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Database: UniProt
Entry: A0A1B9I3S8_9TREE
LinkDB: A0A1B9I3S8_9TREE
Original site: A0A1B9I3S8_9TREE 
ID   A0A1B9I3S8_9TREE        Unreviewed;      1188 AA.
AC   A0A1B9I3S8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN   ORFNames=I206_03501 {ECO:0000313|EMBL:OCF50182.1};
OS   Kwoniella pini CBS 10737.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296096 {ECO:0000313|EMBL:OCF50182.1, ECO:0000313|Proteomes:UP000094020};
RN   [1] {ECO:0000313|EMBL:OCF50182.1, ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|EMBL:OCF50182.1,
RC   ECO:0000313|Proteomes:UP000094020};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus pinus CBS10737.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|Proteomes:UP000094020};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC       {ECO:0000256|RuleBase:RU361221}.
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DR   EMBL; KI894010; OCF50182.1; -; Genomic_DNA.
DR   RefSeq; XP_019011401.1; XM_019155247.1.
DR   AlphaFoldDB; A0A1B9I3S8; -.
DR   STRING; 1296096.A0A1B9I3S8; -.
DR   GeneID; 30171870; -.
DR   OrthoDB; 150430at2759; -.
DR   Proteomes; UP000094020; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03684; ClC_3_like; 1.
DR   Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR   InterPro; IPR000644; CBS_dom.
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.
DR   PROSITE; PS51371; CBS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU361221};
KW   Ion transport {ECO:0000256|RuleBase:RU361221};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094020};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361221};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361221}; Transport {ECO:0000256|RuleBase:RU361221}.
FT   TRANSMEM        424..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        517..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        691..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        726..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        765..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        806..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        861..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        888..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        928..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        953..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   DOMAIN          1130..1188
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          1..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1188 AA;  129831 MW;  689BAA170672C6E5 CRC64;
     MSQSREEEEQ RMSTSASTTH STHTIKPPRP PSIASLRHNR FYGSSSSSSA GAGPSSRSSH
     SHSRRQSLDI AETQPPSPIT YFPNPSTFQS NSASYPQPPI SSTSNSISTS PKNSTFSMSN
     SVVSLPEESE FEGPTPKMSL VNLDSAASSP RMTRGGGNSQ LEQRRRSSVA PSTSQGMRQF
     STPVNGYGST HTSNSNLGLG LGRTPSLSTL NNPNQDATLS SPRRISTSRV PPGPSTNRFT
     VTPPQGLLNL PTHEAYYSAS QPGTATTSRF RDKDLHQSHP LPHSAIPYSN QLATQMTSNS
     NSHRRHLSVN SIIHSPLFPG RHSLPHSPTG SVMRKIKRTA STIGMGFGRP DHYDDDASRG
     KGGEDEMLED DEGERANGTR VWYSSYVTID WIHDAIKDSS RVRRLRHAAH RSIRGKLANS
     WDRIQGWLVV TIVGVLSAVI AFFIIRTEMA LFDLKEGFCG SSWGTAKRFC CAPHHPSGRG
     DAGDEENCGD WVEWGEFFAP HQRGGPEGQW IWGGPEFIAY AVVALCLATL ASFLTVYLTS
     AAHHTTSKDS TFLTTPTEHN DNKSKQPKQI PTMNNGENSN ERQPLLEGIA NEPITPITEA
     FPPTEPPRKI MYYAAGSGIP EIKTILSGFV IHGYLGGWTL ITKSVGLALS VASGLSLGKE
     GPLVHISSCV GNIVSRLFLK FECNEAKRRE ILSAACAAGV AVAFGAPVGG VLFSLEEVSY
     YFPPKVMWRS FWCAAVAAIT LKSLNPFGNG SLVLFNVTYT KEYHYWEYVI FVFLGVFGGL
     YGAIFARLNI IWSRQVRGGT WLKKHPIFEV ALVTILTTVI SFLNPYTRMG GTELVASLFE
     ECQPSSSSSF CVNHPHEIAP VIWTIGTALL IKGALTIITF GIKLPAGIFI PSLVVGACFG
     RIVGLTMEYI EYSYPTLGIF DVCKETDCIV PGLYAMVGAA ATLAGVTRTT VSLAVIMFEL
     TSTLNYVVPV MLGVLIAKTV ADGLEKKGIY DLVIDLNQLP YLDQKHEYLW GSRRASSVAD
     KSVPILRADK QHTVRSLTGK LLESVRLGMT DTGFPILVKE RSCLRVIGFL GMNELEHALS
     ELSDEPDATL NLMPDDATSH RRRSSAMSIF SFADSYADGQ WSPYDLSRYI DRAPITVQIH
     SPLELVQQLF VKLGARQIIV TNSRGVFQGM VTKKNWLNFL GELEEDGH
//
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