ID   A3LTB3_PICST            Unreviewed;       818 AA.
AC   A3LTB3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 83.
DE   SubName: Full=Chloride channel, possibly voltage gated {ECO:0000313|EMBL:ABN66376.2};
GN   Name=GEF2 {ECO:0000313|EMBL:ABN66376.2};
GN   ORFNames=PICST_83582 {ECO:0000313|EMBL:ABN66376.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66376.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN66376.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000498; ABN66376.2; -; Genomic_DNA.
DR   RefSeq; XP_001384405.2; XM_001384368.1.
DR   AlphaFoldDB; A3LTB3; -.
DR   GeneID; 4838406; -.
DR   KEGG; pic:PICST_83582; -.
DR   eggNOG; KOG0475; Eukaryota.
DR   HOGENOM; CLU_003181_2_2_1; -.
DR   InParanoid; A3LTB3; -.
DR   OMA; SCCILNI; -.
DR   OrthoDB; 150430at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR   CDD; cd03684; ClC_3_like; 1.
DR   Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR   PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 1.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF81340; Clc chloride channel; 1.
PE   4: Predicted;
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        69..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        465..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   818 AA;  90612 MW;  B4B0BD1ED3063769 CRC64;
     MDLFAAGRGA NVSYTDEDIP TLSYNNSDSL EHNIVISTTA KYYENNTYID WSRESLIVPS
     TSSFTSRKWF TLIVSSIIVG YTAAFIDLSS VWLNDLRKGV CFSKVDTWSL LNPYSTCPAG
     KWHDWSVILF NAKGSVSNWL VNFPIYTLFA FCWITLAAYI TIHKDPLIKQ SGIPEIKLII
     SGFNYRINYY LGLQTLFYKT VGLILVVSSG LWLGKEGPLV HVSCCILNIL YGLLVNTSFE
     NEAVRRELLS AATATGIAVA FSSPIGGVLF VLESMATFFT PTKIMWNSFI TASVAVIFLT
     GFRVFTDGSN FQEKDLFSVE FGNFSWLFLE IIPFITLGAL GGIYGYLFIT VNSYFDKSGV
     RHVIQNRLLS LVGASGVKAG QYLEVFAVLL VTSILTFPID ETKLQLNTFL TNLFTACPTD
     TDTSEAITFI CSSSNGITIL KLSYILIQGF ILSTYSFGVN LPGGILMPSL VLGATSGRLL
     GLITQAIQTK FLSSEFLATC TESSCIVSPA SYAVIGAAAF MTGVTKLTMC VVVIMFELTG
     AVSYVLPIML AVMISKFVND VLCTSNIYDT FLKNNFNQSE QNTYGYPNEG KGAGLVNFTS
     LTSTVKDKLP DITVKSIMVP LNRTKCLCLV PETHYTVNSL IEFTNGDTHE GYPLILKYGN
     PLYLGYVNKH ELFSKISNID DRNAVISFQV DGLSRVAISQ QLHYERSIGS VLQQIDIPVE
     RSMIIFNELT SAVLVLETFE KMHVNYFVIL DSNNRNGQTM AGFVDRFVIA HLIDSQFKDL
     EDELVGVEAA SEFDIENNLE DETLLDARRK RLSIELIT
//