KCNV1_RAT
ID KCNV1_RAT Reviewed; 503 AA.
AC P97557;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Potassium voltage-gated channel subfamily V member 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv2.3r;
DE AltName: Full=Voltage-gated potassium channel subunit Kv8.1;
GN Name=Kcnv1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KCNB1, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain, and Hippocampus;
RX PubMed=9169526; DOI=10.1523/jneurosci.17-12-04652.1997;
RA Castellano A., Chiara M.D., Mellstroem B., Molina A., Monje F.,
RA Naranjo J.R., Lopez-Barneo J.;
RT "Identification and functional characterization of a K+ channel alpha-
RT subunit with regulatory properties specific to brain.";
RL J. Neurosci. 17:4652-4661(1997).
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 ECO:0000269|PubMed:9169526}.
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, in neocortex, olfactory
CC tubercle, hippocampus, dentate gyrus, piriform cortex and amygdala.
CC Detected in Purkinje cells and granular cells of the cerebellum, in
CC hippocampal CA4 neurons and neocortex pyramidal cells.
CC {ECO:0000269|PubMed:9169526}.
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; X98564; CAA67174.1; -; mRNA.
DR RefSeq; NP_067729.1; NM_021697.1.
DR AlphaFoldDB; P97557; -.
DR SMR; P97557; -.
DR STRING; 10116.ENSRNOP00000005556; -.
DR ChEMBL; CHEMBL4524039; -.
DR TCDB; 1.A.1.2.9; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; P97557; -.
DR PhosphoSitePlus; P97557; -.
DR PaxDb; P97557; -.
DR Ensembl; ENSRNOT00000005556; ENSRNOP00000005556; ENSRNOG00000004117.
DR GeneID; 60326; -.
DR KEGG; rno:60326; -.
DR UCSC; RGD:621264; rat.
DR CTD; 27012; -.
DR RGD; 621264; Kcnv1.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000159740; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; P97557; -.
DR OMA; LRINPCC; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; P97557; -.
DR TreeFam; TF313103; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:P97557; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004117; Expressed in frontal cortex and 3 other tissues.
DR Genevisible; P97557; RN.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:RGD.
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; 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 1: Evidence at protein 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..503
FT /note="Potassium voltage-gated channel subfamily V member
FT 1"
FT /id="PRO_0000308355"
FT TOPO_DOM 3..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..334
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 395..400
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
SQ SEQUENCE 503 AA; 56663 MW; DC559010D00D8E9E CRC64;
MDLSPRNRPL LDSSSLDSGS LTSLDSSVFC SEGEGEPLAL GDCLTVNVGG SRFVLSQQAL
SCFPHTRLGK LAVVVASYRR LGALAAAPSP LELCDDANPV DNEYFFDRSS QAFRYVLHYY
RTGRLHVMEQ LCALSFLQEI QYWGIDELSI DSCCRDRYFR RKELSETLDF KKDTDDQESQ
HESEQDFSQG PCPTVRQKLW DILEKPGSST AARIFGVISI IFVAVSIVNM ALMSAELSWL
NLQLLEILEY VCISWFTGEF ILRFLCVKDR CHFLRKVPNI IDLLAILPFY ITLLVESLSG
SHTTQELENV GRLVQVLRLL RALRMLKLGR HSTGLRSLGM TITQCYEEVG LLLLFLSVGI
SIFSTIEYFA EQSIPDTTFT SVPCAWWWAT TSMTTVGYGD IRPDTTTGKI VAFMCILSGI
LVLALPIAII NDRFSACYFT LKLKEAAVRQ REALKKLTKN IATDSYISVN LRDIYARSIM
EMLRLKGRER ASTRSSGGDD FWF
