ID A0A1D2MCU4_ORCCI Unreviewed; 512 AA.
AC A0A1D2MCU4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
DE Flags: Fragment;
GN ORFNames=Ocin01_15913 {ECO:0000313|EMBL:ODM90769.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM90769.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM90769.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM90769.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM90769.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJIJ01001798; ODM90769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2MCU4; -.
DR STRING; 48709.A0A1D2MCU4; -.
DR OMA; AFLCCRN; -.
DR OrthoDB; 2902976at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005261; F:monoatomic cation channel activity; IEA:UniProt.
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; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR047871; K_chnl_Slo-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027359; Volt_channel_dom_sf.
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; PF07885; Ion_trans_2; 1.
DR PRINTS; PR01449; BKCHANNELA.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000313|EMBL:ODM90769.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..512
FT /note="BK channel"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008903811"
FT TRANSMEM 40..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..120
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 141..198
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 355..443
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODM90769.1"
SQ SEQUENCE 512 AA; 58888 MW; D011896578A9F3B7 CRC64;
VVLVFKLSIA SLVIYFIDAS SDAVEKCQEW SQNITQQIDL AFNIFFMVYF FIRFIAASDK
LWFMLEMYSF VDYFTIPPSF VSIYMDRTWI GLRFLRALRL MTVPDILQYL NVLKTSSSIR
LAQLISIFIS LENSGDPFDF ENPNQMPYWT CVYFLIVTMS TVGYGDVFCQ TVLGRTFLVF
FLLVGLAIFA SCIPEIIDLI GTRPKYGGTL KNERGRRHIV VCGHITYESV SHFLKDFLHE
DREDVDVEVV FLHRKPPDLE LEGLFKRHFT TVEFFQGTIM NPIDLQRVKV HEADACLVLA
NKYCQDPDAE DAANIMRVIS IKNYSDDIRV IIQLMQYHNK AYLLNIPSWD WKRGDDVICL
AELKLGFIAQ SCLAPGFSTM MANLFAMRSF KTSPDTQAWQ NDYLQGTGCE MYTETLSPSF
VGMTFPQACE LCFIKLKLLL LAIEMKIDDG NDSKISINPR GAKIQANTIG FFIAQSADEV
KRAWFYCKAC HDHITDETMI KKCKCKNCKF FQ
//