ID A8XQV5_CAEBR Unreviewed; 1098 AA.
AC A8XQV5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Protein CBR-SLO-2 {ECO:0000313|EMBL:CAP35030.2};
GN Name=slo-2 {ECO:0000313|WormBase:CBG17348a};
GN Synonyms=Cbr-slo-2 {ECO:0000313|EMBL:CAP35030.2};
GN ORFNames=CBG17348 {ECO:0000313|WormBase:CBG17348a}, CBG_17348
GN {ECO:0000313|EMBL:CAP35030.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP35030.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP35030.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP35030.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HE600924; CAP35030.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XQV5; -.
DR STRING; 6238.A8XQV5; -.
DR WormBase; CBG17348a; CBP43605; WBGene00036999; Cbr-slo-2.
DR eggNOG; KOG3193; Eukaryota.
DR HOGENOM; CLU_003370_0_0_1; -.
DR InParanoid; A8XQV5; -.
DR OMA; MMNDLNR; -.
DR OrthoDB; 2907493at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005228; F:intracellular sodium-activated potassium channel activity; IBA:GO_Central.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR047871; K_chnl_Slo-like.
DR PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR PANTHER; PTHR10027:SF10; SLOWPOKE 2, ISOFORM D; 1.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF07885; Ion_trans_2; 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};
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:UP000008549};
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 136..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..289
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 445..537
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
SQ SEQUENCE 1098 AA; 126482 MW; 6E3EABCA9C48B324 CRC64;
MGTNNNSNRS SMKQRHKRVE SCHSLPADYR IPNKHVARMQ YGEKKNIKHK LQQWFIENPK
ISGFRNFGII FFQINIPGAR IRSCNVLIKL LTCILYCFRV VNDERTYPEE FPLAEAKEKD
LTFYEYLLWV DFDFKIWFAQ TFFALISMVY TILVFYLSYS GSVIRLLINI HFLLELITSF
PFILSIFIPS LTYLYVPVFL NCWLAKERSQ SQILHILISS LPPASSLVHY LQRARAKQID
LFTSFYFVMV TFSTVGYGDW YPDYWASQLC VVILICVALG LIPKQLDELG QTWSERQKSG
TDFSSWNGVE SHVVVTITTL EVEFIRDFLE EFYAHPENQR IQVVLLSPAE LDNQTRMLLK
IPLWNNRVHY VRGSSLRDED LERARVSTAK ACFILSARHV NRKVATDEHT ILRSWAIKDF
APNVRQYVQI FRAETKMHIE HAEVLICEDE FKYALLANNC ICPGISTFIT LLMHTSRGEE
GQKSTEPWHK VYGFHSGNEM YQIRVQDSRF FGEYVGKSFS STSFHAHKEY GIGLIAVAPE
GDTSRMKLNP GSSHIIQSTD TVYYMGLTNE ESLTDFRKGI QSQQKRANVA STIANVGSVA
VDVPHEKTEL ATRKKKKRKE KAADEIHLIE IGEHIQSSRR PSIAMVTEGK IDSSSDSDQE
EICDKCRGPC IQHKLQRTYP QVRTYIGTSN TVCHMMKERR SLCCLKLDEK CAHKSATSAH
EYQWRNRPII LAADRTSSGM YNLVIPLRAY YRPVHDLHPI IILLELEEQD SLNDAFLDAI
SYFPDVYWMK GKIGNLDCLL RAGVSSAEHV VVVKETAVMA EEHTADCNTI ITVQKIHRMF
PRLRMITELT HATNMRFVQF NPNNAYSLAQ SRFEKKERKR GSHMPFMFRL PFAQGGVFSA
NMLDRLLYQA IIKPFVVDLV RLLLGIDQHS DGGYLTSFVI TSDDLWIRNY GRLYQKLCSS
VADIPIGIFR TKKMDTKTVS LDLQEQCKDF ESTEMNRNKD MYDHVKNRMR VLNIRDSHTL
LEGSDEKSAI SYVIINPAQD LELESGDIVY VIRSPIRKDA TNARINPRRG LRRSKNVSET
MDSSNNQVPV IVIDENNM
//
