GENTAUR Molecular Products.

 KCMB1_CANLF             Reviewed;         191 AA.
 Q28266;
 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
 23-JAN-2007, sequence version 3.
 07-NOV-2018, entry version 91.
 RecName: Full=Calcium-activated potassium channel subunit beta-1;
 AltName: Full=BK channel subunit beta-1;
          Short=BKbeta;
          Short=BKbeta1;
 AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-1;
          Short=Calcium-activated potassium channel subunit beta;
 AltName: Full=Charybdotoxin receptor subunit beta-1;
 AltName: Full=K(VCA)beta-1;
 AltName: Full=Maxi K channel subunit beta-1;
 AltName: Full=Slo-beta-1;
          Short=Slo-beta;
 Name=KCNMB1;
 Canis lupus familiaris (Dog) (Canis familiaris).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
 Canis.
 NCBI_TaxID=9615;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=8897882;
 Vogalis F., Vincent T., Qureshi I., Schmalz F.M., Ward M.W.,
 Sanders K.M., Horowitz B.;
 "Cloning and expression of the large-conductance Ca(2+)-activated K+
 channel from colonic smooth muscle.";
 Am. J. Physiol. 271:G629-G639(1996).
 -!- FUNCTION: Regulatory subunit of the calcium activated potassium
     KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and
     gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel
     diversity. Increases the apparent Ca(2+)/voltage sensitivity of
     the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and
     alters its pharmacological properties. It slows down the
     activation and the deactivation kinetics of the channel. Acts as a
     negative regulator of smooth muscle contraction by enhancing the
     calcium sensitivity to KCNMA1. Its presence is also a requirement
     for internal binding of the KCNMA1 channel opener
     dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external
     binding of the agonist hormone 17-beta-estradiol (E2). Increases
     the binding activity of charybdotoxin (CTX) toxin to KCNMA1
     peptide blocker by increasing the CTX association rate and
     decreasing the dissociation rate (By similarity). {ECO:0000250}.
 -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4
     molecules of KCMNB1 per KCNMA1 tetramer (By similarity).
     {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
     protein {ECO:0000250}.
 -!- PTM: N-glycosylated. {ECO:0000250}.
 -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB1
     subfamily. {ECO:0000305}.
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 EMBL; U41002; AAA84001.1; -; mRNA.
 RefSeq; NP_001003299.1; NM_001003299.1.
 UniGene; Cfa.3852; -.
 STRING; 9615.ENSCAFP00000024942; -.
 PaxDb; Q28266; -.
 GeneID; 403983; -.
 KEGG; cfa:403983; -.
 CTD; 3779; -.
 eggNOG; ENOG410IWME; Eukaryota.
 eggNOG; ENOG41116AX; LUCA.
 HOGENOM; HOG000290180; -.
 HOVERGEN; HBG052223; -.
 InParanoid; Q28266; -.
 KO; K04937; -.
 Proteomes; UP000002254; Unplaced.
 GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
 GO; GO:0015269; F:calcium-activated potassium channel activity; IBA:GO_Central.
 GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
 GO; GO:0005513; P:detection of calcium ion; IBA:GO_Central.
 InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu.
 PANTHER; PTHR10258; PTHR10258; 1.
 Pfam; PF03185; CaKB; 1.
 PRINTS; PR01450; BKCHANNELB.
 2: Evidence at transcript level;
 Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
 Reference proteome; Transmembrane; Transmembrane helix; Transport.
 CHAIN         1    191       Calcium-activated potassium channel
                              subunit beta-1.
                              /FTId=PRO_0000187045.
 TOPO_DOM      1     15       Cytoplasmic. {ECO:0000255}.
 TRANSMEM     16     36       Helical; Name=1. {ECO:0000255}.
 TOPO_DOM     37    157       Extracellular. {ECO:0000255}.
 TRANSMEM    158    178       Helical; Name=2. {ECO:0000255}.
 TOPO_DOM    179    191       Cytoplasmic. {ECO:0000255}.
 CARBOHYD     80     80       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    142    142       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 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

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