ID A0A2K5LU17_CERAT Unreviewed; 502 AA.
AC A0A2K5LU17;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Potassium voltage-gated channel subfamily V member 1 {ECO:0000256|ARBA:ARBA00020321};
DE AltName: Full=Voltage-gated potassium channel subunit Kv8.1 {ECO:0000256|ARBA:ARBA00032563};
GN Name=KCNV1 {ECO:0000313|Ensembl:ENSCATP00000016438.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000016438.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000016438.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00024762}.
CC -!- SUBUNIT: Heteromultimer with KCNB1 and KCNB2. Interacts with KCNC4 and
CC KCND1. {ECO:0000256|ARBA:ARBA00025980}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the potassium channel family. V (TC 1.A.1.2)
CC subfamily. Kv8.1/KCNV1 sub-subfamily. {ECO:0000256|ARBA:ARBA00009030}.
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 AlphaFoldDB; A0A2K5LU17; -.
DR STRING; 9531.ENSCATP00000016438; -.
DR Ensembl; ENSCATT00000040599.1; ENSCATP00000016438.1; ENSCATG00000032152.1.
DR GeneTree; ENSGT00940000159740; -.
DR OMA; AWFTAEF; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000032152; Expressed in frontal cortex.
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 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.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..159
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
FT REGION 170..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 56546 MW; 0229E21AABF594A7 CRC64;
IEMPSSGRAL LDSPLDSGSL TSLDSSVFCS EGEGEPLALG DCFTVNVGGS RFVLSQQALS
CFPHTRLGKL AVVVASYRRP GALAAVPSPL ELCDDANPVD NEYFFDRSSQ AFRYVLHYYR
TGRLHVMEQL CALSFLQEIQ YWGIDELSID SCCRDRYFRR KELSETLDFK KDTEDQESQH
ESEQDFSQGP CPTVRQKLWN ILEKPGSSTA ARIFGVISII FVVVSIINMA LMSAELSWLD
LQLLEILEYV CISWFTGEFV LRFLCVRDRC RFLRKVPNII DLLAILPFYI TLLVESLSGS
QTTQELENVG RIVQVLRLLR ALRMLKLGRH STGLRSLGMT ITQCYEEVGL LLLFLSVGIS
IFSTVEYFAE QSIPDTTFTS VPCAWWWATT SMTTVGYGDI RPDTTTGKIV AFMCILSGIL
VLALPIAIIN DRFSACYFTL KLKEAAVRQR EALKKLTKNI ATDSYISVNL RDVYARSIME
MLRLKGRERA STRSSGGDDF WF
//
