KCMB1_RAT
ID KCMB1_RAT Reviewed; 191 AA.
AC P97678; O35337; O88805; Q9ESK7; Q9QWI7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Calcium-activated potassium channel subunit beta-1;
DE AltName: Full=BK channel subunit beta-1;
DE Short=BKbeta;
DE Short=BKbeta1;
DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-1;
DE Short=Calcium-activated potassium channel subunit beta;
DE AltName: Full=Charybdotoxin receptor subunit beta-1;
DE AltName: Full=K(VCA)beta-1;
DE AltName: Full=Maxi K channel subunit beta-1;
DE AltName: Full=Slo-beta-1;
DE Short=Slo-beta;
DE AltName: Full=Slowpoke-beta;
GN Name=Kcnmb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=9105668; DOI=10.1016/s0169-328x(96)00230-6;
RA Chang C.-P., Dworetzky S.I., Wang J., Goldstein M.E.;
RT "Differential expression of the alpha and beta subunits of the large-
RT conductance calcium-activated potassium channel: implication for channel
RT diversity.";
RL Brain Res. Mol. Brain Res. 45:33-40(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=9888999; DOI=10.1006/geno.1998.5627;
RA Jiang Z., Wallner M., Meera P., Toro L.;
RT "Human and rodent MaxiK channel beta-subunit genes: cloning and
RT characterization.";
RL Genomics 55:57-67(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Vascular smooth muscle;
RA Lange A.R., Gebremedhin D., Aebly M., Harder D.R.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RA Reimann F.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Aorta;
RA Ohya S., Watanabe M., Imaizumi Y.;
RT "Molecular cloning of a novel spliced variant of calcium activated
RT potassium channel beta subunit in rat smooth muscle.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1
CC (maxiK) channel. Modulates the calcium sensitivity and gating kinetics
CC of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases
CC the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also
CC modifies KCNMA1 channel kinetics and alters its pharmacological
CC properties. It slows down the activation and the deactivation kinetics
CC of the channel. Acts as a negative regulator of smooth muscle
CC contraction by enhancing the calcium sensitivity to KCNMA1. Its
CC presence is also a requirement for internal binding of the KCNMA1
CC channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and
CC for external binding of the agonist hormone 17-beta-estradiol (E2).
CC Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1
CC peptide blocker by increasing the CTX association rate and decreasing
CC the dissociation rate (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules
CC of KCMNB1 per KCNMA1 tetramer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P97678-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=P97678-2; Sequence=VSP_009825, VSP_009826;
CC Name=3; Synonyms=1c;
CC IsoId=P97678-3; Sequence=VSP_009824, VSP_009825, VSP_009826;
CC -!- TISSUE SPECIFICITY: Weakly expressed. In brain, it is expressed in a
CC few discrete populations of neurons that also express KCNMA1.
CC {ECO:0000269|PubMed:9105668}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB1
CC subfamily. {ECO:0000305}.
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DR EMBL; U54498; AAD11548.1; -; mRNA.
DR EMBL; AF020712; AAD11858.1; -; mRNA.
DR EMBL; U79661; AAB38413.1; -; mRNA.
DR EMBL; U40602; AAB96355.1; -; mRNA.
DR EMBL; AB010963; BAA33448.1; -; mRNA.
DR EMBL; AB050745; BAB17678.1; -; mRNA.
DR RefSeq; NP_062146.1; NM_019273.1. [P97678-1]
DR RefSeq; XP_006246151.1; XM_006246089.3. [P97678-1]
DR RefSeq; XP_008765785.1; XM_008767563.2. [P97678-1]
DR RefSeq; XP_008765786.1; XM_008767564.2. [P97678-2]
DR AlphaFoldDB; P97678; -.
DR SMR; P97678; -.
DR BioGRID; 248358; 1.
DR STRING; 10116.ENSRNOP00000007408; -.
DR BindingDB; P97678; -.
DR GlyGen; P97678; 2 sites.
DR PaxDb; P97678; -.
DR Ensembl; ENSRNOT00000007408; ENSRNOP00000007408; ENSRNOG00000005465. [P97678-1]
DR Ensembl; ENSRNOT00000090659; ENSRNOP00000071161; ENSRNOG00000005465. [P97678-2]
DR GeneID; 29747; -.
DR KEGG; rno:29747; -.
DR UCSC; RGD:2961; rat. [P97678-1]
DR CTD; 3779; -.
DR RGD; 2961; Kcnmb1.
DR eggNOG; ENOG502RZA0; Eukaryota.
DR GeneTree; ENSGT00950000183039; -.
DR InParanoid; P97678; -.
DR OMA; FPYPCLQ; -.
DR OrthoDB; 1178937at2759; -.
DR PhylomeDB; P97678; -.
DR TreeFam; TF328589; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:P97678; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000005465; Expressed in colon and 16 other tissues.
DR Genevisible; P97678; RN.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:1903413; P:cellular response to bile acid; IDA:RGD.
DR GO; GO:0071361; P:cellular response to ethanol; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0005513; P:detection of calcium ion; IBA:GO_Central.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:0051592; P:response to calcium ion; IDA:RGD.
DR GO; GO:0042311; P:vasodilation; IDA:RGD.
DR InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
DR PANTHER; PTHR10258; PTHR10258; 1.
DR Pfam; PF03185; CaKB; 1.
DR PRINTS; PR01450; BKCHANNELB.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..191
FT /note="Calcium-activated potassium channel subunit beta-1"
FT /id="PRO_0000187049"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 103..122
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_009824"
FT VAR_SEQ 123..146
FT /note="VRANFYKHHNFYCFSAPQVNETSV -> LRSRPISSAQQHGVTRNGRGPGQA
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_009825"
FT VAR_SEQ 147..191
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_009826"
FT CONFLICT 14
FT /note="T -> A (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 28..30
FT /note="AIT -> VVA (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="V -> M (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..61
FT /note="VETNIK -> IESNIR (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="R -> K (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="M -> V (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="Y -> H (in Ref. 1; AAD11548)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..111
FT /note="NLD -> SLE (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..121
FT /note="TALVDVK -> VARADVE (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> T (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..132
FT /note="YKHHN -> HEHRI (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..141
FT /note="APQV -> TTRE (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..149
FT /note="SVVYQ -> TVLYR (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="I -> T (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="F -> L (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="M -> I (in Ref. 1; AAD11548)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..182
FT /note="LNR -> INQ (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..187
FT /note="VL -> IP (in Ref. 1; AAD11548)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="V -> I (in Ref. 2; AAB38413)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21909 MW; D39F2FE4D69D7662 CRC64;
MGKKLVMAQK RGETRALCLG VAMVVCAAIT YYILGTTVLP LYQKSVWTQE STCHLVETNI
KDQEELEGRK VPQYPCLWVN VSAVGRWAML YHTEDTRDQN QQCSYIPRNL DNYQTALVDV
KKVRANFYKH HNFYCFSAPQ VNETSVVYQR LYGPQILLFS FFWPTFLLTG GLLIIAMVKL
NRSLSVLAAQ K
