P63142 (KCNA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
RAK
RBK2
RCK5
Voltage-gated potassium channel subunit Kv1.2

Gene names

Name:

Kcna2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Ref.6
Subunit structure	Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4. Ref.7 Ref.8
Subcellular location	Membrane; Multi-pass membrane protein.
Domain	The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. 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 tyrosine residues by activated PTK2B/PYK2; this regulates ion channel activity. Ref.6
Sequence similarities	Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily. [View classification]

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 Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	optic nerve structural organization Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: InterPro protein oligomerization Inferred from mutant phenotype PubMed 12127166. Source: RGD
Cellular_component	juxtaparanode region of axon Inferred from direct assay PubMed 10624965. Source: BHF-UCL voltage-gated potassium channel complex Inferred from electronic annotation. Source: Compara
Molecular_function	delayed rectifier potassium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome outward rectifier potassium channel activity Inferred from mutant phenotype PubMed 12127166. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DLG4	P78352	2	EBI-631446,EBI-80389	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 499

499

Potassium voltage-gated channel subfamily A member 2

PRO_0000053975

Regions

Transmembrane

164 – 182

19

Helical; Name=Segment S1

Transmembrane

222 – 243

22

Helical; Name=Segment S2

Transmembrane

255 – 275

21

Helical; Name=Segment S3

Transmembrane

293 – 311

19

Helical; Name=Segment S4

Transmembrane

328 – 347

20

Helical; Name=Segment S5

Transmembrane

389 – 411

23

Helical; Name=Segment S6

Motif

374 – 379

6

Selectivity filter

Motif

497 – 499

3

PDZ-binding

Amino acid modifications

Modified residue

421

1

Phosphothreonine By similarity

Modified residue

429

1

Phosphotyrosine By similarity

Modified residue

433

1

Phosphothreonine By similarity

Modified residue

449

1

Phosphoserine; by PKA Potential

Lipidation

244

1

S-palmitoyl cysteine Potential

Glycosylation

38

1

N-linked (GlcNAc...) Potential

Glycosylation

207

1

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

34

1

R → L: No effect on channel opening. Ref.7

Mutagenesis

38

1

N → A: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

40

1

S → A: No effect on channel opening. Ref.7

Mutagenesis

41

1

G → A: Loss of channel activity. Ref.7

Mutagenesis

42

1

L → A: No effect on channel opening. Ref.7

Mutagenesis

43

1

R → A: No effect on channel opening. Ref.7

Mutagenesis

44

1

F → A: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

45

1

E → A: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

46

1

T → D: Loss of tetramerization and channel activity. Ref.7

Mutagenesis

46

1

T → V or A: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

47

1

Q → A: No effect on channel opening. Ref.7

Mutagenesis

50

1

T → A: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

70

1

D → A: No effect on channel opening. Ref.7

Mutagenesis

73

1

R → A: No effect on channel opening. Ref.7

Mutagenesis

75

1

E → A: No effect on channel opening. Ref.7

Mutagenesis

77

1

F → W: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

79

1

D → N: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

81

1

N → A: No effect on channel opening. Ref.7

Mutagenesis

82

1

R → A: Loss of channel activity. Ref.7

Mutagenesis

86

1

D → A: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

89

1

L → A: No effect on channel opening. Ref.7

Mutagenesis

90

1

Y → A: No effect on channel opening. Ref.7

Mutagenesis

93

1

Q → A: Loss of channel activity. Ref.7

Mutagenesis

97

1

R → A: No effect on channel opening. Ref.7

Mutagenesis

99

1

R → A: No effect on channel opening. Ref.7

Mutagenesis

102

1

V → T: Interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

103

1

N → A: No effect on channel opening. Ref.7

Mutagenesis

105

1

P → A: No effect on channel opening. Ref.7

Mutagenesis

107

1

D → A: Strongly interferes with voltage-sensitive channel opening. Ref.7

Mutagenesis

108

1

I → A: No effect on channel opening. Ref.7

Mutagenesis

111

1

E → A: Interferes with voltage-sensitive channel opening. Ref.7

Sequence conflict

411

1

S → F in AAA19867. Ref.4

Secondary structure

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499

Helix Strand Turn

Details...

Beta strand

34 – 39

6

Beta strand

42 – 47

6

Helix

48 – 52

5

Turn

58 – 60

3

Helix

62 – 66

5

Turn

71 – 74

4

Beta strand

75 – 78

4

Turn

82 – 84

3

Helix

85 – 93

9

Helix

106 – 116

11

Helix

120 – 130

11

Helix

141 – 144

4

Helix

146 – 149

4

Turn

150 – 154

5

Helix

160 – 182

23

Helix

186 – 189

4

Turn

193 – 196

4

Helix

202 – 210

9

Helix

220 – 242

23

Helix

247 – 249

3

Helix

254 – 261

8

Helix

264 – 273

10

Helix

279 – 282

4

Helix

291 – 299

9

Helix

302 – 309

8

Helix

312 – 323

12

Helix

325 – 345

21

Helix

347 – 350

4

Beta strand

351 – 353

3

Helix

362 – 372

11

Beta strand

378 – 380

3

Helix

385 – 402

18

Helix

405 – 420

16

Sequences

	Sequence		Length	Mass (Da)
	P63142 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: A8FEA6F3F59AF42A	FASTA	499	56,701
	10 20 30 40 50 60 MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG 70 80 90 100 110 120 DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE 130 140 150 160 170 180 EAMEMFREDE GYIKEEERPL PENEFQRQVW LLFEYPESSG PARIIAIVSV MVILISIVSF 190 200 210 220 230 240 CLETLPIFRD ENEDMHGGGV TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR 250 260 270 280 290 300 FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR 310 320 330 340 350 360 VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE ADERDSQFPS 370 380 390 400 410 420 IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE 430 440 450 460 470 480 TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA STISKSDYME IQEGVNNSNE DFREENLKTA 490 NCTLANTNYV NITKMLTDV

References

[1]	"Isolation of a cDNA clone coding for a putative second potassium channel indicates the existence of a gene family." McKinnon D. J. Biol. Chem. 264:8230-8236(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain." Stuehmer W., Ruppersberg J.P., Schroerter K.H., Sakmann B., Stocker M., Giese K.P., Perschke A., Baumann A., Pongs O. EMBO J. 8:3235-3244(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	Ludwig J. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Cloning and expression of a rat cardiac delayed rectifier potassium channel." Paulmichl M., Nasmith P., Herllmiss R., Reed K., Boyle W.A., Nerbonne J.M., Peralta E.G., Clapham D.E. Proc. Natl. Acad. Sci. U.S.A. 88:7892-7895(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart atrium.
[5]	"Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases." Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M. Nature 378:85-88(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DLG1; DLG2 AND DLG4.
[6]	"Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions." Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J. Nature 376:737-745(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION. Tissue: Brain.
[7]	"The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel." Minor D.L. Jr., Lin Y.-F., Mobley B.C., Avelar A., Jan Y.N., Jan L.Y., Berger J.M. Cell 102:657-670(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 33-119, TETRAMERIZATION, MUTAGENESIS OF ARG-34; ASN-38; SER-40; GLY-41; LEU-42; ARG-43; PHE-44; GLU-45; THR-46; GLN-47; THR-50; ASP-70; ARG-73; GLU-75; PHE-77; ASP-79; ASN-81; ARG-82; ASP-86; LEU-89; TYR-90; GLN-93; ARG-97; ARG-99; VAL-102; ASN-103; PRO-105; ASP-107; ILE-108 AND GLU-111.
[8]	"Crystal structure of a mammalian voltage-dependent Shaker family K+ channel." Long S.B., Campbell E.B., Mackinnon R. Science 309:897-903(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04731 mRNA. Translation: AAA40819.1.
X16003 mRNA. Translation: CAA34134.1.
M74449 mRNA. Translation: AAA19867.1.

IPI

IPI00208365.

PIR

A33814.

RefSeq

NP_037102.1. NM_012970.3.

UniGene

Rn.10298.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DSX	X-ray	1.60	A/B/C/D/E/F/G/H	33-119	[»]
1QDV	X-ray	1.60	A/B/C/D	33-131	[»]
1QDW	X-ray	2.10	A/B/C/D/E/F/G/H	33-119	[»]
2A79	X-ray	2.90	B	1-499	[»]
2R9R	X-ray	2.40	B/H	1-499	[»]
3LNM	X-ray	2.90	B/D	1-499	[»]
3LUT	X-ray	2.90	B	1-499	[»]

ProteinModelPortal

P63142.

SMR

P63142. Positions 3-421.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63142. 1 interaction.

STRING

10116.ENSRNOP00000042653.

PTM databases

PhosphoSite

P63142.

Proteomic databases

PaxDb

P63142.

PRIDE

P63142.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.

GeneID

25468.

KEGG

rno:25468.

Organism-specific databases

CTD

3737.

RGD

2950. Kcna2.

Phylogenomic databases

eggNOG

COG1226.

GeneTree

ENSGT00560000076957.

HOGENOM

HOG000231015.

HOVERGEN

HBG052230.

InParanoid

P63142.

KO

K04875.

OMA

AQYLQVN.

OrthoDB

EOG4DR9CB.

Gene expression databases

Genevestigator

P63142.

GermOnline

ENSRNOG00000018285. Rattus norvegicus.

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.
IPR003972. K_chnl_volt-dep_Kv1.
IPR004049. K_chnl_volt-dep_Kv1.2.
IPR003131. T1-type_BTB.
[Graphical view]

PANTHER

PTHR11537. PTHR11537. 1 hit.

Pfam

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

PRINTS

PR00169. KCHANNEL.
PR01509. KV12CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.

SMART

SM00225. BTB. 1 hit.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P63142.

NextBio

289787.

Entry information

Entry name

KCNA2_RAT

Accession

Primary (citable) accession number: P63142
Secondary accession number(s): P15386, Q02010

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program