P22001 (KCNA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	KCNA3
Synonyms:	HGK5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Subunit structure	Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4 By similarity.
Subcellular location	Cell membrane By similarity; 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	N-glycosylation promotes the cell surface expression By similarity.
Sequence similarities	Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.3/KCNA3 sub-subfamily. [View classification]
Caution	It is uncertain whether Met-1 or Met-53 is the initiator.
Sequence caution	The sequence AAA36425.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAA36425.1 differs from that shown. Reason: Frameshift at position 42. The sequence AAA59457.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAA59457.1 differs from that shown. Reason: Frameshift at several positions. 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. The sequence AAC31761.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein homooligomerization Inferred from electronic annotation. Source: InterPro synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	membrane raft Inferred from electronic annotation. Source: Compara voltage-gated potassium channel complex Traceable author statement Ref.6. Source: ProtInc
Molecular_function	delayed rectifier potassium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome outward rectifier potassium channel activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 575	575	Potassium voltage-gated channel subfamily A member 3		PRO_0000053977
Regions
	Topological domain	1 – 234	234	Cytoplasmic Potential
	Transmembrane	235 – 253	19	Helical; Name=Segment S1; Potential
	Topological domain	254 – 294	41	Extracellular Potential
	Transmembrane	295 – 316	22	Helical; Name=Segment S2; Potential
	Topological domain	317 – 327	11	Cytoplasmic Potential
	Transmembrane	328 – 348	21	Helical; Name=Segment S3; Potential
	Topological domain	349 – 362	14	Extracellular Potential
	Transmembrane	363 – 381	19	Helical; Voltage-sensor; Name=Segment S4; Potential
	Topological domain	382 – 397	16	Cytoplasmic Potential
	Transmembrane	398 – 417	20	Helical; Name=Segment S5; Potential
	Topological domain	418 – 458	41	Extracellular Potential
	Transmembrane	459 – 481	23	Helical; Name=Segment S6; Potential
	Topological domain	482 – 575	94	Cytoplasmic Potential
	Motif	444 – 449	6	Selectivity filter By similarity
	Motif	573 – 575	3	PDZ-binding By similarity
Amino acid modifications
	Modified residue	520	1	Phosphoserine; by PKA Potential
	Lipidation	317	1	S-palmitoyl cysteine Potential
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	72	1	A → G in AAA36425. Ref.5
	Sequence conflict	89	1	L → V in AAA36425. Ref.5
	Sequence conflict	113	1	L → V in AAA59457. Ref.6
	Sequence conflict	143	1	L → V in AAA36425. Ref.5
	Sequence conflict	309	1	E → K in AAC31761. Ref.1
	Sequence conflict	390	1	T → S in AAA36425. Ref.5
	Sequence conflict	471	1	T → S in AAA36425. Ref.5
	Sequence conflict	540	1	S → T in AAA36425. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P22001 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 0E98905187A85F48	FASTA	575	63,842
	10 20 30 40 50 60 MDERLSLLRS PPPPSARHRA HPPQRPASSG GAHTLVNHGY AEPAAGRELP PDMTVVPGDH 70 80 90 100 110 120 LLEPEVADGG GAPPQGGCGG GGCDRYEPLP PSLPAAGEQD CCGERVVINI SGLRFETQLK 130 140 150 160 170 180 TLCQFPETLL GDPKRRMRYF DPLRNEYFFD RNRPSFDAIL YYYQSGGRIR RPVNVPIDIF 190 200 210 220 230 240 SEEIRFYQLG EEAMEKFRED EGFLREEERP LPRRDFQRQV WLLFEYPESS GPARGIAIVS 250 260 270 280 290 300 VLVILISIVI FCLETLPEFR DEKDYPASTS QDSFEAAGNS TSGSRAGASS FSDPFFVVET 310 320 330 340 350 360 LCIIWFSFEL LVRFFACPSK ATFSRNIMNL IDIVAIIPYF ITLGTELAER QGNGQQAMSL 370 380 390 400 410 420 AILRVIRLVR VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE 430 440 450 460 470 480 ADDPTSGFSS IPDAFWWAVV TMTTVGYGDM HPVTIGGKIV GSLCAIAGVL TIALPVPVIV 490 500 510 520 530 540 SNFNYFYHRE TEGEEQSQYM HVGSCQHLSS SAEELRKARS NSTLSKSEYM VIEEGGMNHS 550 560 570 AFPQTPFKTG NSTATCTTNN NPNSCVNIKK IFTDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00217447.
PIR	A38101.
RefSeq	NP_002223.3. NM_002232.3.
UniGene	Hs.169948.
3D structure databases
ProteinModelPortal	P22001.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-44822N.
STRING	9606.ENSP00000358784.
Protein family/group databases
TCDB	1.A.1.2.4. voltage-gated ion channel (VIC) superfamily.
PTM databases
PhosphoSite	P22001.
Polymorphism databases
DMDM	215274135.
Proteomic databases
PaxDb	P22001.
PRIDE	P22001.
Protocols and materials databases
DNASU	3738.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369769; ENSP00000358784; ENSG00000177272.
GeneID	3738.
KEGG	hsa:3738.
UCSC	uc001dzv.1. human.
Organism-specific databases
CTD	3738.
GeneCards	GC01M111214.
HGNC	HGNC:6221. KCNA3.
HPA	HPA016625.
MIM	176263. gene.
neXtProt	NX_P22001.
PharmGKB	PA30021.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1226.
HOGENOM	HOG000231015.
HOVERGEN	HBG052230.
InParanoid	P22001.
KO	K04876.
OMA	CDRYEPL.
OrthoDB	EOG4QC155.
Enzyme and pathway databases
Reactome	REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	P22001.
Bgee	P22001.
CleanEx	HS_KCNA3.
Genevestigator	P22001.
GermOnline	ENSG00000177272. Homo sapiens.
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. IPR004050. K_chnl_volt-dep_Kv1.3. 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. PR01510. KV13CHANNEL. PR01491. KVCHANNEL. PR01496. SHAKERCHANEL.
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
ProtoNet	Search...
Other
BindingDB	P22001.
ChEMBL	CHEMBL4633.
GenomeRNAi	3738.
NextBio	14631.
SOURCE	Search...

Entry information

Entry name

KCNA3_HUMAN

Accession

Primary (citable) accession number: P22001
Secondary accession number(s): Q5VWN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.