KCAB1_CHICK
ID KCAB1_CHICK Reviewed; 401 AA.
AC Q9PWR1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
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; Synonyms=KVB1.1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cochlea;
RX PubMed=10095080; DOI=10.1016/s0169-328x(99)00012-1;
RA Rajeevan M.S., Hu S., Sakai Y., Sokolowski B.H.A.;
RT "Cloning and expression of Shaker alpha- and beta-subunits during inner ear
RT development.";
RL Brain Res. Mol. Brain Res. 66:83-93(1999).
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). Binds NADPH; this is required for efficient down-
CC regulation of potassium channel activity (By similarity). Has NADPH-
CC dependent aldoketoreductase activity (By similarity). Oxidation of the
CC bound NADPH strongly decreases N-type inactivation of potassium channel
CC activity (By similarity). {ECO:0000250|UniProtKB:P63143,
CC ECO:0000250|UniProtKB:P63144, ECO:0000250|UniProtKB:Q14722}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric
CC potassium channel alpha subunits gives rise to a heterooctamer
CC (Probable). {ECO:0000250|UniProtKB:P63144, 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 -!- DEVELOPMENTAL STAGE: In the inner ear, expression detected in the
CC otocyst at embryonic day 3 and in the whole cochlea at E 6. Expressed
CC throughout embryonic development and adulthood.
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:P63144}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; U87787; AAD10624.1; -; mRNA.
DR RefSeq; NP_990237.1; NM_204906.1.
DR AlphaFoldDB; Q9PWR1; -.
DR SMR; Q9PWR1; -.
DR STRING; 9031.ENSGALP00000032335; -.
DR PaxDb; Q9PWR1; -.
DR Ensembl; ENSGALT00000089976; ENSGALP00000059084; ENSGALG00000010269.
DR GeneID; 395730; -.
DR KEGG; gga:395730; -.
DR CTD; 7881; -.
DR VEuPathDB; HostDB:geneid_395730; -.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT00940000156760; -.
DR HOGENOM; CLU_023205_2_0_1; -.
DR InParanoid; Q9PWR1; -.
DR OMA; VDLWQVH; -.
DR OrthoDB; 1106773at2759; -.
DR PhylomeDB; Q9PWR1; -.
DR Reactome; R-GGA-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q9PWR1; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000010269; Expressed in brain and 7 other tissues.
DR ExpressionAtlas; Q9PWR1; baseline and differential.
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; IBA:GO_Central.
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: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_0000148744"
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; 44639 MW; 89DE1F37F5070F89 CRC64;
MQVSIACTEH NLKSRNGEER LISKQNAAAP NVVNAARAKF RTVAIIARSL GTFTPQHHIS
LKESTAKQTG MKYRNLGKSG LRVSCLGLGT WVTFGGQISD EVAEQLMTIA YESGVNLFDT
AEVYAAGKAE VILGNILKKK GWRRSSLVIT TKLYWGGKAE TERGLSRKHI IEGLRASLQR
LQLEYVDVVF ANRPDNNTPM EEIVRAMTHV INQGMAMYWG TSRWSAMEIM EAYSVARQFN
LIPPVCEQAE YHLFQREKVE VQLPELYHKI GVGAMTWSPL ACGIISGKYG NGVPESSRAA
LKCYQWLKEK IISEEGRKQQ TKLKDLSPIA ERLGCTLPQL AVAWCLRNEG VSSVLLGSSN
PEQLIENLGA IQVLPKMTSH IVNEIDNILG NKPYSKKDYR S
