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Database: UniProt
Entry: J3QMT8_MOUSE
LinkDB: J3QMT8_MOUSE
Original site: J3QMT8_MOUSE 
ID   J3QMT8_MOUSE            Unreviewed;      1135 AA.
AC   J3QMT8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
DE   AltName: Full=Slowpoke homolog {ECO:0000256|ARBA:ARBA00033447};
GN   Name=Kcnma1 {ECO:0000313|Ensembl:ENSMUSP00000136447.2,
GN   ECO:0000313|MGI:MGI:99923};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000136447.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000136447.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000136447.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000136447.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000136447.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC       (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily.
CC       {ECO:0000256|ARBA:ARBA00008648}.
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DR   AlphaFoldDB; J3QMT8; -.
DR   SMR; J3QMT8; -.
DR   ProteomicsDB; 320469; -.
DR   Antibodypedia; 29733; 381 antibodies from 37 providers.
DR   Ensembl; ENSMUST00000177634.8; ENSMUSP00000136447.2; ENSMUSG00000063142.16.
DR   AGR; MGI:99923; -.
DR   MGI; MGI:99923; Kcnma1.
DR   VEuPathDB; HostDB:ENSMUSG00000063142; -.
DR   GeneTree; ENSGT00940000154935; -.
DR   TreeFam; TF314283; -.
DR   ChiTaRS; Kcnma1; mouse.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000063142; Expressed in habenula and 181 other cell types or tissues.
DR   ExpressionAtlas; J3QMT8; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022839; F:monoatomic ion-gated channel activity; IEA:UniProt.
DR   GO; GO:0005267; F:potassium channel activity; IEA:UniProt.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR047871; K_chnl_Slo-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR048735; Slowpoke-like_C.
DR   PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR   PANTHER; PTHR10027:SF33; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT ALPHA-1; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF21014; Slowpoke_C; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   PRINTS; PR00169; KCHANNEL.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW   Proteomics identification {ECO:0007829|MaxQB:J3QMT8,
KW   ECO:0007829|PeptideAtlas:J3QMT8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        54..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          56..271
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          421..508
FT                   /note="Calcium-activated potassium channel BK alpha
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03493"
FT   DOMAIN          903..1023
FT                   /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21014"
FT   REGION          578..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1065..1094
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1135 AA;  127571 MW;  79A978280E9AB2B6 CRC64;
     QEAQKINNGS SQADGTLKPV DEKEEVVAAE VGWMTSVKDW AGVMISAQTL TGRVLVVLVF
     ALSIGALVIY FIDSSNPIES CQNFYKDFTL QIDMAFNVFF LLYFGLRFIA ANDKLWFWLE
     VNSVVDFFTV PPVFVSVYLN RSWLGLRFLR ALRLIQFSEI LQFLNILKTS NSIKLVNLLS
     IFISTWLTAA GFIHLVENSG DPWENFQNNQ ALTYWECVYL LMVTMSTVGY GDVYAKTTLG
     RLFMVFFILG GLAMFASYVP EIIELIGNRK KYGGSYSAVS GRKHIVVCGH ITLESVSNFL
     KDFLHKDRDD VNVEIVFLHN ISPNLELEAL FKRHFTQVEF YQGSVLNPHD LARVKIESAD
     ACLILANKYC ADPDAEDASN IMRVISIKNY HPKIRIITQM LQYHNKAHLL NIPSWNWKEG
     DDAICLAELK LGFIAQSCLA QGLSTMLANL FSMRSFIKIE EDTWQKYYLE GVSNEMYTEY
     LSSAFVGLSF PTVCELCFVK LKLLMIAIEY KSANRESRIL INPGNHLKIQ EGTLGFFIAS
     DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRPVYVEDEQ PPTLSPKKKQ RNGGMRNSPN
     TSPKLMRHDP LLIPGNDQID NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG
     HVVVCIFGDV SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS
     ILPGTPLSRA DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG
     VLQANSQGFT PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP IITELAKPGK LPLVSVNQEK
     NSGTHILMIT ELVNDTNVQF LDQDDDDDPD TELYLTQPFA CGTAFAVSVL DSLMSATYFN
     DNILTLIRTL VTGGATPELE ALIAEENALR GGYSTPQTLA NRDRCRVAQL ALLDGPFADL
     GDGGCYGDLF CKALKTYNML CFGIYRLRDA HLSTPSQCTK RYVITNPPYE FELVPTDLIF
     CLMQFDHNAG QSRASLSHSS HSSQSSSKKS SSVHSIPSTA NRPNRPKSRE SRDKQNATRM
     TRMGQEKKWF TDEPDNAYPR NIQIKPMSTH MANQINQYKS TSSLIPPIRE VEDEC
//
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