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Database: UniProt
Entry: G1MHE3_AILME
LinkDB: G1MHE3_AILME
Original site: G1MHE3_AILME 
ID   G1MHE3_AILME            Unreviewed;      1269 AA.
AC   G1MHE3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 58.
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:ENSAMEP00000018778.2};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000018778.2, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000018778.2, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000018778.2}
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; G1MHE3; -.
DR   Ensembl; ENSAMET00000019530.2; ENSAMEP00000018778.2; ENSAMEG00000017723.2.
DR   GeneTree; ENSGT00940000154935; -.
DR   HOGENOM; CLU_006846_0_0_1; -.
DR   InParanoid; G1MHE3; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005901; C:caveola; IEA:Ensembl.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR   GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IEA:Ensembl.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:Ensembl.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0045794; P:negative regulation of cell volume; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR   GO; GO:0060083; P:smooth muscle contraction involved in micturition; IEA:Ensembl.
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:UP000008912};
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        67..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          162..377
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          527..614
FT                   /note="Calcium-activated potassium channel BK alpha
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03493"
FT   DOMAIN          1037..1157
FT                   /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21014"
FT   REGION          19..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1167..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1199..1228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1269 AA;  142263 MW;  7B43A3ECFF47769C CRC64;
     GGGSSLRMSS NIHANHLSLD ASSSSSSSSS SSSSSSSSSS SVHEPKMDAL IIPVTMEVPC
     DSRGQRMWWA FLASSMVTFF GGLFIILLWR TLKYLWTVCC HCGGKTKEAQ KINNGSTQAD
     GTLKPVDEKE EAVAAEVGWM TSVKDWAGVM ISAQTLTGRV LVVLVFALSI GALVIYFIDS
     SNPIESCQNF YKDFTLQIDM AFNVFFLLYF GLRFIAANDK LWFWLEVNSV VDFFTVPPVF
     VSVYLNRSWL GLRFLRALRL IQFSEILQFL NILKTSNSIK LVNLLSIFIS TWLTAAGFIH
     LVENSGDPWE NFQNNQALTY WECVYLLMVT MSTVGYGDVY AKTTLGRLFM VFFILGGLAM
     FASYVPEIIE LIGNRKKYGG SYSAVSGRKH IVVCGHITLE SVSNFLKDFL HKDRDDVNVE
     IVFLHNISPN LELEALFKRH FTQVEFYQGS VLNPHDLARV KIESADACLI LANKYCADPD
     AEDASNIMRV ISIKNYHPKI RIITQMLQYH NKAHLLNIPS WNWKEGDDAI CLAELKLGFI
     AQSCLAQGLS TMLANLFSMR SFIKIEEDTW QKYYLEGVSN EMYTEYLSSA FVGLSFPTVC
     ELCFVKLKLL MIAIEYKSAN RESRILINPG NHLKIQEGTL GFFIASDAKE VKRAFFYCKA
     CHDDITDPKR IKKCGCKRPK MSIYKRMRRA CCFDCGRSER DCSCMSGRVR ANMDTLERNF
     PLSSVSVNDC STSFRAFEDE QPSTLSPKKK QRNGGMRNSP SSSPKLMRHD PLLIPGNDQI
     DNMDSNVKKY DSTGMFHWCA PKEIEKVILT RSEAAMTVLS GHVVVCIFGD VSSALIGLRN
     LVMPLRASNF HYHELKHIVF VGSIEYLKRE WETLHNFPKV SILPGTPLSR ADLRAVNINL
     CDMCVILSAN QNNIDDTSLQ DKECILASLN IKSMQFDDSI GVLQANSQGF TPPGMDRSSP
     DNSPVHGMLR QPSITTGVNI PIITELVNDT NVQFLDQDDD DDPDTELYLT QPFACGTAFA
     VSVLDSLMSA TYFNDNILTL IRTLVTGGAT PELEALIAEE NALRGGYSTP QTLANRDRCR
     VAQLALLDGP FADLGDGGCY GDLFCKALKT YNMLCFGIYR LRDAHLSTPS QCTKRYVITN
     PPYEFELVPT DLIFCLMQFD HNAGQSRASL SHSSHSSQSS SKKSSSVHSI PSTANRQNRP
     KSRESRDKQN ATRMNRMGQE KKWFTDEPDN AYPRNIQIKP MSTHMANQIN QYKSTSSLIP
     PIREVEDEC
//
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