ID A0A077YZ43_TRITR Unreviewed; 1206 AA.
AC A0A077YZ43;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
GN ORFNames=TTRE_0000160601 {ECO:0000313|EMBL:CDW53342.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW53342.1};
RN [1] {ECO:0000313|EMBL:CDW53342.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW53342.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HG805850; CDW53342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077YZ43; -.
DR STRING; 36087.A0A077YZ43; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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; IPR048735; Slowpoke-like_C.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10027:SF33; BK CHANNEL; 1.
DR PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF21014; Slowpoke_C; 1.
DR PRINTS; PR01449; BKCHANNELA.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000313|EMBL:CDW53342.1};
KW Ion transport {ECO:0000313|EMBL:CDW53342.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..272
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 343..418
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 574..662
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT DOMAIN 1074..1190
FT /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21014"
FT REGION 82..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1206 AA; 137056 MW; A4CECA833264E812 CRC64;
MTDFHKGSKS MGFYPLNCNQ TAYQHRFEQM TEEERRCLEE RKYWCFLLSS IITFCLSMLL
VVTYRILNHL CCERKKSRRA DVTEPDHREA NGLFPTSPSN NTIEKTSLTA AVADAQSPPQ
QHQTEEAHVG WMTEAKDWAG ELISGQSTTG RILVVLVFVL SIASLIIYFY DASNPHFQVE
TCIPLSQSPS QQIDLAFNIF FLVYFFIRFI AATDKVWFLL EVYSFVDYFT IPPSFVAIYL
ERNWLGLRFS RALRLMTLPD ILQYLNIMKT SNAIRLAQLV SIFISVNLTG AGLIHLVSLR
FVRALRLMSV PDILQYLNVL KTCRSIRLTQ LLSIFLSVSL TGAGFIHLLE NSGDPFQNFE
NPQRITYWEC VYFLLVTMST VGYGDIYCKT TLARLFMVFF ILGGLAMFAS YVPEIADLIG
ARQKYGGQYK SEHGKRHIVV CGYITFESVS HFLQDFLHED REDVDVEVLF IHRVPPDLEL
EGLFKRHFTK VEFFQGTVMD SVDLTRVKVD EADACLVLAN KYSPDPDAED AANIMRVISI
KNYSADIRVI VQLMQYHNKA YLLNIPSWDW RRGDDVICLA ELKLGFIAQS CLAPGFSTMM
ANLFAMRSFK TLPNMPQWLN DYLRGAGMEM YTEKFSTSFY GMTFPEAADL LYTKLGLLLL
AIETKDDEKR ECNIAINPGP SVLITGHTQG FFIAQSADEV KRAFFYCKSC HADIKDVTLI
KKCKCKNLAL FRKEIKQIAM MSNSTRKVSM AVMRPTDRRM SEVRNRHREE GRARRADRYK
RPRVRCDSLE STLDSETTDG SPTDADPKLY ISDSATIETP TIKMGDMEHQ EIKYDSTGMF
HWCPPRPIEE CVLDRNQAKM TVLNGHVVVC LFADKDSPLI GLRNFVMPLR ASNFHYHELK
HMVIVGDIEY LKREWRTLYN LPKISILQGS PLSRADLRAV NINNCDMCVI LSARVPNPSE
DPTLADKEAI LASLNIKAMQ FEDATSFYSF PQELVGLSPF GNTGMLLRPS VSLGTQVPMI
TELVNDSNVQ FLDQDDDDDP DTELYLTQPF ACGTAFAISV LDSLMSTTYF NDSALTLIRT
LVTGGATPEL ELILAEGAGL RGDFSTEERL KNRDRCRVAQ IPLVDSCFQA FQTGATYGQV
LSQALKEYGM LCIGLYRLHD MAPSELNKRY VITNPPPDLK LLPTDYVYVL QPYDHGLKYP
AKQAEQ
//