KCNV1_MACFA
ID KCNV1_MACFA Reviewed; 500 AA.
AC Q9GKU7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Potassium voltage-gated channel subfamily V member 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv8.1;
GN Name=KCNV1; ORFNames=QccE-20536;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (NOV-2000) 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; AB051133; BAB18159.1; -; mRNA.
DR RefSeq; NP_001274541.1; NM_001287612.1.
DR RefSeq; XP_005564006.1; XM_005563949.2.
DR AlphaFoldDB; Q9GKU7; -.
DR SMR; Q9GKU7; -.
DR STRING; 9541.XP_005564006.1; -.
DR Ensembl; ENSMFAT00000006442; ENSMFAP00000032221; ENSMFAG00000037130.
DR GeneID; 102134648; -.
DR KEGG; mcf:102134648; -.
DR CTD; 27012; -.
DR VEuPathDB; HostDB:ENSMFAG00000037130; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000159740; -.
DR OMA; LRINPCC; -.
DR OrthoDB; 818306at2759; -.
DR Proteomes; UP000233100; Chromosome 8.
DR Bgee; ENSMFAG00000037130; Expressed in temporal lobe and 1 other tissue.
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..500
FT /note="Potassium voltage-gated channel subfamily V member
FT 1"
FT /id="PRO_0000308351"
FT TOPO_DOM 1..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..331
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 168..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 392..397
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
SQ SEQUENCE 500 AA; 56304 MW; C229E21ABC869C73 CRC64;
MPSSGRALLD SPLDSGSLTS LDSSVFCSEG EGEPLALGDC FTVNVGGSRF VLSQQALSCF
PHTRLGKLAV VVASYRRPGA LAAVPSPLEL CDDANPVDNE YFFDRSSQAF RYVLHYYRTG
RLHVMEQLCA LSFLQEIQYW GIDELSIDSC CRDRYFRRKE LSETLDFKKD TEDQESQHES
EQDFSQGPCP TVRQKLWNIL EKPGSSTAAR IFGVISIIFV VVSIINMALM SAELSWLDLQ
LLEILEYVCI SWFTGEFVLR FLCVRDRCRF LRKVPNIIDL LAILPFYITL LVESLSGSQT
TQELENVGRI VQVLRLLRAL RMLKLGRHST GLRSLGMTIT QCYEEVGLLL LFLSVGISIF
STVEYFAEQS IPDTTFTSVP CAWWWATTSM TTVGYGDIRP DTTTGKIVAF MCILSGILVL
ALPIAIINDR FSACYFTLKL KEAAVRQREA LKKLTKNIAT DSYISVNLRD VYARSIMEML
RLKGRERAST RSSGGDDFWF
