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P63142

- KCNA2_RAT

UniProt

P63142 - KCNA2_RAT

Protein

Potassium voltage-gated channel subfamily A member 2

Gene

Kcna2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      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.1 Publication

    GO - Molecular functioni

    1. delayed rectifier potassium channel activity Source: RefGenome
    2. outward rectifier potassium channel activity Source: RGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. optic nerve structural organization Source: Ensembl
    2. protein homooligomerization Source: InterPro
    3. protein oligomerization Source: RGD

    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_199159. Voltage gated Potassium channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium voltage-gated channel subfamily A member 2
    Alternative name(s):
    RAK
    RBK2
    RCK5
    Voltage-gated potassium channel subunit Kv1.2
    Gene namesi
    Name:Kcna2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi2950. Kcna2.

    Subcellular locationi

    GO - Cellular componenti

    1. juxtaparanode region of axon Source: BHF-UCL
    2. voltage-gated potassium channel complex Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341R → L: No effect on channel opening. 1 Publication
    Mutagenesisi38 – 381N → A: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi40 – 401S → A: No effect on channel opening. 1 Publication
    Mutagenesisi41 – 411G → A: Loss of channel activity. 1 Publication
    Mutagenesisi42 – 421L → A: No effect on channel opening. 1 Publication
    Mutagenesisi43 – 431R → A: No effect on channel opening. 1 Publication
    Mutagenesisi44 – 441F → A: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi45 – 451E → A: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi46 – 461T → D: Loss of tetramerization and channel activity. 1 Publication
    Mutagenesisi46 – 461T → V or A: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi47 – 471Q → A: No effect on channel opening. 1 Publication
    Mutagenesisi50 – 501T → A: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi70 – 701D → A: No effect on channel opening. 1 Publication
    Mutagenesisi73 – 731R → A: No effect on channel opening. 1 Publication
    Mutagenesisi75 – 751E → A: No effect on channel opening. 1 Publication
    Mutagenesisi77 – 771F → W: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi79 – 791D → N: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi81 – 811N → A: No effect on channel opening. 1 Publication
    Mutagenesisi82 – 821R → A: Loss of channel activity. 1 Publication
    Mutagenesisi86 – 861D → A: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi89 – 891L → A: No effect on channel opening. 1 Publication
    Mutagenesisi90 – 901Y → A: No effect on channel opening. 1 Publication
    Mutagenesisi93 – 931Q → A: Loss of channel activity. 1 Publication
    Mutagenesisi97 – 971R → A: No effect on channel opening. 1 Publication
    Mutagenesisi99 – 991R → A: No effect on channel opening. 1 Publication
    Mutagenesisi102 – 1021V → T: Interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi103 – 1031N → A: No effect on channel opening. 1 Publication
    Mutagenesisi105 – 1051P → A: No effect on channel opening. 1 Publication
    Mutagenesisi107 – 1071D → A: Strongly interferes with voltage-sensitive channel opening. 1 Publication
    Mutagenesisi108 – 1081I → A: No effect on channel opening. 1 Publication
    Mutagenesisi111 – 1111E → A: Interferes with voltage-sensitive channel opening. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 499499Potassium voltage-gated channel subfamily A member 2PRO_0000053975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Lipidationi244 – 2441S-palmitoyl cysteineSequence Analysis
    Modified residuei429 – 4291PhosphotyrosineBy similarity
    Modified residuei449 – 4491Phosphoserine; by PKASequence Analysis

    Post-translational modificationi

    Phosphorylated on tyrosine residues by activated PTK2B/PYK2; this regulates ion channel activity.1 Publication

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP63142.
    PRIDEiP63142.

    PTM databases

    PhosphoSiteiP63142.

    Expressioni

    Gene expression databases

    GenevestigatoriP63142.

    Interactioni

    Subunit structurei

    Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DLG4P783522EBI-631446,EBI-80389From a different organism.

    Protein-protein interaction databases

    BioGridi247501. 5 interactions.
    IntActiP63142. 1 interaction.
    STRINGi10116.ENSRNOP00000042653.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 396
    Beta strandi42 – 476
    Helixi48 – 525
    Turni58 – 603
    Helixi62 – 665
    Turni71 – 744
    Beta strandi75 – 784
    Turni82 – 843
    Helixi85 – 939
    Helixi106 – 11611
    Helixi120 – 13011
    Turni143 – 1453
    Helixi146 – 1494
    Turni150 – 1545
    Beta strandi156 – 1583
    Helixi160 – 18223
    Helixi186 – 1894
    Beta strandi190 – 1923
    Turni193 – 1964
    Helixi202 – 2109
    Helixi221 – 24121
    Turni249 – 2524
    Helixi254 – 2618
    Helixi264 – 2674
    Helixi268 – 2703
    Beta strandi273 – 2775
    Helixi279 – 2824
    Helixi291 – 2999
    Helixi304 – 3096
    Helixi312 – 32312
    Helixi325 – 35127
    Helixi361 – 37212
    Beta strandi378 – 3803
    Helixi385 – 40319
    Helixi406 – 41813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DSXX-ray1.60A/B/C/D/E/F/G/H33-119[»]
    1QDVX-ray1.60A/B/C/D33-131[»]
    1QDWX-ray2.10A/B/C/D/E/F/G/H33-119[»]
    2A79X-ray2.90B1-499[»]
    2R9RX-ray2.40B/H1-499[»]
    3LNMX-ray2.90B/D1-266[»]
    B/D303-499[»]
    3LUTX-ray2.90B1-499[»]
    4JTAX-ray2.50B/Q1-499[»]
    4JTCX-ray2.56B/H1-266[»]
    B/H304-499[»]
    4JTDX-ray2.54B/H1-266[»]
    B/H304-499[»]
    ProteinModelPortaliP63142.
    SMRiP63142. Positions 3-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63142.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei164 – 18219Helical; Name=Segment S1Add
    BLAST
    Transmembranei222 – 24322Helical; Name=Segment S2Add
    BLAST
    Transmembranei255 – 27521Helical; Name=Segment S3Add
    BLAST
    Transmembranei293 – 31119Helical; Voltage-sensor; Name=Segment S4Add
    BLAST
    Transmembranei328 – 34720Helical; Name=Segment S5Add
    BLAST
    Transmembranei389 – 41123Helical; Name=Segment S6Add
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi374 – 3796Selectivity filter
    Motifi497 – 4993PDZ-binding

    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.
    GeneTreeiENSGT00740000115256.
    HOGENOMiHOG000231015.
    HOVERGENiHBG052230.
    InParanoidiP63142.
    KOiK04875.
    OMAiMTFHTYS.
    OrthoDBiEOG7M0NRD.
    PhylomeDBiP63142.
    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.
    IPR004049. K_chnl_volt-dep_Kv1.2.
    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.
    PR01509. KV12CHANNEL.
    PR01491. KVCHANNEL.
    PR01496. SHAKERCHANEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P63142-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT    50
    LAQFPETLLG DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR 100
    PVNVPLDIFS EEIRFYELGE EAMEMFREDE GYIKEEERPL PENEFQRQVW 150
    LLFEYPESSG PARIIAIVSV MVILISIVSF CLETLPIFRD ENEDMHGGGV 200
    TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR FFACPSKAGF 250
    FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR 300
    VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE 350
    ADERDSQFPS IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL 400
    TIALPVPVIV SNFNYFYHRE TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA 450
    STISKSDYME IQEGVNNSNE DFREENLKTA NCTLANTNYV NITKMLTDV 499
    Length:499
    Mass (Da):56,701
    Last modified:September 13, 2004 - v1
    Checksum:iA8FEA6F3F59AF42A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti411 – 4111S → F in AAA19867. (PubMed:1715584)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04731 mRNA. Translation: AAA40819.1.
    X16003 mRNA. Translation: CAA34134.1.
    M74449 mRNA. Translation: AAA19867.1.
    PIRiA33814.
    RefSeqiNP_037102.1. NM_012970.3.
    XP_006233194.1. XM_006233132.1.
    XP_006233195.1. XM_006233133.1.
    XP_006233196.1. XM_006233134.1.
    XP_006233197.1. XM_006233135.1.
    UniGeneiRn.10298.
    Rn.40779.

    Genome annotation databases

    EnsembliENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
    GeneIDi25468.
    KEGGirno:25468.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04731 mRNA. Translation: AAA40819.1 .
    X16003 mRNA. Translation: CAA34134.1 .
    M74449 mRNA. Translation: AAA19867.1 .
    PIRi A33814.
    RefSeqi NP_037102.1. NM_012970.3.
    XP_006233194.1. XM_006233132.1.
    XP_006233195.1. XM_006233133.1.
    XP_006233196.1. XM_006233134.1.
    XP_006233197.1. XM_006233135.1.
    UniGenei Rn.10298.
    Rn.40779.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 1-266 [» ]
    B/D 303-499 [» ]
    3LUT X-ray 2.90 B 1-499 [» ]
    4JTA X-ray 2.50 B/Q 1-499 [» ]
    4JTC X-ray 2.56 B/H 1-266 [» ]
    B/H 304-499 [» ]
    4JTD X-ray 2.54 B/H 1-266 [» ]
    B/H 304-499 [» ]
    ProteinModelPortali P63142.
    SMRi P63142. Positions 3-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247501. 5 interactions.
    IntActi P63142. 1 interaction.
    STRINGi 10116.ENSRNOP00000042653.

    Chemistry

    GuidetoPHARMACOLOGYi 539.

    PTM databases

    PhosphoSitei P63142.

    Proteomic databases

    PaxDbi P63142.
    PRIDEi P63142.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000050149 ; ENSRNOP00000042653 ; ENSRNOG00000018285 .
    GeneIDi 25468.
    KEGGi rno:25468.

    Organism-specific databases

    CTDi 3737.
    RGDi 2950. Kcna2.

    Phylogenomic databases

    eggNOGi COG1226.
    GeneTreei ENSGT00740000115256.
    HOGENOMi HOG000231015.
    HOVERGENi HBG052230.
    InParanoidi P63142.
    KOi K04875.
    OMAi MTFHTYS.
    OrthoDBi EOG7M0NRD.
    PhylomeDBi P63142.
    TreeFami TF313103.

    Enzyme and pathway databases

    Reactomei REACT_199159. Voltage gated Potassium channels.

    Miscellaneous databases

    EvolutionaryTracei P63142.
    NextBioi 289787.
    PROi P63142.

    Gene expression databases

    Genevestigatori P63142.

    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.
    IPR004049. K_chnl_volt-dep_Kv1.2.
    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.
    PR01509. KV12CHANNEL.
    PR01491. KVCHANNEL.
    PR01496. SHAKERCHANEL.
    SMARTi SM00225. BTB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiKCNA2_RAT
    AccessioniPrimary (citable) accession number: P63142
    Secondary accession number(s): P15386, Q02010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3