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KCNV2_MOUSE
ID   KCNV2_MOUSE             Reviewed;         562 AA.
AC   Q8CFS6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 143.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NMRI; TISSUE=Retina;
RX   PubMed=17652418; DOI=10.1152/jn.00493.2007;
RA   Czirjak G., Toth Z.E., Enyedi P.;
RT   "Characterization of the heteromeric potassium channel formed by Kv2.1 and
RT   the retinal subunit Kv8.2 in Xenopus oocytes.";
RL   J. Neurophysiol. 98:1213-1222(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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).
CC   -!- FUNCTION: Potassium channel subunit. Modulates channel activity by
CC       shifting the threshold and the half-maximal activation to more negative
CC       values (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heteromultimer with KCNB1, KCNC1 and KCNF1. Does not form
CC       homomultimers (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. V (TC 1.A.1.2)
CC       subfamily. Kv8.2/KCNV2 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY238939; AAP70480.1; -; mRNA.
DR   EMBL; BC039042; AAH39042.1; -; mRNA.
DR   CCDS; CCDS29722.1; -.
DR   RefSeq; NP_899002.1; NM_183179.1.
DR   AlphaFoldDB; Q8CFS6; -.
DR   SMR; Q8CFS6; -.
DR   STRING; 10090.ENSMUSP00000055091; -.
DR   GlyGen; Q8CFS6; 1 site.
DR   iPTMnet; Q8CFS6; -.
DR   PhosphoSitePlus; Q8CFS6; -.
DR   PaxDb; Q8CFS6; -.
DR   PRIDE; Q8CFS6; -.
DR   ProteomicsDB; 263506; -.
DR   ABCD; Q8CFS6; 2 sequenced antibodies.
DR   Antibodypedia; 23918; 214 antibodies from 25 providers.
DR   DNASU; 240595; -.
DR   Ensembl; ENSMUST00000056708; ENSMUSP00000055091; ENSMUSG00000047298.
DR   GeneID; 240595; -.
DR   KEGG; mmu:240595; -.
DR   UCSC; uc008hbw.1; mouse.
DR   CTD; 169522; -.
DR   MGI; MGI:2670981; Kcnv2.
DR   VEuPathDB; HostDB:ENSMUSG00000047298; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000157438; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; Q8CFS6; -.
DR   OMA; HMRYYGP; -.
DR   OrthoDB; 818306at2759; -.
DR   PhylomeDB; Q8CFS6; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 240595; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q8CFS6; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q8CFS6; protein.
DR   Bgee; ENSMUSG00000047298; Expressed in retinal neural layer and 19 other tissues.
DR   Genevisible; Q8CFS6; MM.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Potassium; Potassium channel; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..562
FT                   /note="Potassium voltage-gated channel subfamily V member
FT                   2"
FT                   /id="PRO_0000320144"
FT   TOPO_DOM        1..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..269
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..344
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        366..391
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        413..427
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        449..461
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        462..482
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        483..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..562
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           474..479
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   562 AA;  64461 MW;  4D06B01C93BF8C61 CRC64;
     MLKQSNERRW SLSYKPWSTP ETEDVPNTGS NQHRRSICSL GARTGSQASI APQWTEGNYN
     YYIEEDEDCG EEGEDWKDDL AEENQKAECL TSLLDGHNDT PAQMSTLKVN VGGHSYLLEC
     CELANYPKTR LGRLATSTTR RGQLGLCDDY EAQTDEYFFD RDPAVFQLIY NFYTSGVLLV
     RDELCPRSFL EELGYWGVRL KYTPRCCRIC FEERRDELSE QLKIQRELRA QAQAEEAEEL
     FRDMRFYGPQ RQRLWNLMEK PFSSVAAKAM GVATNLFVLI SVVALALNTV EEMQHQAEQG
     TGGGDPRPIL EHVEMLCVAF FTLEFLLRLA STPNLQRFAR SALNLVDLVA ILPFYLQLLL
     ECFTSEDQRH NKDSPREHDL ETVGRVGKVG QVLRIMRLMR IFRILKLARH STGLRAFGFT
     LRQCYQQVGC LMLFITMGIF SFSAAVYSVE HDVPGTNFTS ILHAWWWAAV SISTVGYGDM
     YPETHLGRLF AFLCIAFGII LNGMPISILY NKFSDYYSKL KAYEYTAIRR ERGKVNFMQR
     ATKKMAECLS ESHAQSTTRQ EN
 
 
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