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 24-JAN-2024, entry version 150. 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}. 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; 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; 10116-ENSRNOP00000005556; -. DR Ensembl; ENSRNOT00000005556.5; ENSRNOP00000005556.1; ENSRNOG00000004117.7. DR Ensembl; ENSRNOT00055042986; ENSRNOP00055035087; ENSRNOG00055024942. DR Ensembl; ENSRNOT00060011096; ENSRNOP00060008288; ENSRNOG00060006771. DR Ensembl; ENSRNOT00065005553; ENSRNOP00065004042; ENSRNOG00065003798. DR GeneID; 60326; -. DR KEGG; rno:60326; -. DR UCSC; RGD:621264; rat. DR AGR; RGD:621264; -. 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; AWFTAEF; -. DR OrthoDB; 1478695at2759; -. 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 cell types or tissues. 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 Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR11537:SF38; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY V MEMBER 1; 1. DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1. DR Pfam; PF02214; BTB_2; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01493; KV8CHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; P97557; RN. 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 //