KCMB1_RABIT
ID KCMB1_RABIT Reviewed; 191 AA.
AC O46372; Q5MGS8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
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;
GN Name=KCNMB1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Brain;
RX PubMed=10821684; DOI=10.1021/bi992865z;
RA Giangiacomo K.M., Fremont V., Mullmann T.J., Hanner M., Cox R.H.,
RA Garcia M.L.;
RT "Interaction of charybdotoxin S10A with single maxi-K channels: kinetics of
RT blockade depend on the presence of the beta 1 subunit.";
RL Biochemistry 39:6115-6122(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11294242; DOI=10.1007/s004240000463;
RA Ohya S., Yamamura H., Muraki K., Watanabe M., Imaizumi Y.;
RT "Comparative study of the molecular and functional expression of L-type
RT Ca2+ channels and large-conductance, Ca2+-activated K+ channels in rabbit
RT aorta and vas deferens smooth muscle.";
RL Pflugers Arch. 441:611-620(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Sakamoto H., Ide T., Kasai M.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15613616; DOI=10.1152/ajprenal.00340.2004;
RA Pluznick J.L., Wei P., Grimm P.R., Sansom S.C.;
RT "BK-beta1 subunit: immunolocalization in the mammalian connecting tubule
RT and its role in the kaliuretic response to volume expansion.";
RL Am. J. Physiol. 288:F846-F854(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Sphincter of Oddi;
RA Zhang X., Wang S., Wang Y., Du P., Wei J.;
RT "Cloning and characterization of large conductance Ca2+-activated K+
RT channel beta1 subunit in rabbit sphincter of Oddi.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang X., Wang S., Yan Z., Zhang Y., Wei J.;
RT "Cloning and characterization of rabbit large conductance calcium activated
RT potassium channel beta1 subunit gene and its promoter region.";
RL Submitted (JUL-2006) 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 -!- 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; AF107300; AAD17994.1; -; mRNA.
DR EMBL; AB001934; BAA25630.1; -; mRNA.
DR EMBL; AB009313; BAA23748.1; -; mRNA.
DR EMBL; AY829265; AAV88620.1; -; mRNA.
DR EMBL; DQ821756; ABG49461.1; -; mRNA.
DR EMBL; DQ839485; ABG74946.1; -; Genomic_DNA.
DR RefSeq; NP_001075694.1; NM_001082225.1.
DR AlphaFoldDB; O46372; -.
DR SMR; O46372; -.
DR STRING; 9986.ENSOCUP00000000466; -.
DR Ensembl; ENSOCUT00000000539; ENSOCUP00000000466; ENSOCUG00000000539.
DR GeneID; 100009034; -.
DR KEGG; ocu:100009034; -.
DR CTD; 3779; -.
DR eggNOG; ENOG502RZA0; Eukaryota.
DR GeneTree; ENSGT00950000183039; -.
DR HOGENOM; CLU_085739_1_1_1; -.
DR InParanoid; O46372; -.
DR OMA; FPYPCLQ; -.
DR OrthoDB; 1178937at2759; -.
DR TreeFam; TF328589; -.
DR Proteomes; UP000001811; Chromosome 3.
DR Bgee; ENSOCUG00000000539; Expressed in aorta and 15 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro.
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 Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..191
FT /note="Calcium-activated potassium channel subunit beta-1"
FT /id="PRO_0000187048"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..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"
SQ SEQUENCE 191 AA; 21829 MW; 51EA2FEF9E3C9474 CRC64;
MGKKLVMAQK RGETRALCLG VAMVMCAVIT YYILGTTMLP LYQKSVWTQE SLCRLIETNI
RDQEELEGKK VPQYPCLWVN VSAVGKWAVL YHTEETRDRN QQCSYIPGSL DNYQMALADV
EKVRAKFHER QVFYCFSTTQ ENETSVLYQR LYGPQALLAS LFWPTFLLTG GLLIIAMVKI
NRSLSILAAQ K
