KCAB2_XENLA
ID KCAB2_XENLA Reviewed; 367 AA.
AC Q9PTM5;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Voltage-gated potassium channel subunit beta-2;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P62483};
DE AltName: Full=K(+) channel subunit beta-2;
DE AltName: Full=Kv-beta-2;
GN Name=kcnab2; Synonyms=kvb-A, kvb2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tadpole head;
RX PubMed=10594054; DOI=10.1523/jneurosci.19-24-10706.1999;
RA Lazaroff M.A., Hofmann A.D., Ribera A.B.;
RT "Xenopus embryonic spinal neurons express potassium channel Kvbeta
RT subunits.";
RL J. Neurosci. 19:10706-10715(1999).
CC -!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits
CC (PubMed:10594054). Contributes to the regulation of nerve signaling,
CC and prevents neuronal hyperexcitability (By similarity). Promotes
CC expression of the pore-forming alpha subunits at the cell membrane, and
CC thereby increases channel activity (By similarity). Promotes potassium
CC channel closure via a mechanism that does not involve physical
CC obstruction of the channel pore (By similarity). Promotes KCNA4 channel
CC closure (By similarity). Modulates the functional properties of KCNA5
CC (By similarity). Enhances KCNB2 channel activity (By similarity). Binds
CC NADPH and has NADPH-dependent aldoketoreductase activity (By
CC similarity). Has broad substrate specificity and can catalyze the
CC reduction of methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2,
CC 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in
CC vitro) (By similarity). {ECO:0000250|UniProtKB:P62482,
CC ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:10594054}.
CC -!- SUBUNIT: Forms heteromultimeric complex with alpha subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62483}.
CC Membrane {ECO:0000250|UniProtKB:P62483}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P62483}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P62483}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P62483}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P62483}. Note=Recruited to the cytoplasmic side
CC of the cell membrane via its interaction with pore-forming potassium
CC channel alpha subunits. Associates with microtubules when
CC unphosphorylated. {ECO:0000250|UniProtKB:P62483}.
CC -!- DEVELOPMENTAL STAGE: Expression first detected in somites at embryonic
CC stage 24 (26 hours). At stage 29 (35 hours), expression is detected in
CC the spinal cord. In stage 30 embryos (36 hours), expression is down-
CC regulated in somites and up-regulated in spinal cord. By stage 35-36
CC (50 hours), expression is limited to dorsal spinal neurons of the
CC spinal cord. {ECO:0000269|PubMed:10594054}.
CC -!- DOMAIN: In contrast to KCNAB1, the shorter N-terminal domain of KCNAB2
CC cannot mediate closure of delayed rectifier potassium channels by
CC physically obstructing the pore. {ECO:0000250|UniProtKB:Q13303}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AF172144; AAD56312.1; ALT_SEQ; mRNA.
DR RefSeq; XP_018079897.1; XM_018224408.1.
DR AlphaFoldDB; Q9PTM5; -.
DR SMR; Q9PTM5; -.
DR MaxQB; Q9PTM5; -.
DR DNASU; 399149; -.
DR GeneID; 399149; -.
DR CTD; 399149; -.
DR Xenbase; XB-GENE-990282; kcnab2.L.
DR OrthoDB; 1106773at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 399149; Expressed in brain and 18 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0070995; P:NADPH oxidation; 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; IPR005401; K_chnl_volt-dep_bsu_KCNAB2.
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; PR01579; KCNAB2CHANEL.
DR PRINTS; PR01577; KCNABCHANNEL.
DR SUPFAM; SSF51430; SSF51430; 1.
DR TIGRFAMs; TIGR01293; Kv_beta; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Ion channel;
KW Ion transport; Membrane; NADP; Oxidoreductase; Potassium;
KW Potassium transport; Reference proteome; Synapse; Synaptosome; Transport;
KW Voltage-gated channel.
FT CHAIN 1..367
FT /note="Voltage-gated potassium channel subunit beta-2"
FT /id="PRO_0000148749"
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 56..57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 188..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 243..248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 323..329
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
SQ SEQUENCE 367 AA; 40982 MW; A8425593690F48A0 CRC64;
MYPESTTDSP ARLSLRQTGS PGMIYSARYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF
GGQITDEMAE QLMTLAYDNG INLFDTAEVY AAGKAEVVLG NIIKKKGWRR SSLVITTKIF
WGGKAETERG LSRKHIIEGL KASLERLQLD YVDVVFANRP DPNTPMEETV RAMTHVINQG
MAMYWGTSRW SSMEIMEAYS VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA
MTWSPLACGI VSGKYDGGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK EFQAIAERLG
CTLPQLAIAW CLRNEGVSSV LLGASNADQL LENIGAIQVL PKLSSSIIHE IDGILGNKPY
SKKDYRS
