KCNV1_BOVIN
ID KCNV1_BOVIN Reviewed; 503 AA.
AC Q0P583;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 85.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; EE347275; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC120369; AAI20370.1; -; mRNA.
DR RefSeq; NP_001160032.1; NM_001166560.1.
DR AlphaFoldDB; Q0P583; -.
DR SMR; Q0P583; -.
DR STRING; 9913.ENSBTAP00000011219; -.
DR PaxDb; Q0P583; -.
DR PRIDE; Q0P583; -.
DR GeneID; 505732; -.
DR KEGG; bta:505732; -.
DR CTD; 27012; -.
DR eggNOG; KOG3713; Eukaryota.
DR InParanoid; Q0P583; -.
DR OrthoDB; 818306at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; 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..503
FT /note="Potassium voltage-gated channel subfamily V member
FT 1"
FT /id="PRO_0000308349"
FT TOPO_DOM 1..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..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..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 MOTIF 395..400
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
SQ SEQUENCE 503 AA; 56725 MW; 15B769F9FFD7FCA6 CRC64;
MELLPPRGRA PPDSSLDSAS LTSLDSSVFC SEGEGEPLAL GDSFTVNVGG SRFVLSQQAL
SCFPHTRLGK LAVVVASCRR RGALAAVPSP LELCDDANPV DNEYFFDRSS QAFRYVLHYY
RTGRLHVMEQ LCALSFLQEI QYWGIDELSI DSCCRDRYFR RKELSETLDF KKDTEDQESQ
HESEQDFSQG RCPTIRQKLW NILEKPGSCT AARIFGVISI IFVAVSIVNM ALMSAELSWL
DPQLLEILEY VCISWFTGEF VLRFLCVRDR CRFLRKVPNI IDLLAILPFY ITLLVESLSG
SQTTQELENV GRIVQVLRLL RALRMLKLGR HSTGLRSLGM TITQCYEEVG LLLLFLSVGI
SIFSTVEYFA EQSIPDTTFT SVPCAWWWAT TSMTTVGYGD IRPDTTTGKI VAFMCILSGI
LVLALPIAII NDRFSACYFT LKLKEAAVRQ REALKKLTKN IATDSYISVN LRDVYARSIM
EMLRLKGRER ASTRSSGGDD FWF
