KCAB2_BOVIN
ID KCAB2_BOVIN Reviewed; 367 AA.
AC Q27955; Q58HC4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
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=KVB2;
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], AND PROTEIN SEQUENCE OF 1-18; 78-107; 198-215;
RP 217-233 AND 266-294.
RC TISSUE=Brain;
RX PubMed=8127858; DOI=10.1073/pnas.91.5.1637;
RA Scott V.E.S., Rettig J., Parcej D.N., Keen J.N., Findlay J.B.C., Pongs O.,
RA Dolly J.O.;
RT "Primary structure of a beta subunit of alpha-dendrotoxin-sensitive K+
RT channels from bovine brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1637-1641(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L.;
RT "Ion channels in lens epithelia.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH KCNA1 AND KCNA2, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11086297;
RX DOI=10.1002/1096-9861(20000101)429:1<166::aid-cne13>3.0.co;2-y;
RA Rasband M.N., Trimmer J.S.;
RT "Subunit composition and novel localization of K+ channels in spinal
RT cord.";
RL J. Comp. Neurol. 429:166-176(2001).
CC -!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits (By similarity).
CC Contributes to the regulation of nerve signaling, and prevents neuronal
CC hyperexcitability (By similarity). Promotes expression of the pore-
CC forming alpha subunits at the cell membrane, and thereby increases
CC channel activity (By similarity). Promotes potassium channel closure
CC via a mechanism that does not involve physical obstruction of the
CC channel pore (By similarity). Promotes KCNA4 channel closure (By
CC similarity). Modulates the functional properties of KCNA5 (By
CC 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}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric
CC potassium channel alpha subunits gives rise to a heterooctamer (By
CC similarity). Identified in potassium channel complexes containing
CC KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity).
CC Interacts with KCNA1 (PubMed:11086297). Interacts with KCNA2
CC (PubMed:11086297). Interacts with KCNA4 and KCND3 (By similarity).
CC Interacts with KCNA5 (By similarity). Interacts with KCNB2 (By
CC similarity). Interacts (in unphosphorylated form) with MAPRE1 (By
CC similarity). Forms a ternary complex with SQSTM1 and PRKCZ (By
CC similarity). {ECO:0000250|UniProtKB:P62482,
CC ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:11086297}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62483}.
CC Membrane {ECO:0000269|PubMed:11086297}; 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:0000269|PubMed:11086297}. 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 -!- TISSUE SPECIFICITY: Detected in the juxtaparanodal region of nodes of
CC Ranvier in myelinated nerve fibers in the spinal cord (at protein
CC level). {ECO:0000269|PubMed:11086297}.
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 -!- PTM: Phosphorylated by PRKCZ; may be regulated by incorporation in a
CC complex composed of PRKCZ and SQSTM1. {ECO:0000250|UniProtKB:P62483}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; X70661; CAA49999.1; -; mRNA.
DR EMBL; AY950785; AAX51985.1; -; mRNA.
DR PIR; A53131; A53131.
DR RefSeq; NP_001014405.1; NM_001014383.1.
DR RefSeq; XP_005217169.1; XM_005217112.3.
DR AlphaFoldDB; Q27955; -.
DR SMR; Q27955; -.
DR CORUM; Q27955; -.
DR STRING; 9913.ENSBTAP00000042823; -.
DR PaxDb; Q27955; -.
DR PRIDE; Q27955; -.
DR Ensembl; ENSBTAT00000070629; ENSBTAP00000059526; ENSBTAG00000008125.
DR GeneID; 541597; -.
DR KEGG; bta:541597; -.
DR CTD; 8514; -.
DR VEuPathDB; HostDB:ENSBTAG00000008125; -.
DR VGNC; VGNC:30428; KCNAB2.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT00940000157867; -.
DR InParanoid; Q27955; -.
DR OMA; PPYSLFW; -.
DR OrthoDB; 1106773at2759; -.
DR TreeFam; TF324563; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000008125; Expressed in temporal cortex and 102 other tissues.
DR ExpressionAtlas; Q27955; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:1990031; C:pinceau fiber; ISS:UniProtKB.
DR GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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: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:0070995; P:NADPH oxidation; ISS:UniProtKB.
DR GO; GO:0098900; P:regulation of action potential; IBA:GO_Central.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; 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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Ion channel; Ion transport; Membrane;
KW Methylation; NADP; Oxidoreductase; Phosphoprotein; 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_0000148745"
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"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62482"
FT MOD_RES 28
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 28
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62482"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
SQ SEQUENCE 367 AA; 40985 MW; 2C8B5EDED031AED8 CRC64;
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF
GGQITDEMAE QLMTLAYDNG INLFDTAEVY AAGKAEVVLG NIIKKKGWRR SSLVITTKIF
WGGKAETERG LSRKHIIEGL KASLERLQLE YVDVVFANRP DPNTPMEETV RAMTHVINQG
MAMYWGTSRW SSMEIMEAYS VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA
MTWSPLACGI VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
CTLPQLAIAW CLRNEGVSSV LLGASSADQL MENIGAIQVL PKLSSSIIHE IDSILGNKPY
SKKDYRS
