KCNV1_MESAU
ID KCNV1_MESAU Reviewed; 504 AA.
AC Q60565;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Potassium voltage-gated channel subfamily V member 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv8.1;
GN Name=KCNV1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8670833; DOI=10.1002/j.1460-2075.1996.tb00697.x;
RA Hugnot J.-P., Salinas M., Lesage F., Guillemare E., de Weille J.,
RA Heurteaux C., Mattei M.-G., Lazdunski M.;
RT "Kv8.1, a new neuronal potassium channel subunit with specific inhibitory
RT properties towards Shab and Shaw channels.";
RL EMBO J. 15:3322-3331(1996).
CC -!- FUNCTION: Potassium channel subunit that does not form functional
CC channels by itself. Modulates KCNB1 and KCNB2 channel activity by
CC shifting the threshold for inactivation to more negative values and by
CC slowing the rate of inactivation. Can down-regulate the channel
CC activity of KCNB1, KCNB2, KCNC4 and KCND1, possibly by trapping them in
CC intracellular membranes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heteromultimer with KCNB1 and KCNB2. Interacts with KCNC4 and
CC KCND1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Has to be associated with another potassium
CC channel subunit to get inserted in the plasma membrane. Remains
CC intracellular in the absence of KCNB2 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain, throughout layers II, IV and VI
CC of the brain cortex. Detected in cerebellum and hippocampus, in the
CC granule cell layer, Purkinje cell layer, pyramidal cell layer and
CC dentate gyrus. Detected at lower levels in olfactory bulb, amygdala,
CC thalamus, hypothalamus, midbrain and brainstem.
CC {ECO:0000269|PubMed:8670833}.
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. Kv8.1/KCNV1 sub-subfamily. {ECO:0000305}.
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DR EMBL; U62810; AAC52727.1; -; mRNA.
DR RefSeq; NP_001268571.1; NM_001281642.1.
DR RefSeq; XP_012970704.1; XM_013115250.1.
DR AlphaFoldDB; Q60565; -.
DR SMR; Q60565; -.
DR STRING; 10036.XP_005072672.1; -.
DR PRIDE; Q60565; -.
DR GeneID; 101835683; -.
DR CTD; 27012; -.
DR eggNOG; KOG3713; Eukaryota.
DR OrthoDB; 818306at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003970; K_chnl_volt-dep_Kv8.1.
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 PANTHER; PTHR11537:SF38; PTHR11537:SF38; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01493; KV8CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..504
FT /note="Potassium voltage-gated channel subfamily V member
FT 1"
FT /id="PRO_0000308352"
FT TOPO_DOM 1..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..335
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 396..401
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 56725 MW; BB667FB17E57A6F0 CRC64;
MDLSPRNRPL LESSSLDSGG SLSSLDSSVF CSEGEGEPLA LGDCLTVNVG GSRFVLSQQA
LSCFPHTRLG KLAVVVASYR RLGALAAAPS PLELCDDANP VDNEYFFDRS SQAFRYVLHY
YRTGRLHVME QLCALSFLQE IQYWGIDELS IDSCCRDRYF RRKELSETLD FKKDTDDQES
QHESEQDFSQ GPCPTVRQKL WDILEKPGSS TAARIFGVIS IIFVAVSIVN MALMSAELSW
LNLQLLEILE YVCISWFTGE FILRFLCVKD RCRFLRKVPN IIDLLAILPF YITLLVESLS
GSHTTQELEN VGRLVQVLRL LRALRMLKLG RHSTGLRSLG MTITQCYEEV GLLLLFLSVG
ISIFSTIEYF AEQSIPDTTF TSVPCAWWWA TTSMTTVGYG DIRPDTTTGK IVAFMCILSG
ILVLALPIAI INDRFSACYF TLKLKEAAVR QREALKKLTK NIATDSYISV NLRDVYARSI
MEMLRLKGRE RASTRSSGGD DFWF