KCNV2_HUMAN
ID KCNV2_HUMAN Reviewed; 545 AA.
AC Q8TDN2; Q5T6X0;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Potassium voltage-gated channel subfamily V member 2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv8.2;
GN Name=KCNV2;
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], SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12060745; DOI=10.1073/pnas.122617999;
RA Ottschytsch N., Raes A., Van Hoorick D., Snyders D.J.;
RT "Obligatory heterotetramerization of three previously uncharacterized Kv
RT channel alpha-subunits identified in the human genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7986-7991(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP VARIANTS RCD3B GLN-126; CYS-188; TRP-256; VAL-259; 339-ASP--VAL-341 DEL AND
RP ASP-459, AND VARIANT VAL-533.
RX PubMed=16909397; DOI=10.1086/507568;
RA Wu H., Cowing J.A., Michaelides M., Wilkie S.E., Jeffery G., Jenkins S.A.,
RA Mester V., Bird A.C., Robson A.G., Holder G.E., Moore A.T., Hunt D.M.,
RA Webster A.R.;
RT "Mutations in the gene KCNV2 encoding a voltage-gated potassium channel
RT subunit cause 'cone dystrophy with supernormal rod electroretinogram' in
RT humans.";
RL Am. J. Hum. Genet. 79:574-579(2006).
CC -!- FUNCTION: Potassium channel subunit. Modulates channel activity by
CC shifting the threshold and the half-maximal activation to more negative
CC values.
CC -!- SUBUNIT: Heteromultimer with KCNB1, KCNC1 and KCNF1. Does not form
CC homomultimers. {ECO:0000269|PubMed:12060745}.
CC -!- INTERACTION:
CC Q8TDN2; O15084: ANKRD28; NbExp=3; IntAct=EBI-12014650, EBI-359567;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Note=Has to be associated with KCNB1 or possibly another partner to get
CC inserted in the plasma membrane. Remains intracellular in the absence
CC of KCNB1.
CC -!- TISSUE SPECIFICITY: Detected in lung, liver, kidney, pancreas, spleen,
CC thymus, prostate, testis, ovary and colon.
CC {ECO:0000269|PubMed:12060745}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- DISEASE: Cone dystrophy retinal 3B (RCD3B) [MIM:610356]: A rare form of
CC cone dystrophy associated with supernormal rod responses. The disorder
CC is characterized by reduced visual acuity, photoaversion, night
CC blindness, and abnormal color vision. At an early age, the retina shows
CC subtle depigmentation at the macula and, later, more obvious areas of
CC atrophy. {ECO:0000269|PubMed:16909397}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the potassium channel family. V (TC 1.A.1.2)
CC subfamily. Kv8.2/KCNV2 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF348983; AAL83910.1; -; mRNA.
DR EMBL; AL354723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101352; AAI01353.1; -; mRNA.
DR EMBL; BC101353; AAI01354.1; -; mRNA.
DR CCDS; CCDS6447.1; -.
DR RefSeq; NP_598004.1; NM_133497.3.
DR AlphaFoldDB; Q8TDN2; -.
DR SMR; Q8TDN2; -.
DR BioGRID; 127982; 15.
DR IntAct; Q8TDN2; 4.
DR STRING; 9606.ENSP00000371514; -.
DR ChEMBL; CHEMBL2362996; -.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q8TDN2; -.
DR TCDB; 1.A.1.2.23; the voltage-gated ion channel (vic) superfamily.
DR TCDB; 1.A.1.2.24; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q8TDN2; 1 site.
DR iPTMnet; Q8TDN2; -.
DR PhosphoSitePlus; Q8TDN2; -.
DR BioMuta; KCNV2; -.
DR DMDM; 26006804; -.
DR MassIVE; Q8TDN2; -.
DR PaxDb; Q8TDN2; -.
DR PeptideAtlas; Q8TDN2; -.
DR PRIDE; Q8TDN2; -.
DR ProteomicsDB; 74309; -.
DR Antibodypedia; 23918; 214 antibodies from 25 providers.
DR DNASU; 169522; -.
DR Ensembl; ENST00000382082.4; ENSP00000371514.3; ENSG00000168263.9.
DR GeneID; 169522; -.
DR KEGG; hsa:169522; -.
DR MANE-Select; ENST00000382082.4; ENSP00000371514.3; NM_133497.4; NP_598004.1.
DR UCSC; uc003zho.3; human.
DR CTD; 169522; -.
DR DisGeNET; 169522; -.
DR GeneCards; KCNV2; -.
DR HGNC; HGNC:19698; KCNV2.
DR HPA; ENSG00000168263; Tissue enriched (retina).
DR MalaCards; KCNV2; -.
DR MIM; 607604; gene.
DR MIM; 610356; phenotype.
DR neXtProt; NX_Q8TDN2; -.
DR OpenTargets; ENSG00000168263; -.
DR Orphanet; 209932; Cone dystrophy with supernormal rod response.
DR PharmGKB; PA134992655; -.
DR VEuPathDB; HostDB:ENSG00000168263; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000157438; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; Q8TDN2; -.
DR OMA; HMRYYGP; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q8TDN2; -.
DR TreeFam; TF313103; -.
DR PathwayCommons; Q8TDN2; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; Q8TDN2; -.
DR BioGRID-ORCS; 169522; 12 hits in 1061 CRISPR screens.
DR ChiTaRS; KCNV2; human.
DR GeneWiki; KCNV2; -.
DR GenomeRNAi; 169522; -.
DR Pharos; Q8TDN2; Tclin.
DR PRO; PR:Q8TDN2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8TDN2; protein.
DR Bgee; ENSG00000168263; Expressed in sperm and 52 other tissues.
DR Genevisible; Q8TDN2; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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; 3.30.710.10; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003971; K_chnl_volt-dep_Kv9.
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 PRINTS; PR01494; KV9CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cone-rod dystrophy; Disease variant; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..545
FT /note="Potassium voltage-gated channel subfamily V member
FT 2"
FT /id="PRO_0000054094"
FT TOPO_DOM 1..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 445..465
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..471
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 457..462
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 126
FT /note="L -> Q (in RCD3B; dbSNP:rs776275880)"
FT /evidence="ECO:0000269|PubMed:16909397"
FT /id="VAR_027632"
FT VARIANT 188
FT /note="W -> C (in RCD3B; dbSNP:rs772921412)"
FT /evidence="ECO:0000269|PubMed:16909397"
FT /id="VAR_027633"
FT VARIANT 256
FT /note="S -> W (in RCD3B; dbSNP:rs104894116)"
FT /evidence="ECO:0000269|PubMed:16909397"
FT /id="VAR_027634"
FT VARIANT 259
FT /note="A -> V (in RCD3B)"
FT /evidence="ECO:0000269|PubMed:16909397"
FT /id="VAR_027635"
FT VARIANT 339..341
FT /note="Missing (in RCD3B)"
FT /evidence="ECO:0000269|PubMed:16909397"
FT /id="VAR_027636"
FT VARIANT 459
FT /note="G -> D (in RCD3B; dbSNP:rs104894115)"
FT /evidence="ECO:0000269|PubMed:16909397"
FT /id="VAR_027637"
FT VARIANT 533
FT /note="L -> V (in dbSNP:rs12352254)"
FT /evidence="ECO:0000269|PubMed:16909397"
FT /id="VAR_027638"
SQ SEQUENCE 545 AA; 62459 MW; 72D175B4C0C6B1DA CRC64;
MLKQSERRRS WSYRPWNTTE NEGSQHRRSI CSLGARSGSQ ASIHGWTEGN YNYYIEEDED
GEEEDQWKDD LAEEDQQAGE VTTAKPEGPS DPPALLSTLN VNVGGHSYQL DYCELAGFPK
TRLGRLATST SRSRQLSLCD DYEEQTDEYF FDRDPAVFQL VYNFYLSGVL LVLDGLCPRR
FLEELGYWGV RLKYTPRCCR ICFEERRDEL SERLKIQHEL RAQAQVEEAE ELFRDMRFYG
PQRRRLWNLM EKPFSSVAAK AIGVASSTFV LVSVVALALN TVEEMQQHSG QGEGGPDLRP
ILEHVEMLCM GFFTLEYLLR LASTPDLRRF ARSALNLVDL VAILPLYLQL LLECFTGEGH
QRGQTVGSVG KVGQVLRVMR LMRIFRILKL ARHSTGLRAF GFTLRQCYQQ VGCLLLFIAM
GIFTFSAAVY SVEHDVPSTN FTTIPHSWWW AAVSISTVGY GDMYPETHLG RFFAFLCIAF
GIILNGMPIS ILYNKFSDYY SKLKAYEYTT IRRERGEVNF MQRARKKIAE CLLGSNPQLT
PRQEN
