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Database: UniProt
Entry: F6YC69_CALJA
LinkDB: F6YC69_CALJA
Original site: F6YC69_CALJA 
ID   F6YC69_CALJA            Unreviewed;      1215 AA.
AC   F6YC69;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Calcium-activated potassium channel subunit alpha-1 {ECO:0000256|ARBA:ARBA00018044};
DE   AltName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
DE   AltName: Full=BKCA alpha {ECO:0000256|ARBA:ARBA00030518};
DE   AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-1 {ECO:0000256|ARBA:ARBA00030288};
DE   AltName: Full=K(VCA)alpha {ECO:0000256|ARBA:ARBA00031597};
DE   AltName: Full=KCa1.1 {ECO:0000256|ARBA:ARBA00030652};
DE   AltName: Full=Maxi K channel {ECO:0000256|ARBA:ARBA00031999};
DE   AltName: Full=Slo-alpha {ECO:0000256|ARBA:ARBA00029583};
DE   AltName: Full=Slo1 {ECO:0000256|ARBA:ARBA00030326};
DE   AltName: Full=Slowpoke homolog {ECO:0000256|ARBA:ARBA00033447};
GN   Name=KCNMA1 {ECO:0000313|Ensembl:ENSCJAP00000001906.3};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001906.3, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000001906.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000001906.3}
RP   IDENTIFICATION.
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; F6YC69; -.
DR   Ensembl; ENSCJAT00000002020.4; ENSCJAP00000001906.3; ENSCJAG00000001073.5.
DR   GeneTree; ENSGT00940000154935; -.
DR   HOGENOM; CLU_006846_0_0_1; -.
DR   Proteomes; UP000008225; Chromosome 12.
DR   Bgee; ENSCJAG00000001073; Expressed in frontal cortex and 5 other cell types or tissues.
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:SF28; 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   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
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        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        296..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        332..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..392
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          542..629
FT                   /note="Calcium-activated potassium channel BK alpha
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03493"
FT   DOMAIN          1035..1155
FT                   /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21014"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1165..1215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1215 AA;  135280 MW;  93A4C9D0767C891F CRC64;
     MANGGGGGGG NSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSVHEP
     KMDALIIPVT MEVPCDSRGQ RMWWAFLASS MVTFFGGLFI ILLWRTLKYL WTVCCHCGGK
     TKEAQKINNG SSQADGTLKP VDEKEEAVAA EVGWMTSVKD WAGVMISAQT LTGRVLVVLV
     FALSIGALVI YFIDSSNPIE SCQNFYKDFT LQIDMAFNVF FLLYFGLRFI AANDKLWFWL
     EVNSVVDFFT VPPVFVSVYL NRSWLGLRFL RALRLIQFSE ILQFLNILKT SNSIKLVNLL
     SIFISTWLTA AGFIHLVENS GDPWENFQNN QALTYWECVY LLMVTMSTVG YGDVYAKTTL
     GRLFMVFFIL GGLAMFASYV PEIIELIGNR KKYGGSYSAV SGRKHIVVCG HITLESVSNF
     LKDFLHKDRD DVNVEIVFLH NISPNLELEA LFKRHFTQVE FYQGSVLNPH DLARVKIESA
     DACLILANKY CADPDAEDAS NIMRVISIKN YHPKIRIITQ MLQYHNKAHL LNIPSWNWKE
     GDDAICLAEL KLGFIAQSCL AQGLSTMLAN LFSMRSFIKI EEDTWQKYYL EGVSNEMYTE
     YLSSAFVGLS FPTVCELCFV KLKLLMIAIE YKSANRESRI LINPGNHLKI QEGTLGFFIA
     SDAKEVKRAF FYCKACHDDI TDPKRIKKCG CKRLEDEQPS TLSPKKKQRN GGMRNSPNTS
     PKLMRHDPLL IPGNDQIDNM DSNVKKYDST GMFHWCAPKD IEKVILVIGW MPYLGPRVLM
     TCLDIAEVRM PTDIQSTSPT STKKLRKTRS EAAMTVLSGH VVVCIFGDVS SALIGLRNLV
     MPLRASNFHY HELKHIVFVG SIEYLKREWE TLHNFPKVSI LPGTPLSRAD LRAVNINLCD
     MCVILSANQN NIDDTSLQDK ECILASLNIK SMQFDDSIGV LQANSQGFTP PGMDRSSPDN
     SPVHGMLRQP SITTGVNIPI ITELVNDTNV QFLDQDDDDD PDTELYLTQP FACGTAFAVS
     VLDSLMSATY FNDNILTLIR TLVTGGATPE LEALIAEENA LRGGYSTPQT LANRDRCRVA
     QLALLDGPFA DLGDGGCYGD LFCKALKTYN MLCFGIYRLR DAHLSTPSQC TKRYVITNPP
     YEFELVPTDL IFCLMQFDHN AGQSRASLSH SSHSSQSSSK KSSSVHSIPS TANRQNRPKS
     RESRDKQKYV QEERL
//
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