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P22001

- KCNA3_HUMAN

UniProt

P22001 - KCNA3_HUMAN

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
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiP22001.
    BgeeiP22001.
    CleanExiHS_KCNA3.
    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. 11 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.
    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

    MDERLSLLRS PPPPSARHRA HPPQRPASSG GAHTLVNHGY AEPAAGRELP    50
    PDMTVVPGDH LLEPEVADGG GAPPQGGCGG GGCDRYEPLP PSLPAAGEQD 100
    CCGERVVINI SGLRFETQLK TLCQFPETLL GDPKRRMRYF DPLRNEYFFD 150
    RNRPSFDAIL YYYQSGGRIR RPVNVPIDIF SEEIRFYQLG EEAMEKFRED 200
    EGFLREEERP LPRRDFQRQV WLLFEYPESS GPARGIAIVS VLVILISIVI 250
    FCLETLPEFR DEKDYPASTS QDSFEAAGNS TSGSRAGASS FSDPFFVVET 300
    LCIIWFSFEL LVRFFACPSK ATFSRNIMNL IDIVAIIPYF ITLGTELAER 350
    QGNGQQAMSL AILRVIRLVR VFRIFKLSRH SKGLQILGQT LKASMRELGL 400
    LIFFLFIGVI LFSSAVYFAE ADDPTSGFSS IPDAFWWAVV TMTTVGYGDM 450
    HPVTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE TEGEEQSQYM 500
    HVGSCQHLSS SAEELRKARS NSTLSKSEYM VIEEGGMNHS AFPQTPFKTG 550
    NSTATCTTNN NPNSCVNIKK IFTDV 575
    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. 11 interactions.
    DIPi DIP-44822N.
    MINTi MINT-1528422.
    STRINGi 9606.ENSP00000358784.

    Chemistry

    BindingDBi P22001.
    ChEMBLi CHEMBL4633.
    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.
    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

    ArrayExpressi P22001.
    Bgeei P22001.
    CleanExi HS_KCNA3.
    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

    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 1, 2014
    This is version 152 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