal	O08962.
SMR	O08962. Positions 26-135, 572-613.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000013800.
PTM databases
PhosphoSite	O08962.
Proteomic databases
PaxDb	O08962.
PRIDE	O08962.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	117018.
KEGG	rno:117018.
Organism-specific databases
CTD	3757.
RGD	621414. Kcnh2.
Phylogenomic databases
eggNOG	COG2202.
HOGENOM	HOG000230793.
HOVERGEN	HBG052232.
InParanoid	O08962.
KO	K04905.
OrthoDB	EOG4RJG0T.
Gene expression databases
ArrayExpress	O08962.
Genevestigator	O08962.
GermOnline	ENSRNOG00000009872. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.120.10. 2 hits.
InterPro	IPR018490. cNMP-bd-like. IPR000595. cNMP-bd_dom. IPR005821. Ion_trans_dom. IPR003938. K_chnl_volt-dep_EAG/ELK/ERG. IPR003967. K_chnl_volt-dep_ERG. IPR001610. PAC. IPR000014. PAS. IPR000700. PAS-assoc_C. IPR014710. RmlC-like_jellyroll. [Graphical view]
Pfam	PF00027. cNMP_binding. 1 hit. PF00520. Ion_trans. 1 hit. [Graphical view]
PRINTS	PR01463. EAGCHANLFMLY. PR01470. ERGCHANNEL.
SMART	SM00100. cNMP. 1 hit. SM00086. PAC. 1 hit. SM00091. PAS. 1 hit. [Graphical view]
SUPFAM	SSF51206. cNMP_binding. 1 hit.
TIGRFAMs	TIGR00229. sensory_box. 1 hit.
PROSITE	PS00888. CNMP_BINDING_1. False negative. PS00889. CNMP_BINDING_2. False negative. PS50042. CNMP_BINDING_3. 1 hit. PS50113. PAC. 1 hit. PS50112. PAS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	619763.

Entry information

Entry name

KCNH2_RAT

Accession

Primary (citable) accession number: O08962
Secondary accession number(s): O08720

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents