Potassium voltage-gated channel subfamily B member 1

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P15387 (KCNB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. History...

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

Documents (2) |

Third-party data

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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 B member 1

Alternative name(s):
Delayed rectifier potassium channel 1
Short name=DRK1
Voltage-gated potassium channel subunit Kv2.1

Gene names

Name:

Kcnb1

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	857 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates the voltage-dependent potassium ion permeability of excitable membranes. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Ref.4 Ref.5 Ref.6 Ref.7
Subunit structure	Heteromultimer with KCNG2, KCNG3, KCNG4, KCNS1, KCNS2, KCNS3 and KCNV2 By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	In the brain, the greatest density occurs in the cerebral cortex, followed by the hippocampus, cerebellum, and olfactory bulb. In peripheral tissues it is most prominent in retina and kidney. Also present in cardiac muscle tissue of the atrium and ventricle and in skeletal muscle.
Developmental stage	Levels remain constant throughout postnatal development. Ref.6
Domain	The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Post-translational modification	Highly phosphorylated on serine residues in the C-terminal. Differential phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are all regulated by calcineurin-mediated dephosphorylation. Particularly, Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/ dephosphorylation activities. Tyr-128 can be dephosphorylated by PTPalpha and cyt-PTPepsilon. Phosphorylation levels on Ser-607 are supersensitive to neuronal activity. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5. Levels then increase to reach adult levels by P14. Phosphorylation levels on Ser-564 and Ser-607 are greatly reduced during seizures, by 40% and 85% respectively. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Miscellaneous	As phosphorylation levels on Ser-607 are highly sensitive to changes in neuronal activity, the immunoreactivity of Ser-607P could serve as a bidirectional biomarker for neuronal activity.
Sequence similarities	Belongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. [View classification]
Sequence caution	The sequence CAA34497.1 differs from that shown. Reason: Erroneous initiation.

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	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein homooligomerization Inferred from electronic annotation. Source: InterPro protein oligomerization Inferred from mutant phenotype PubMed 12127166. Source: RGD
Cellular_component	dendrite Inferred from direct assay PubMed 8463836. Source: RGD dendrite membrane Inferred from direct assay PubMed 14608003. Source: RGD neuronal cell body membrane Inferred from direct assay PubMed 14608003. Source: RGD postsynaptic membrane Inferred from direct assay PubMed 14608003. Source: RGD voltage-gated potassium channel complex Inferred from electronic annotation. Source: InterPro
Molecular_function	delayed rectifier potassium channel activity Inferred from direct assay PubMed 8189205. Source: RGD outward rectifier potassium channel activity Inferred from mutant phenotype PubMed 12127166. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 857

857

Potassium voltage-gated channel subfamily B member 1

PRO_0000054046

Regions

Topological domain

1 – 186

186

Cytoplasmic Potential

Transmembrane

187 – 208

Helical; Name=Segment S1; Potential

Transmembrane

229 – 250

Helical; Name=Segment S2; Potential

Topological domain

251 – 260

Cytoplasmic Potential

Transmembrane

261 – 282

Helical; Name=Segment S3; Potential

Transmembrane

295 – 316

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

Topological domain

317 – 330

Cytoplasmic Potential

Transmembrane

331 – 352

Helical; Name=Segment S5; Potential

Intramembrane

365 – 385

Pore-forming; Name=Segment H5; Potential

Transmembrane

393 – 414

Helical; Name=Segment S6; Potential

Topological domain

415 – 857

443

Cytoplasmic Potential

Motif

377 – 382

Selectivity filter By similarity

Compositional bias

517 – 520

Poly-Ser

Compositional bias

700 – 705

Poly-Ala

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.7 Ref.8

Modified residue

128

Phosphotyrosine; by Src Ref.5

Modified residue

457

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

484

Phosphoserine Ref.7

Modified residue

496

Phosphoserine Ref.7

Modified residue

503

Phosphoserine Ref.7

Modified residue

520

Phosphoserine Ref.7

Modified residue

541

Phosphoserine Ref.7 Ref.8

Modified residue

567

Phosphoserine Ref.6 Ref.7

Modified residue

590

Phosphoserine Ref.7

Modified residue

607

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

655

Phosphoserine Ref.7 Ref.8

Modified residue

719

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

771

Phosphoserine Ref.7

Modified residue

799

Phosphoserine Ref.7 Ref.8

Modified residue

804

Phosphoserine Ref.7 Ref.8

Modified residue

836

Phosphothreonine Ref.7 Ref.8

Experimental info

Mutagenesis

S → A: Shift in voltage-dependent gating on calcineurin activation and steady-state inactivation. Additive effect on activation and steady-state inactivation; when associated with A-457. Ref.7

Mutagenesis

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

128

Y → F: Significant loss of Src-mediated phosphorylation. Ref.5

Mutagenesis

444

S → A: No effect on Src-mediated phosphorylation. Ref.4

Mutagenesis

457

S → A: Shift in voltage-dependent gating on calcineurin activation and steady-state inactivation. Additive effect on activation and steady-state inactivation; when associated with A-15. Ref.7

Mutagenesis

457

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

484

S → A: No change in calcineurin-dependent regulation of voltage-dependent gating. Ref.7

Mutagenesis

484

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

496

S → A: No effect on Src-mediated phosphorylation. Ref.4

Mutagenesis

541

S → A: Shift in voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

541

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

567

S → A: Shift in voltage-dependent gating on calcineurin activation and steady-state inactivation. Larger effect on activation and steady-state inactivation; when associated with A-607. Ref.7

Mutagenesis

567

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

607

S → A: Shift in voltage-dependent gating on calcineurin activation and steady-state inactivation. Larger effect on activation and steady-state inactivation; when associated with A-567. Ref.7

Mutagenesis

607

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

655

S → A: Shift in voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

655

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

719

S → A: Shift in voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

771

S → A: No change in calcineurin-dependent regulation of voltage-dependent gating. Ref.7

Mutagenesis

771

S → D: Resists voltage-dependent gating on calcineurin activation and steady-state inactivation. Ref.7

Mutagenesis

804

S → A: No change in calcineurin-dependent regulation of voltage-dependent gating. Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P15387 [UniParc].

Last modified October 25, 2002. Version 3.
Checksum: B3C5B0839AB15FD0
Show »

FASTA

857

95,637

        10         20         30         40         50         60 
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL 

        70         80         90        100        110        120 
RDCNTHDSLL QVCDDYSLED NEYFFDRHPG AFTSILNFYR TGRLHMMEEM CALSFSQELD 

       130        140        150        160        170        180 
YWGIDEIYLE SCCQARYHQK KEQMNEELKR EAETLREREG EEFDNTCCAE KRKKLWDLLE 

       190        200        210        220        230        240 
KPNSSVAAKI LAIISIMFIV LSTIALSLNT LPELQSLDEF GQSTDNPQLA HVEAVCIAWF 

       250        260        270        280        290        300 
TMEYLLRFLS SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR 

       310        320        330        340        350        360 
IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF FAEKDEDDTK 

       370        380        390        400        410        420 
FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA GVLVIALPIP IIVNNFSEFY 

       430        440        450        460        470        480 
KEQKRQEKAI KRREALERAK RNGSIVSMNM KDAFARSIEM MDIVVEKNGE SIAKKDKVQD 

       490        500        510        520        530        540 
NHLSPNKWKW TKRALSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYSKMAKTQ 

       550        560        570        580        590        600 
SQPILNTKEM APQSKPPEEL EMSSMPSPVA PLPARTEGVI DMRSMSSIDS FISCATDFPE 

       610        620        630        640        650        660 
ATRFSHSPLA SLSSKAGSST APEVGWRGAL GASGGRLTET NPIPETSRSG FFVESPRSSM 

       670        680        690        700        710        720 
KTNNPLKLRA LKVNFVEGDP TPLLPSLGLY HDPLRNRGGA AAAVAGLECA SLLDKPVLSP 

       730        740        750        760        770        780 
ESSIYTTASA RTPPRSPEKH TAIAFNFEAG VHHYIDTDTD DEGQLLYSVD SSPPKSLHGS 

       790        800        810        820        830        840 
TSPKFSTGAR TEKNHFESSP LPTSPKFLRP NCVYSSEGLT GKGPGAQEKC KLENHTPPDV 

       850 
HMLPGGGAHG STRDQSI

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References

[1]	"A novel potassium channel with delayed rectifier properties isolated from rat brain by expression cloning." Frech G.C., Vandongen A.M.J., Schuster G., Brown A.M., Joho R.H. Nature 340:642-645(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-857. Tissue: Brain.
[2]	Frech G.C. Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Distinct spatial and temporal expression patterns of K+ channel mRNAs from different subfamilies." Drewe J.A., Verma S., Frech G.C., Joho R.H. J. Neurosci. 12:538-548(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-575.
[4]	"Phosphorylation of the Kv2.1 K+ channel alters voltage-dependent activation." Murakoshi H., Shi G., Scannevin R.H., Trimmer J.S. Mol. Pharmacol. 52:821-828(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, FUNCTION, MUTAGENESIS OF SER-444 AND SER-496.
[5]	"Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase epsilon." Tiran Z., Peretz A., Attali B., Elson A. J. Biol. Chem. 278:17509-17514(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-128, FUNCTION, MUTAGENESIS OF TYR-128.
[6]	"Bidirectional activity-dependent regulation of neuronal ion channel phosphorylation." Misonou H., Menegola M., Mohapatra D.P., Guy L.K., Park K.-S., Trimmer J.S. J. Neurosci. 26:13505-13514(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-457; SER-567; SER-607 AND SER-719, DEVELOPMENTAL STAGE, FUNCTION.
[7]	"Graded regulation of the Kv2.1 potassium channel by variable phosphorylation." Park K.-S., Mohapatra D.P., Misonou H., Trimmer J.S. Science 313:976-979(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15; SER-457; SER-484; SER-496; SER-503; SER-520; SER-541; SER-567; SER-590; SER-607; SER-655; SER-719; SER-771; SER-799; SER-804 AND THR-836, FUNCTION, MASS SPECTROMETRY, MUTAGENESIS OF SER-15; SER-457; SER-484; SER-541; SER-567; SER-607; SER-655; SER-719; SER-771 AND SER-804.
[8]	"Proteomic analyses of K(v)2.1 channel phosphorylation sites determining cell background specific differences in function." Park K.S., Mohapatra D.P., Trimmer J.S. Channels 1:59-61(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15; SER-457; SER-541; SER-607; SER-655; SER-719; SER-799; SER-804 AND THR-836, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16476 mRNA. Translation: CAA34497.1. Different initiation.

IPI

IPI00208368.

PIR

CHRTD1. S05448.

RefSeq

NP_037318.1. NM_013186.1.

UniGene

Rn.26724.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LNM	X-ray	2.90	B/D	274-305	[»]

ProteinModelPortal

P15387.

ModBase

Search...

PTM databases

PhosphoSite

P15387.

Proteomic databases

PRIDE

P15387.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000074023; ENSRNOP00000065961; ENSRNOG00000046949.

GeneID

25736.

KEGG

rno:25736.

UCSC

RGD:2954. rat.

Organism-specific databases

CTD

3745.

RGD

2954. Kcnb1.

Phylogenomic databases

GeneTree

ENSGT00690000101842.

HOVERGEN

HBG052225.

K04885.

Gene expression databases

Genevestigator

P15387.

Family and domain databases

Gene3D

3.30.710.10. 1 hit.

InterPro

IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003973. K_chnl_volt-dep_Kv2.
IPR004350. K_chnl_volt-dep_Kv2.1.
IPR003131. T1-type_BTB.
[Graphical view]

PANTHER

PTHR11537. PTHR11537. 1 hit.

Pfam

PF00520. Ion_trans. 1 hit.
PF02214. K_tetra. 1 hit.
PF03521. Kv2channel. 1 hit.
[Graphical view]

PRINTS

PR00169. KCHANNEL.
PR01514. KV21CHANNEL.
PR01491. KVCHANNEL.
PR01495. SHABCHANNEL.

SMART

SM00225. BTB. 1 hit.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075226.

EvolutionaryTrace

P15387.

NextBio

607875.

Entry information

Entry name

KCNB1_RAT

Accession

Primary (citable) accession number: P15387

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	October 25, 2002
Last modified:	April 3, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

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