KCMB1_CANLF
ID KCMB1_CANLF Reviewed; 191 AA.
AC Q28266;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 102.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8897882; DOI=10.1152/ajpgi.1996.271.4.g629;
RA Vogalis F., Vincent T., Qureshi I., Schmalz F.M., Ward M.W., Sanders K.M.,
RA Horowitz B.;
RT "Cloning and expression of the large-conductance Ca(2+)-activated K+
RT channel from colonic smooth muscle.";
RL Am. J. Physiol. 271:G629-G639(1996).
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 {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; U41002; AAA84001.1; -; mRNA.
DR RefSeq; NP_001003299.1; NM_001003299.1.
DR AlphaFoldDB; Q28266; -.
DR SMR; Q28266; -.
DR STRING; 9615.ENSCAFP00000024942; -.
DR PaxDb; Q28266; -.
DR GeneID; 403983; -.
DR KEGG; cfa:403983; -.
DR CTD; 3779; -.
DR eggNOG; ENOG502RZA0; Eukaryota.
DR InParanoid; Q28266; -.
DR OrthoDB; 1178937at2759; -.
DR Proteomes; UP000002254; Unplaced.
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_0000187045"
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; 21935 MW; 31E115A8FA530875 CRC64;
MGKKLVMAQK RGETRALCLG VAMVMCAVIA YYILGTTMLP LYQKSVWTQK STCHLIETNI
REQEELEGKK VPQYPCLWVN VSAVGRWAVL YHTEDTRDQN HQCSYIPGSL ENYQVARADV
EKVKAKFHEQ QIFYCFSTTR ENETTVLYRR LYGPQTLLFS LFWPTFLLTG GLLIIAMVKI
NQSLSILAAQ R
