KCNA4_HUMAN
ID KCNA4_HUMAN Reviewed; 653 AA.
AC P22459;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 4;
DE AltName: Full=HPCN2;
DE AltName: Full=Voltage-gated K(+) channel HuKII {ECO:0000303|PubMed:19912772};
DE AltName: Full=Voltage-gated potassium channel HBK4;
DE AltName: Full=Voltage-gated potassium channel HK1 {ECO:0000303|PubMed:2001794};
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.4;
GN Name=KCNA4; Synonyms=KCNA4L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=2263489; DOI=10.1093/nar/18.23.7160;
RA Philipson L.H., Schaefer K., Lamendola J., Bell G.I., Steiner D.F.;
RT "Sequence of a human fetal skeletal muscle potassium channel cDNA related
RT to RCK4.";
RL Nucleic Acids Res. 18:7160-7160(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=2001794; DOI=10.1096/fasebj.5.3.2001794;
RA Tamkun M.M., Knoth K.M., Walbridge J.A., Kroemer H., Roden D.M.,
RA Glover D.M.;
RT "Molecular cloning and characterization of two voltage-gated K+ channel
RT cDNAs from human ventricle.";
RL FASEB J. 5:331-337(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RC TISSUE=Brain;
RX PubMed=19912772; DOI=10.1016/1044-7431(90)90004-n;
RA Ramaswami M., Gautam M., Kamb A., Rudy B., Tanouye M.A., Mathew M.K.;
RT "Human potassium channel genes: molecular cloning and functional
RT expression.";
RL Mol. Cell. Neurosci. 1:214-223(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8495559; DOI=10.1161/01.res.72.6.1326;
RA Po S., Roberds S., Snyders D.J., Tamkun M.M., Bennett P.B.;
RT "Heteromultimeric assembly of human potassium channels. Molecular basis of
RT a transient outward current?";
RL Circ. Res. 72:1326-1336(1993).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17156368; DOI=10.1111/j.1460-9568.2006.05186.x;
RA Imbrici P., D'Adamo M.C., Kullmann D.M., Pessia M.;
RT "Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast
RT inactivation properties of the human potassium channels Kv1.4-1.1/Kvbeta1.1
RT and Kv1.4-1.1/Kvbeta1.2.";
RL Eur. J. Neurosci. 24:3073-3083(2006).
RN [7]
RP INTERACTION WITH KCNRG, AND SUBCELLULAR LOCATION.
RX PubMed=19968958; DOI=10.1016/j.bbrc.2009.11.143;
RA Usman H., Mathew M.K.;
RT "Potassium channel regulator KCNRG regulates surface expression of Shaker-
RT type potassium channels.";
RL Biochem. Biophys. Res. Commun. 391:1301-1305(2010).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN MCIDDS, VARIANT MCIDDS GLN-89,
RP AND CHARACTERIZATION OF VARIANT MCIDDS GLN-89.
RX PubMed=27582084; DOI=10.1136/jmedgenet-2015-103637;
RA Kaya N., Alsagob M., D'Adamo M.C., Al-Bakheet A., Hasan S., Muccioli M.,
RA Almutairi F.B., Almass R., Aldosary M., Monies D., Mustafa O.M.,
RA Alyounes B., Kenana R., Al-Zahrani J., Naim E., Binhumaid F.S., Qari A.,
RA Almutairi F., Meyer B., Plageman T.F., Pessia M., Colak D., Al-Owain M.;
RT "KCNA4 deficiency leads to a syndrome of abnormal striatum, congenital
RT cataract and intellectual disability.";
RL J. Med. Genet. 53:786-792(2016).
RN [9]
RP STRUCTURE BY NMR OF 1-37.
RX PubMed=9000078; DOI=10.1038/385272a0;
RA Antz C., Geyer M., Fakler B., Schott M.K., Guy H.R., Frank R.,
RA Ruppersberg J.P., Kalbitzer H.R.;
RT "NMR structure of inactivation gates from mammalian voltage-dependent
RT potassium channels.";
RL Nature 385:272-275(1997).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes. Forms tetrameric potassium-
CC selective channels through which potassium ions pass in accordance with
CC their electrochemical gradient. The channel alternates between opened
CC and closed conformations in response to the voltage difference across
CC the membrane (PubMed:19912772, PubMed:8495559). Can form functional
CC homotetrameric channels and heterotetrameric channels that contain
CC variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other
CC family members as well; channel properties depend on the type of alpha
CC subunits that are part of the channel (PubMed:8495559). Channel
CC properties are modulated by cytoplasmic beta subunits that regulate the
CC subcellular location of the alpha subunits and promote rapid
CC inactivation. In vivo, membranes probably contain a mixture of
CC heteromeric potassium channel complexes, making it difficult to assign
CC currents observed in intact tissues to any particular potassium channel
CC family member. Homotetrameric KCNA4 forms a potassium channel that
CC opens in response to membrane depolarization, followed by rapid
CC spontaneous channel closure (PubMed:19912772, PubMed:8495559).
CC Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows
CC rapid inactivation (PubMed:17156368). {ECO:0000269|PubMed:17156368,
CC ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:27582084,
CC ECO:0000269|PubMed:8495559}.
CC -!- ACTIVITY REGULATION: Inhibited by 4-aminopyridine (4-AP), but not by
CC tetraethylammonium (TEA) and charybdotoxin (CTX).
CC {ECO:0000269|PubMed:19912772}.
CC -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins
CC (By similarity). Interacts with KCNAB1 and KCNAB2 (By similarity).
CC Binds PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts
CC with SIGMAR1 (By similarity). Detected in a complex with KCNA1 (By
CC similarity). Interacts with KCNA2 (By similarity). Part of a complex
CC containing KCNA1, KCNAB1 and LGI1 (By similarity). Interacts (via
CC cytoplasmic N-terminal domain) with KCNRG (PubMed:19968958).
CC {ECO:0000250|UniProtKB:P15385}.
CC -!- INTERACTION:
CC P22459; P78352: DLG4; NbExp=2; IntAct=EBI-631235, EBI-80389;
CC P22459; P21673: SAT1; NbExp=4; IntAct=EBI-631235, EBI-711613;
CC P22459; Q62936: Dlg3; Xeno; NbExp=4; IntAct=EBI-631235, EBI-349596;
CC P22459; P31016: Dlg4; Xeno; NbExp=3; IntAct=EBI-631235, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17156368,
CC ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:19968958,
CC ECO:0000269|PubMed:8495559}; Multi-pass membrane protein {ECO:0000255}.
CC Cell projection, axon {ECO:0000250|UniProtKB:P15385}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, and at lower levels in the
CC testis, lung, kidney, colon and heart (PubMed:27582084). Detected in
CC heart ventricle. {ECO:0000269|PubMed:2001794,
CC ECO:0000269|PubMed:27582084}.
CC -!- DOMAIN: The N-terminus may be important in determining the rate of
CC inactivation of the channel while the tail may play a role in
CC modulation of channel activity and/or targeting of the channel to
CC specific subcellular compartments. {ECO:0000250|UniProtKB:Q28527}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- DISEASE: Microcephaly, cataracts, impaired intellectual development,
CC and dystonia with abnormal striatum (MCIDDS) [MIM:618284]: An autosomal
CC recessive syndrome characterized by cognitive impairment, attention
CC deficit hyperactivity disorder, microcephaly, growth retardation,
CC congenital cataract, and dystonia. Brain MRI shows unusual thinning of
CC the lentiform nucleus, predominantly involving the putamen, and
CC swelling in the caudate heads. {ECO:0000269|PubMed:27582084}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily. {ECO:0000305}.
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DR EMBL; M55514; AAA60034.1; -; mRNA.
DR EMBL; M60450; AAA61275.1; -; mRNA.
DR EMBL; L02751; AAA36140.1; -; mRNA.
DR EMBL; AC124657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41629.1; -.
DR PIR; A39922; A39922.
DR RefSeq; NP_002224.1; NM_002233.3.
DR AlphaFoldDB; P22459; -.
DR BMRB; P22459; -.
DR SMR; P22459; -.
DR BioGRID; 109942; 72.
DR IntAct; P22459; 7.
DR MINT; P22459; -.
DR STRING; 9606.ENSP00000328511; -.
DR BindingDB; P22459; -.
DR ChEMBL; CHEMBL4205; -.
DR DrugBank; DB02299; Arginineamide.
DR DrugBank; DB06637; Dalfampridine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; P22459; -.
DR TCDB; 1.A.1.2.31; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P22459; 1 site.
DR iPTMnet; P22459; -.
DR PhosphoSitePlus; P22459; -.
DR BioMuta; KCNA4; -.
DR DMDM; 313104127; -.
DR jPOST; P22459; -.
DR MassIVE; P22459; -.
DR PaxDb; P22459; -.
DR PeptideAtlas; P22459; -.
DR PRIDE; P22459; -.
DR ProteomicsDB; 53992; -.
DR ABCD; P22459; 1 sequenced antibody.
DR Antibodypedia; 3115; 196 antibodies from 32 providers.
DR DNASU; 3739; -.
DR Ensembl; ENST00000328224.7; ENSP00000328511.6; ENSG00000182255.7.
DR GeneID; 3739; -.
DR KEGG; hsa:3739; -.
DR MANE-Select; ENST00000328224.7; ENSP00000328511.6; NM_002233.4; NP_002224.1.
DR UCSC; uc001msk.4; human.
DR CTD; 3739; -.
DR DisGeNET; 3739; -.
DR GeneCards; KCNA4; -.
DR HGNC; HGNC:6222; KCNA4.
DR HPA; ENSG00000182255; Group enriched (adrenal gland, brain).
DR MalaCards; KCNA4; -.
DR MIM; 176266; gene.
DR MIM; 618284; phenotype.
DR neXtProt; NX_P22459; -.
DR OpenTargets; ENSG00000182255; -.
DR PharmGKB; PA207; -.
DR VEuPathDB; HostDB:ENSG00000182255; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000162248; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; P22459; -.
DR OMA; GDECSYT; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; P22459; -.
DR TreeFam; TF313103; -.
DR PathwayCommons; P22459; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; P22459; -.
DR BioGRID-ORCS; 3739; 13 hits in 1072 CRISPR screens.
DR GeneWiki; KCNA4; -.
DR GenomeRNAi; 3739; -.
DR Pharos; P22459; Tclin.
DR PRO; PR:P22459; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P22459; protein.
DR Bgee; ENSG00000182255; Expressed in adrenal tissue and 104 other tissues.
DR Genevisible; P22459; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043194; C:axon initial segment; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IMP:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 1.20.5.600; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR020467; K_chnl_volt-dep_Kv1.4.
DR InterPro; IPR012897; K_chnl_volt-dep_Kv1.4_TID.
DR InterPro; IPR037065; K_chnl_volt-dep_Kv1.4_TID_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF07941; K_channel_TID; 1.
DR PRINTS; PR01511; KV14CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cataract; Cell membrane; Cell projection; Disease variant; Dystonia;
KW Glycoprotein; Intellectual disability; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..653
FT /note="Potassium voltage-gated channel subfamily A member
FT 4"
FT /id="PRO_0000053981"
FT TOPO_DOM 1..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 305..326
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 327..370
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 371..392
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 393..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 404..424
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 425..439
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 440..460
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 461..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 476..497
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 498..511
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 512..523
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 524..531
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 532..538
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 539..567
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 568..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 24..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..475
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 629..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 524..529
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 651..653
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..94
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61423"
FT MOD_RES 599
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 89
FT /note="R -> Q (in MCIDDS; unknown pathological
FT significance; mildly decreased function in potassium
FT transmembrane transport; dbSNP:rs779101828)"
FT /evidence="ECO:0000269|PubMed:27582084"
FT /id="VAR_081837"
FT CONFLICT 38
FT /note="A -> R (in Ref. 1; AAA60034)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="A -> R (in Ref. 1; AAA60034)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..88
FT /note="RRRRQ -> EEEAT (in Ref. 1; AAA60034)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="S -> D (in Ref. 1; AAA60034)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="S -> V (in Ref. 1; AAA60034)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="G -> A (in Ref. 1; AAA60034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 73257 MW; 5E511DB704CCA013 CRC64;
MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGSGGSGGG
SHHHHQSRGA CTSHDPQSSR GSRRRRRQRS EKKKAHYRQS SFPHCSDLMP SGSEEKILRE
LSEEEEDEEE EEEEEEEGRF YYSEDDHGDE CSYTDLLPQD EGGGGYSSVR YSDCCERVVI
NVSGLRFETQ MKTLAQFPET LLGDPEKRTQ YFDPLRNEYF FDRNRPSFDA ILYYYQSGGR
LKRPVNVPFD IFTEEVKFYQ LGEEALLKFR EDEGFVREEE DRALPENEFK KQIWLLFEYP
ESSSPARGIA IVSVLVILIS IVIFCLETLP EFRDDRDLVM ALSAGGHGGL LNDTSAPHLE
NSGHTIFNDP FFIVETVCIV WFSFEFVVRC FACPSQALFF KNIMNIIDIV SILPYFITLG
TDLAQQQGGG NGQQQQAMSF AILRIIRLVR VFRIFKLSRH SKGLQILGHT LRASMRELGL
LIFFLFIGVI LFSSAVYFAE ADEPTTHFQS IPDAFWWAVV TMTTVGYGDM KPITVGGKIV
GSLCAIAGVL TIALPVPVIV SNFNYFYHRE TENEEQTQLT QNAVSCPYLP SNLLKKFRSS
TSSSLGDKSE YLEMEEGVKE SLCAKEEKCQ GKGDDSETDK NNCSNAKAVE TDV
