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Database: UniProt
Entry: A0A2Y9J1S9_ENHLU
LinkDB: A0A2Y9J1S9_ENHLU
Original site: A0A2Y9J1S9_ENHLU 
ID   A0A2Y9J1S9_ENHLU        Unreviewed;      1238 AA.
AC   A0A2Y9J1S9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=LOC111144685 {ECO:0000313|RefSeq:XP_022354802.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022354802.1};
RN   [1] {ECO:0000313|RefSeq:XP_022354802.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022354802.1};
RG   RefSeq;
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   RefSeq; XP_022354802.1; XM_022499094.1.
DR   AlphaFoldDB; A0A2Y9J1S9; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
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   ECO:0000313|RefSeq:XP_022354802.1};
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:UP000248482};
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        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        369..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          183..398
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          548..635
FT                   /note="Calcium-activated potassium channel BK alpha
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03493"
FT   DOMAIN          1058..1178
FT                   /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21014"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..786
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1220..1238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1238 AA;  137679 MW;  23E5587C5ACA5D1D CRC64;
     MANGGGGGGG SSGGGGGGGG GGGSSLRMSS NIHANHLSLD ASSSSSSSSS SSSSSSSSSS
     SSVHEPKMDA LIIPVTMEVP CDSRGQRMWW AFLASSMVTF FGGLFIILLW RTLKYLWTVC
     CHCGGKTKEA QKINNGSSQA DGTLKPVDEK EEAVAAEVGW MTSVKDWAGV MISAQTLTGR
     VLVVLVFALS IGALVIYFID SSNPIESCQN FYKDFTLQID MAFNVFFLLY FGLRFIAAND
     KLWFWLEVNS VVDFFTVPPV FVSVYLNRSW LGLRFLRALR LIQFSEILQF LNILKTSNSI
     KLVNLLSIFI STWLTAAGFI HLVENSGDPW ENFQNNQALT YWECVYLLMV TMSTVGYGDV
     YAKTTLGRLF MVFFILGGLA MFASYVPEII ELIGNRKKYG GSYSAVSGRK HIVVCGHITL
     ESVSNFLKDF LHKDRDDVNV EIVFLHNISP NLELEALFKR HFTQVEFYQG SVLNPHDLAR
     VKIESADACL ILANKYCADP DAEDASNIMR VISIKNYHPK IRIITQMLQY HNKAHLLNIP
     SWNWKEGDDA ICLAELKLGF IAQSCLAQGL STMLANLFSM RSFIKIEEDT WQKYYLEGVS
     NEMYTEYLSS AFVGLSFPTV CELCFVKLKL LMIAIEYKSA NRESRILINP GNHLKIQEGT
     LGFFIASDAK EVKRAFFYCK ACHDDITDPK RIKKCGCKRP KMSIYKRMRR ACCFDCGRSE
     RDCSCMSGRV RANMDTLERT FPLSSVSVND CSTSFRAFED EQPSTLSPKK KQRNGGMRNS
     PSSSPKLMRH DPLLIPGNDQ IDNMDSNVKK YDSTGMFHWC APKEIEKVIL TRSEAAMTVL
     SGHVVVCIFG DVSSALIGLR NLVMPLRASN FHYHELKHIV FVGSIEYLKR EWETLHNFPK
     VSILPGTPLS RADLRAVNIN LCDMCVILSA NQNNIDDTSL QDKECILASL NIKSMQFDDS
     IGVLQANSQG FTPPGMDRSS PDNSPVHGML RQPSITTGVN IPIITELVND TNVQFLDQDD
     DDDPDTELYL TQPFACGTAF AVSVLDSLMS ATYFNDNILT LIRTLVTGGA TPELEALIAE
     ENALRGGYST PQTLANRDRC RVAQLALLDG PFADLGDGGC YGDLFCKALK TYNMLCFGIY
     RLRDAHLSTP SQCTKRYVIT NPPYEFELVP TDLIFCLMQF DHNAGQSRAS LSHSSHSSQS
     SSKKSSSVHS IPSTANRQNR PKSRESRDKQ KYVQEERL
//
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