ID A0A1Q3BAL0_CEPFO Unreviewed; 871 AA.
AC A0A1Q3BAL0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cas1_AcylT domain-containing protein/Ion_trans_2 domain-containing protein {ECO:0000313|EMBL:GAV64939.1};
GN ORFNames=CFOL_v3_08454 {ECO:0000313|EMBL:GAV64939.1};
OS Cephalotus follicularis (Albany pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV64939.1, ECO:0000313|Proteomes:UP000187406};
RN [1] {ECO:0000313|Proteomes:UP000187406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA Fukushima K., Hasebe M., Fang X.;
RT "Cephalotus genome sequencing.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010666}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.7) family. {ECO:0000256|ARBA:ARBA00010159}.
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:GAV64939.1}.
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DR EMBL; BDDD01000376; GAV64939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3BAL0; -.
DR InParanoid; A0A1Q3BAL0; -.
DR OrthoDB; 1000700at2759; -.
DR Proteomes; UP000187406; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProt.
DR GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0045492; P:xylan biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.287.70; -; 2.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR13533; N-ACETYLNEURAMINATE 9-O-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR13533:SF1; N-ACETYLNEURAMINATE 9-O-ACETYLTRANSFERASE; 1.
DR Pfam; PF07779; Cas1_AcylT; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000187406};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 593..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 623..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..214
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 261..330
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 426..844
FT /note="Cas1p 10 TM acyl transferase"
FT /evidence="ECO:0000259|Pfam:PF07779"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 100226 MW; 80686B9D2E16F71F CRC64;
MEKDLKLPYL SPRQKPIPPT PPLCPLPEDG EISLPLPLTP SELKNNLIFG PCSPSPRETS
PLVDALTLST NSSIPSPSDS FMSSWLIDPN YLWTKTKLHR SKTAPAIATI NDAMRQVIPK
PQFGSQSVVR QAVVLLVIYL SLGVVIYWFN RDNFTANKTH PVVDALYFCI VTMCTIGYGD
ITPNSVPTKL FSIMFVLVGF GFIDILLSGM VSYVLDLQEN YLLRTLKDHG KEESHRGSYI
IDVKKGRMRI RMKVALALGV VVLCIGIGVA VMRFVEKLEW LDSFYLSVMS VTTVGYGDRA
FTSLPGRIFA SIWLLVSTLA VARAFLYLAE ARVDKRNRKM AKWVLGQDMT VSEFLAADID
NNGLVSHSDN NLVELGKETA SEDDRAVLLE GGLTRSASTK FSSPSIKTNI IRFLTMDDSF
LLENRMTLRV MAEFGLYLFY FYVCDRTYIL GESTKNYNRD LFLFLYIILI IVSATTSLKK
NNDKSLFSGK SISYLNRHQT EEWKGWMQAI CVCKQVLFLM YHYFAATEIY NAIRVFIAAY
VWLTGFGNFS YYYVRKDFSV ARFCQMMWRL NFFVALCCIV LNNNYMLYYI CPMHTLFTLM
VYGALGIFNK YNEIKSVMAM KILACFVVVI LIWEIPGTFD IFWGPLSFLL EYTDPAKPDL
PRLHEWHFRS GLDRYIWIIG MIYAYYHPMV EKWMEKLEEM ETKRKLSIKT GIVSVAIFVG
YLWYECIYKL DKVSYNKYHP YTSWIPITVY ICLRNFTQEL RNFSLTLFAW LGKITLETYI
SQFHIWLRSN SPNGQPKWLL SIIPEYPLLN FMLTTAIYVL VSHRLFIMTN TLKSVFIPTN
NNRRLLHNFF AGAAICLCLY CISFILLQIS H
//
