KCAB1_BOVIN
ID KCAB1_BOVIN Reviewed; 401 AA.
AC Q4PJK1; Q05B86;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Voltage-gated potassium channel subunit beta-1;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P63144};
DE AltName: Full=K(+) channel subunit beta-1;
DE AltName: Full=Kv-beta-1;
GN Name=KCNAB1;
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 [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L.;
RT "Ion channels in ocular epithelia.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits (By similarity).
CC Modulates action potentials via its effect on the pore-forming alpha
CC subunits (By similarity). Promotes expression of the pore-forming alpha
CC subunits at the cell membrane, and thereby increases channel activity
CC (By similarity). Mediates closure of delayed rectifier potassium
CC channels by physically obstructing the pore via its N-terminal domain
CC and increases the speed of channel closure for other family members (By
CC similarity). Promotes the closure of KCNA1, KCNA2 and KCNA5 channels
CC (By similarity). Accelerates KCNA4 channel closure (By similarity).
CC Accelerates the closure of heteromeric channels formed by KCNA1 and
CC KCNA4 (By similarity). Accelerates the closure of heteromeric channels
CC formed by KCNA2, KCNA5 and KCNA6 (By similarity). Enhances KCNB1 and
CC KCNB2 channel activity (By similarity). Binds NADPH; this is required
CC for efficient down-regulation of potassium channel activity (By
CC similarity). Has NADPH-dependent aldoketoreductase activity (By
CC similarity). Oxidation of the bound NADPH strongly decreases N-type
CC inactivation of potassium channel activity (By similarity).
CC {ECO:0000250|UniProtKB:P63143, ECO:0000250|UniProtKB:P63144,
CC ECO:0000250|UniProtKB:Q14722}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric
CC potassium channel alpha subunits gives rise to a heterooctamer
CC (Probable). Identified in potassium channel complexes containing KCNA1,
CC KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity).
CC Interacts with KCNA1 (By similarity). Interacts with the dimer formed
CC by GNB1 and GNG2; this enhances KCNA1 binding (By similarity).
CC Interacts with KCNA4 (By similarity). Interacts with KCNA5 (By
CC similarity). Interacts with KCNB2 (By similarity). Interacts with
CC SQSTM1 (By similarity). Part of a complex containing KCNA1, KCNA4 and
CC LGI1; interaction with LGI1 inhibits down-regulation of KCNA1 channel
CC activity (By similarity). {ECO:0000250|UniProtKB:P63143,
CC ECO:0000250|UniProtKB:P63144, ECO:0000250|UniProtKB:Q14722,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14722}.
CC Membrane {ECO:0000250|UniProtKB:P63144}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P63144}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P63144}. Cell membrane
CC {ECO:0000250|UniProtKB:Q14722}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q14722}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q14722}. Note=Recruited to the cytoplasmic side
CC of the cell membrane via its interaction with pore-forming potassium
CC channel alpha subunits. {ECO:0000250|UniProtKB:Q14722}.
CC -!- DOMAIN: The N-terminal domain of the beta subunit mediates closure of
CC delayed rectifier potassium channels by physically obstructing the
CC pore. {ECO:0000250|UniProtKB:Q14722}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; DQ083328; AAY82471.1; -; mRNA.
DR EMBL; BC122624; AAI22625.1; -; mRNA.
DR RefSeq; NP_001020507.1; NM_001025336.2.
DR AlphaFoldDB; Q4PJK1; -.
DR SMR; Q4PJK1; -.
DR BioGRID; 182744; 1.
DR STRING; 9913.ENSBTAP00000054768; -.
DR PaxDb; Q4PJK1; -.
DR PRIDE; Q4PJK1; -.
DR Ensembl; ENSBTAT00000024576; ENSBTAP00000024576; ENSBTAG00000018465.
DR GeneID; 526133; -.
DR KEGG; bta:526133; -.
DR CTD; 7881; -.
DR VEuPathDB; HostDB:ENSBTAG00000018465; -.
DR VGNC; VGNC:30427; KCNAB1.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT00940000156760; -.
DR HOGENOM; CLU_023205_2_0_1; -.
DR InParanoid; Q4PJK1; -.
DR OMA; VDLWQVH; -.
DR Reactome; R-BTA-1296072; Voltage gated Potassium channels.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000018465; Expressed in trachea and 102 other tissues.
DR ExpressionAtlas; Q4PJK1; baseline.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; IBA:GO_Central.
DR GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
DR InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR InterPro; IPR005400; K_chnl_volt-dep_bsu_KCNAB1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43150; PTHR43150; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR01578; KCNAB1CHANEL.
DR PRINTS; PR01577; KCNABCHANNEL.
DR SUPFAM; SSF51430; SSF51430; 1.
DR TIGRFAMs; TIGR01293; Kv_beta; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Ion channel; Ion transport; Membrane; NADP;
KW Oxidoreductase; Potassium; Potassium transport; Reference proteome;
KW Transport; Voltage-gated channel.
FT CHAIN 1..401
FT /note="Voltage-gated potassium channel subunit beta-1"
FT /id="PRO_0000148738"
FT ACT_SITE 124
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 90..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 222..223
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 277..282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 288
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 357..363
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
SQ SEQUENCE 401 AA; 44710 MW; F9F17404DF35FDA1 CRC64;
MQVSIACTEH NLKSRNGEDR LLSKQSSTAP NVVNAARAKF RTVAIIARSL GTFTPQHHIS
LKESTAKQTG MKYRNLGKSG LRVSCLGLGT WVTFGGQISD EVAERLMTIA YESGVNLFDT
AEVYAAGKAE VILGSIIKKK GWRRSSLVIT TKLYWGGKAE TERGLSRKHI IEGLKGSLQR
LQLEYVDVVF ANRPDSNTPM EEIVRAMTHV INQGMAMYWG TSRWSAMEIM EAYSVARQFN
MIPPVCEQAE YHLFQREKVE VQLPELYHKI GVGAMTWSPL ACGIISGKYG NGVPESSRAS
LKCYQWLKER IVSEEGRKQQ NKLKDLSPIA ERLGCTLPQL AVAWCLRNEG VSSVLLGSST
PEQLIENLGA IQVLPKMTSH VVNEIDNILR NKPYSKKDYR S
