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Q63881

- KCND2_RAT

UniProt

Q63881 - KCND2_RAT

Protein

Potassium voltage-gated channel subfamily D member 2

Gene

Kcnd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi105 – 1051ZincBy similarity
    Metal bindingi132 – 1321ZincBy similarity
    Metal bindingi133 – 1331ZincBy similarity

    GO - Molecular functioni

    1. A-type (transient outward) potassium channel activity Source: RGD
    2. ion channel activity Source: RGD
    3. metal ion binding Source: UniProtKB-KW
    4. potassium channel activity Source: RGD
    5. protein binding Source: RGD
    6. protein heterodimerization activity Source: RGD
    7. voltage-gated potassium channel activity Source: RGD

    GO - Biological processi

    1. action potential Source: RGD
    2. potassium ion transport Source: RGD
    3. protein heterooligomerization Source: RGD
    4. protein homooligomerization Source: InterPro

    Keywords - Molecular functioni

    Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Potassium transport, Transport

    Keywords - Ligandi

    Metal-binding, Potassium, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium voltage-gated channel subfamily D member 2
    Alternative name(s):
    RK5
    Shal1
    Voltage-gated potassium channel subunit Kv4.2
    Gene namesi
    Name:Kcnd2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi68393. Kcnd2.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell projectiondendrite 1 Publication
    Note: Interaction with DPP6, DLG4 or NCS1/FREQ may increase cell surface expression. Localized preferentially to the dendrites of pyramidal cells.

    GO - Cellular componenti

    1. dendrite Source: RGD
    2. dendritic spine Source: RGD
    3. integral component of plasma membrane Source: RGD
    4. neuronal cell body Source: RGD
    5. neuron projection Source: RGD
    6. perinuclear endoplasmic reticulum Source: RGD
    7. plasma membrane Source: RGD
    8. postsynaptic density Source: RGD
    9. potassium channel complex Source: RGD
    10. voltage-gated potassium channel complex Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 115Missing: Greatly reduces interaction with KCNIP1.
    Mutagenesisi8 – 81W → A: Abolishes interaction with KCNP1; when associated with A-11. 1 Publication
    Mutagenesisi11 – 111F → A: Abolishes interaction with KCNP1; when associated with A-8. 1 Publication
    Mutagenesisi66 – 661L → R: Abolishes expression. 1 Publication
    Mutagenesisi71 – 711E → K: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi73 – 731D → M: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi74 – 741F → R: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi79 – 791E → L or R: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi93 – 931R → A: Greatly reduces expression and changes multimerization. 1 Publication
    Mutagenesisi481 – 4822Missing: Loss of dendritic targeted expression.
    Mutagenesisi627 – 6304Missing: Abolishes interaction with DLG4.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630Potassium voltage-gated channel subfamily D member 2PRO_0000054067Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381PhosphothreonineBy similarity
    Modified residuei552 – 5521Phosphoserine1 Publication
    Modified residuei602 – 6021PhosphothreonineBy similarity
    Modified residuei607 – 6071PhosphothreonineBy similarity
    Modified residuei616 – 6161PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on serine and threonine residues.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ63881.
    PRIDEiQ63881.

    PTM databases

    PhosphoSiteiQ63881.

    Expressioni

    Tissue specificityi

    Highly expressed in heart and throughout the brain, with similar levels in cortex and hypothalamus, and much higher levels in hippocampus, dentate gyrus and the habenular nucleus of the thalamus. Detected at similar levels in heart atrium and ventricle. Detected in aorta, cardiac and smooth muscle.2 Publications

    Gene expression databases

    GenevestigatoriQ63881.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer with KCND1 and/or KCND3. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. The KCND2-KCNIP2 channel complex contains four KCND2 and four KCNIP2 subunits. Interacts with FLNA and FLNC By similarity. Interacts with DPP6, DPP10, DLG4, NCS1/FREQ and DLG1.By similarity10 Publications

    Protein-protein interaction databases

    BioGridi249292. 2 interactions.
    IntActiQ63881. 3 interactions.
    MINTiMINT-104113.
    STRINGi10116.ENSRNOP00000039227.

    Structurei

    Secondary structure

    630
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 66
    Helixi9 – 179
    Beta strandi43 – 475
    Beta strandi50 – 545
    Helixi56 – 605
    Beta strandi64 – 663
    Helixi70 – 756
    Helixi78 – 803
    Beta strandi81 – 855
    Turni89 – 913
    Helixi92 – 10110
    Helixi112 – 12211
    Helixi131 – 14515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NN7X-ray2.10A42-146[»]
    1S6CX-ray2.00B1-30[»]
    ProteinModelPortaliQ63881.
    SMRiQ63881. Positions 3-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ63881.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 183183CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini246 – 25914CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini311 – 32313CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini406 – 630225CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei363 – 38321Pore-forming; Name=Segment H5Sequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei184 – 20421Helical; Name=Segment S1Sequence AnalysisAdd
    BLAST
    Transmembranei225 – 24521Helical; Name=Segment S2Sequence AnalysisAdd
    BLAST
    Transmembranei260 – 28021Helical; Name=Segment S3Sequence AnalysisAdd
    BLAST
    Transmembranei290 – 31021Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
    BLAST
    Transmembranei324 – 34421Helical; Name=Segment S5Sequence AnalysisAdd
    BLAST
    Transmembranei385 – 40521Helical; Name=Segment S6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2019Interaction with KCNIP2By similarityAdd
    BLAST
    Regioni7 – 115Interaction with KCNIP1
    Regioni71 – 9020Interaction with KCNIP1Add
    BLAST
    Regioni474 – 48916Mediates dendritic targetingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi370 – 3756Selectivity filterBy similarity

    Domaini

    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.
    HOGENOMiHOG000231013.
    HOVERGENiHBG106687.
    InParanoidiQ63881.
    KOiK04892.
    PhylomeDBiQ63881.

    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.
    IPR003975. K_chnl_volt-dep_Kv4.
    IPR004055. K_chnl_volt-dep_Kv4.2.
    IPR024587. K_chnl_volt-dep_Kv4_C.
    IPR021645. Shal-type.
    IPR003131. T1-type_BTB.
    IPR028325. VG_K_chnl.
    [Graphical view]
    PANTHERiPTHR11537. PTHR11537. 1 hit.
    PfamiPF02214. BTB_2. 1 hit.
    PF11879. DUF3399. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF11601. Shal-type. 1 hit.
    [Graphical view]
    PRINTSiPR00169. KCHANNEL.
    PR01517. KV42CHANNEL.
    PR01491. KVCHANNEL.
    PR01497. SHALCHANNEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q63881-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT    50
    RFQTWQDTLE RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR 100
    TGKLHYPRHE CISAYDEELA FFGLIPEIIG DCCYEEYKDR RRENAERLQD 150
    DADTDNTGES ALPTMTARQR VWRAFENPHT STMALVFYYV TGFFIAVSVI 200
    ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF TVEYLLRLAA 250
    APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI 300
    FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS 350
    ASKFTSIPAA FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL 400
    PVPVIVSNFS RIYHQNQRAD KRRAQKKARL ARIRAAKSGS ANAYMQSKRN 450
    GLLSNQLQSS EDEPAFVSKS GSSFETQHHH LLHCLEKTTN HEFVDEQVFE 500
    ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKSFRI PNANVSGSHR 550
    GSVQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI 600
    PTPPVTTPEG DDRPESPEYS GGNIVRVSAL 630
    Length:630
    Mass (Da):70,549
    Last modified:November 1, 1996 - v1
    Checksum:iFDE57E8A5113BABF
    GO

    Sequence cautioni

    The sequence AAA40929.1 differs from that shown. Reason: Frameshift at position 477.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S64320 mRNA. Translation: AAB19939.1.
    M59980 mRNA. Translation: AAA40929.1. Frameshift.
    PIRiI57681.
    JU0271.
    RefSeqiNP_113918.2. NM_031730.2.
    UniGeneiRn.87841.

    Genome annotation databases

    GeneIDi65180.
    KEGGirno:65180.
    UCSCiRGD:68393. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S64320 mRNA. Translation: AAB19939.1 .
    M59980 mRNA. Translation: AAA40929.1 . Frameshift.
    PIRi I57681.
    JU0271.
    RefSeqi NP_113918.2. NM_031730.2.
    UniGenei Rn.87841.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NN7 X-ray 2.10 A 42-146 [» ]
    1S6C X-ray 2.00 B 1-30 [» ]
    ProteinModelPortali Q63881.
    SMRi Q63881. Positions 3-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249292. 2 interactions.
    IntActi Q63881. 3 interactions.
    MINTi MINT-104113.
    STRINGi 10116.ENSRNOP00000039227.

    Chemistry

    ChEMBLi CHEMBL1075227.
    GuidetoPHARMACOLOGYi 553.

    PTM databases

    PhosphoSitei Q63881.

    Proteomic databases

    PaxDbi Q63881.
    PRIDEi Q63881.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 65180.
    KEGGi rno:65180.
    UCSCi RGD:68393. rat.

    Organism-specific databases

    CTDi 3751.
    RGDi 68393. Kcnd2.

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000231013.
    HOVERGENi HBG106687.
    InParanoidi Q63881.
    KOi K04892.
    PhylomeDBi Q63881.

    Miscellaneous databases

    EvolutionaryTracei Q63881.
    NextBioi 614080.
    PROi Q63881.

    Gene expression databases

    Genevestigatori Q63881.

    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.
    IPR003975. K_chnl_volt-dep_Kv4.
    IPR004055. K_chnl_volt-dep_Kv4.2.
    IPR024587. K_chnl_volt-dep_Kv4_C.
    IPR021645. Shal-type.
    IPR003131. T1-type_BTB.
    IPR028325. VG_K_chnl.
    [Graphical view ]
    PANTHERi PTHR11537. PTHR11537. 1 hit.
    Pfami PF02214. BTB_2. 1 hit.
    PF11879. DUF3399. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF11601. Shal-type. 1 hit.
    [Graphical view ]
    PRINTSi PR00169. KCHANNEL.
    PR01517. KV42CHANNEL.
    PR01491. KVCHANNEL.
    PR01497. SHALCHANNEL.
    SMARTi SM00225. BTB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a mammalian cDNA for an inactivating voltage-sensitive K+ channel."
      Baldwin T.J., Tsaur M.-L., Lopez G.A., Jan Y.N., Jan L.Y.
      Neuron 7:471-483(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Hippocampus.
    2. "Cloning and tissue-specific expression of five voltage-gated potassium channel cDNAs expressed in rat heart."
      Roberds S.L., Tamkun M.M.
      Proc. Natl. Acad. Sci. U.S.A. 88:1798-1802(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Heart.
    3. Cited for: INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3.
    4. "A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-currents."
      Nakamura T.Y., Pountney D.J., Ozaita A., Nandi S., Ueda S., Rudy B., Coetzee W.A.
      Proc. Natl. Acad. Sci. U.S.A. 98:12808-12813(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNIP1 AND NCS1.
    5. "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4."
      Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N., Imaizumi Y., Tomita T., Iwatsubo T.
      J. Biol. Chem. 277:14965-14975(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNIP4.
    6. "Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2."
      Wong W., Newell E.W., Jugloff D.G.M., Jones O.T., Schlichter L.C.
      J. Biol. Chem. 277:20423-20430(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 627-VAL--LEU-630, INTERACTION WITH DLG4.
    7. "A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels."
      Shibata R., Misonou H., Campomanes C.R., Anderson A.E., Schrader L.A., Doliveira L.C., Carroll K.I., Sweatt J.D., Rhodes K.J., Trimmer J.S.
      J. Biol. Chem. 278:36445-36454(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-552.
    8. "An evolutionarily conserved dileucine motif in Shal K+ channels mediates dendritic targeting."
      Rivera J.F., Ahmad S., Quick M.W., Liman E.R., Arnold D.B.
      Nat. Neurosci. 6:243-250(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DENDRITIC TARGETING REGION, MUTAGENESIS OF 481-LEU--LEU-482.
    9. "The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical component of neuronal A-type K+ channels."
      Nadal M.S., Ozaita A., Amarillo Y., Vega-Saenz de Miera E., Ma Y., Mo W., Goldberg E.M., Misumi Y., Ikehara Y., Neubert T.A., Rudy B.
      Neuron 37:449-461(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DPP6.
    10. "KChIPs and Kv4 alpha subunits as integral components of A-type potassium channels in mammalian brain."
      Rhodes K.J., Carroll K.I., Sung M.A., Doliveira L.C., Monaghan M.M., Burke S.L., Strassle B.W., Buchwalder L., Menegola M., Cao J., An W.F., Trimmer J.S.
      J. Neurosci. 24:7903-7915(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNIP1 AND KCNIP3.
    11. Cited for: INTERACTION WITH KCNIP1, MUTAGENESIS OF 7-ALA--PHE-11; GLU-71; ASP-73; PHE-74 AND GLU-79.
    12. Cited for: INTERACTION WITH DPP6 AND DPP10.
    13. "Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes."
      El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., Coulombe A., Jeromin A., Hatem S.N.
      Circ. Res. 104:758-769(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG1.
    14. "Determining the basis of channel-tetramerization specificity by X-ray crystallography and a sequence-comparison algorithm: family values (FamVal)."
      Nanao M.H., Zhou W., Pfaffinger P.J., Choe S.
      Proc. Natl. Acad. Sci. U.S.A. 100:8670-8675(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 42-146, MUTAGENESIS OF LEU-66 AND ARG-93.
    15. "Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels."
      Zhou W., Qian Y., Kunjilwar K., Pfaffinger P.J., Choe S.
      Neuron 41:573-586(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-30, INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3, MUTAGENESIS OF TRP-8 AND PHE-11.

    Entry informationi

    Entry nameiKCND2_RAT
    AccessioniPrimary (citable) accession number: Q63881
    Secondary accession number(s): Q00090, Q99249
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 129 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