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P22001

- KCNA3_HUMAN

UniProt

P22001 - KCNA3_HUMAN

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Protein

Potassium voltage-gated channel subfamily A member 3

Gene

KCNA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. delayed rectifier potassium channel activity Source: RefGenome
  2. outward rectifier potassium channel activity Source: Ensembl
  3. voltage-gated ion channel activity Source: ProtInc

GO - Biological processi

  1. potassium ion transport Source: ProtInc
  2. protein homooligomerization Source: InterPro
  3. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Protein family/group databases

TCDBi1.A.1.2.4. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 3
Alternative name(s):
HGK5
HLK3
HPCN3
Voltage-gated K(+) channel HuKIII
Voltage-gated potassium channel subunit Kv1.3
Gene namesi
Name:KCNA3
Synonyms:HGK5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6221. KCNA3.

Subcellular locationi

GO - Cellular componenti

  1. membrane raft Source: Ensembl
  2. plasma membrane Source: Reactome
  3. voltage-gated potassium channel complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Potassium voltage-gated channel subfamily A member 3PRO_0000053977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Lipidationi317 – 3171S-palmitoyl cysteineSequence Analysis
Modified residuei520 – 5201Phosphoserine; by PKASequence Analysis

Post-translational modificationi

N-glycosylation promotes the cell surface expression.By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP22001.
PaxDbiP22001.
PRIDEiP22001.

PTM databases

PhosphoSiteiP22001.

Expressioni

Gene expression databases

BgeeiP22001.
CleanExiHS_KCNA3.
ExpressionAtlasiP22001. baseline and differential.
GenevestigatoriP22001.

Organism-specific databases

HPAiHPA016625.

Interactioni

Subunit structurei

Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4 (By similarity).By similarity

Protein-protein interaction databases

BioGridi109941. 12 interactions.
DIPiDIP-44822N.
MINTiMINT-1528422.
STRINGi9606.ENSP00000358784.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi105 – 1106
Beta strandi113 – 1186
Helixi119 – 1224
Turni129 – 1313
Helixi133 – 1364
Helixi137 – 1393
Turni142 – 1454
Beta strandi146 – 1494
Helixi153 – 16412
Helixi177 – 18610
Helixi191 – 20111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BGCX-ray1.20A104-204[»]
ProteinModelPortaliP22001.
SMRiP22001. Positions 104-491.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 234234CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini254 – 29441ExtracellularSequence AnalysisAdd
BLAST
Topological domaini317 – 32711CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini349 – 36214ExtracellularSequence AnalysisAdd
BLAST
Topological domaini382 – 39716CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini418 – 45841ExtracellularSequence AnalysisAdd
BLAST
Topological domaini482 – 57594CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei235 – 25319Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei295 – 31622Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Transmembranei328 – 34821Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei363 – 38119Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Transmembranei398 – 41720Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Transmembranei459 – 48123Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi444 – 4496Selectivity filterBy similarity
Motifi573 – 5753PDZ-bindingBy similarity

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP22001.
KOiK04876.
OMAiKRRMRYF.
OrthoDBiEOG7M0NRD.
PhylomeDBiP22001.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003972. K_chnl_volt-dep_Kv1.
IPR004050. K_chnl_volt-dep_Kv1.3.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01510. KV13CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

P22001-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDERLSLLRS PPPPSARHRA HPPQRPASSG GAHTLVNHGY AEPAAGRELP
60 70 80 90 100
PDMTVVPGDH LLEPEVADGG GAPPQGGCGG GGCDRYEPLP PSLPAAGEQD
110 120 130 140 150
CCGERVVINI SGLRFETQLK TLCQFPETLL GDPKRRMRYF DPLRNEYFFD
160 170 180 190 200
RNRPSFDAIL YYYQSGGRIR RPVNVPIDIF SEEIRFYQLG EEAMEKFRED
210 220 230 240 250
EGFLREEERP LPRRDFQRQV WLLFEYPESS GPARGIAIVS VLVILISIVI
260 270 280 290 300
FCLETLPEFR DEKDYPASTS QDSFEAAGNS TSGSRAGASS FSDPFFVVET
310 320 330 340 350
LCIIWFSFEL LVRFFACPSK ATFSRNIMNL IDIVAIIPYF ITLGTELAER
360 370 380 390 400
QGNGQQAMSL AILRVIRLVR VFRIFKLSRH SKGLQILGQT LKASMRELGL
410 420 430 440 450
LIFFLFIGVI LFSSAVYFAE ADDPTSGFSS IPDAFWWAVV TMTTVGYGDM
460 470 480 490 500
HPVTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE TEGEEQSQYM
510 520 530 540 550
HVGSCQHLSS SAEELRKARS NSTLSKSEYM VIEEGGMNHS AFPQTPFKTG
560 570
NSTATCTTNN NPNSCVNIKK IFTDV
Length:575
Mass (Da):63,842
Last modified:November 25, 2008 - v3
Checksum:i0E98905187A85F48
GO

Sequence cautioni

The sequence AAA36425.1 differs from that shown. Reason: Frameshift at position 42.
The sequence AAA59457.1 differs from that shown. Reason: Frameshift at several positions.
The sequence AAC31761.1 differs from that shown. Reason: Frameshift at several positions.
The sequence AAA36425.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAA59457.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAB88073.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAC31761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721A → G in AAA36425. (PubMed:1986382)Curated
Sequence conflicti89 – 891L → V in AAA36425. (PubMed:1986382)Curated
Sequence conflicti113 – 1131L → V in AAA59457. (PubMed:1373731)Curated
Sequence conflicti143 – 1431L → V in AAA36425. (PubMed:1986382)Curated
Sequence conflicti309 – 3091E → K in AAC31761. (PubMed:7829094)Curated
Sequence conflicti390 – 3901T → S in AAA36425. (PubMed:1986382)Curated
Sequence conflicti471 – 4711T → S in AAA36425. (PubMed:1986382)Curated
Sequence conflicti540 – 5401S → T in AAA36425. (PubMed:1986382)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23499 mRNA. Translation: AAC31761.1. Sequence problems.
AL365361 Genomic DNA. Translation: CAH71983.1.
CH471122 Genomic DNA. Translation: EAW56457.1.
BC035059 mRNA. Translation: AAH35059.2.
M55515 Genomic DNA. Translation: AAA36425.1. Sequence problems.
M85217 mRNA. Translation: AAA59457.1. Sequence problems.
M38217 Genomic DNA. Translation: AAB88073.1. Different initiation.
CCDSiCCDS828.2.
PIRiA38101.
RefSeqiNP_002223.3. NM_002232.4.
UniGeneiHs.169948.
Hs.619197.
Hs.628223.

Genome annotation databases

EnsembliENST00000369769; ENSP00000358784; ENSG00000177272.
GeneIDi3738.
KEGGihsa:3738.
UCSCiuc001dzv.1. human.

Polymorphism databases

DMDMi215274135.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23499 mRNA. Translation: AAC31761.1 . Sequence problems.
AL365361 Genomic DNA. Translation: CAH71983.1 .
CH471122 Genomic DNA. Translation: EAW56457.1 .
BC035059 mRNA. Translation: AAH35059.2 .
M55515 Genomic DNA. Translation: AAA36425.1 . Sequence problems.
M85217 mRNA. Translation: AAA59457.1 . Sequence problems.
M38217 Genomic DNA. Translation: AAB88073.1 . Different initiation.
CCDSi CCDS828.2.
PIRi A38101.
RefSeqi NP_002223.3. NM_002232.4.
UniGenei Hs.169948.
Hs.619197.
Hs.628223.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BGC X-ray 1.20 A 104-204 [» ]
ProteinModelPortali P22001.
SMRi P22001. Positions 104-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109941. 12 interactions.
DIPi DIP-44822N.
MINTi MINT-1528422.
STRINGi 9606.ENSP00000358784.

Chemistry

BindingDBi P22001.
ChEMBLi CHEMBL2362996.
DrugBanki DB06637. Dalfampridine.
GuidetoPHARMACOLOGYi 540.

Protein family/group databases

TCDBi 1.A.1.2.4. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei P22001.

Polymorphism databases

DMDMi 215274135.

Proteomic databases

MaxQBi P22001.
PaxDbi P22001.
PRIDEi P22001.

Protocols and materials databases

DNASUi 3738.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369769 ; ENSP00000358784 ; ENSG00000177272 .
GeneIDi 3738.
KEGGi hsa:3738.
UCSCi uc001dzv.1. human.

Organism-specific databases

CTDi 3738.
GeneCardsi GC01M111214.
HGNCi HGNC:6221. KCNA3.
HPAi HPA016625.
MIMi 176263. gene.
neXtProti NX_P22001.
PharmGKBi PA30021.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118846.
HOGENOMi HOG000231015.
HOVERGENi HBG052230.
InParanoidi P22001.
KOi K04876.
OMAi KRRMRYF.
OrthoDBi EOG7M0NRD.
PhylomeDBi P22001.
TreeFami TF313103.

Enzyme and pathway databases

Reactomei REACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

GeneWikii KCNA3.
GenomeRNAii 3738.
NextBioi 14631.
PROi P22001.
SOURCEi Search...

Gene expression databases

Bgeei P22001.
CleanExi HS_KCNA3.
ExpressionAtlasi P22001. baseline and differential.
Genevestigatori P22001.

Family and domain databases

Gene3Di 1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProi IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003972. K_chnl_volt-dep_Kv1.
IPR004050. K_chnl_volt-dep_Kv1.3.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view ]
PANTHERi PTHR11537. PTHR11537. 1 hit.
Pfami PF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
PRINTSi PR00169. KCHANNEL.
PR01510. KV13CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTi SM00225. BTB. 1 hit.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Confirmation of the assignment of the gene encoding Kv1.3, a voltage-gated potassium channel (KCNA3) to the proximal short arm of human chromosome 1."
    Folander K., Douglass J., Swanson R.
    Genomics 23:295-296(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel."
    Philipson L.H., Hice R.E., Schaefer K., Lamendola J., Bell G.I., Nelson D.J., Steiner D.F.
    Proc. Natl. Acad. Sci. U.S.A. 88:53-57(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-575.
    Tissue: Skeletal muscle.
  6. "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes."
    Attali B., Romey G., Honore E., Schmid-Alliana A., Mattei M.-G., Lesage F., Ricard P., Barhanin J., Lazdunski M.
    J. Biol. Chem. 267:8650-8657(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-575.
  7. "Characterization and functional expression of genomic DNA encoding the human lymphocyte type n potassium channel."
    Cai Y.-C., Osborne P.B., North R.A., Dooley D.C., Douglass J.
    DNA Cell Biol. 11:163-172(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-575.
    Tissue: Lymphocyte.

Entry informationi

Entry nameiKCNA3_HUMAN
AccessioniPrimary (citable) accession number: P22001
Secondary accession number(s): Q5VWN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-53 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3