ID Q4Q484_LEIMA Unreviewed; 957 AA.
AC Q4Q484;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=LMJF_33_1060 {ECO:0000313|EMBL:CAJ06203.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ06203.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ06203.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ06203.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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; FR796429; CAJ06203.1; -; Genomic_DNA.
DR RefSeq; XP_001685864.1; XM_001685812.2.
DR AlphaFoldDB; Q4Q484; -.
DR STRING; 5664.Q4Q484; -.
DR EnsemblProtists; CAJ06203; CAJ06203; LMJF_33_1060.
DR GeneID; 5654518; -.
DR KEGG; lma:LMJF_33_1060; -.
DR VEuPathDB; TriTrypDB:LmjF.33.1060; -.
DR VEuPathDB; TriTrypDB:LMJFC_330020200; -.
DR VEuPathDB; TriTrypDB:LMJLV39_330018000; -.
DR VEuPathDB; TriTrypDB:LMJSD75_330017800; -.
DR eggNOG; KOG0474; Eukaryota.
DR HOGENOM; CLU_003181_4_1_1; -.
DR InParanoid; Q4Q484; -.
DR OMA; HEPRWFM; -.
DR Proteomes; UP000000542; Chromosome 33.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd01036; ClC_euk; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 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; PTHR11689:SF68; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR11689; CHLORIDE CHANNEL PROTEIN CLC FAMILY MEMBER; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Chloride {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:UP000000542};
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 30..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 243..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 335..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 540..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 569..594
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 606..631
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 692..751
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 798..855
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 412..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 104534 MW; B7935CBF12ADC510 CRC64;
MTRYESVDTY EADSMLYKDH LETRSHEPRW FMWVFVVVLG VVTSALSVGM MTLLHVLNSV
RYELFGFGLR GFTFADAQRY PNVSEASPAH VTGSGGRGTA RTTSSLDVWA MLRGYSVGLY
GIASPRWYWS GYLLWVAFAV CTSAIASGMC YLVPQSVGSG IPEVRAFLNG VSYPMMRSTR
VLVAKTVAVV FTVASGVCTD HYSHLMLAGA MLGSQLLQRR HGIRCYHVHF VDYFRNPRDH
RTVLVIGAAA GIAAAFCVSV GGLLVILELV SAVFPVRFAL YVFAACLLST LSTQMYWSYC
MNFDSPYRLH GGLLLREVVL FRSHLPFGQH AAMNLMAYIP AFVIGLCSGA CAVGFVRLSW
VALYCRRLLE VRLRTKVIRY VLPILFTLVY VSVHYWVAVA FSAESGPGDT MPSAVGADSN
AQRSGSADPL ASSSSSDGAD VGPPAVCRPV PYTVRSGRNV TTIGFYGMNG FLCPAGSYRV
VDAVDIYNAA EHSNRVSSVT KTLPRRQQTV RVVDAYASLA FSYADSTLQT LLSQRTEYLL
PWPALLTFSV IYFFASAVYS GLALCGDIIL PSLVIGAAIG RCIGAAVHSV AVAHSKDAAT
WADPGVFALF GAGSFVSATS GLSFSIGAIL IECTADFRHL LPLMFSIAVA RRVLLRWGRD
VHTVYLEARA VPLLNAEPYL ERYSLLSARH VMHSPVVTLP VVCTLDDVVR TLCSTPHHGF
PVVSINGRTF KGIVTRAQLK LLLWHIIMTD GRTNHCTYDV MQRVEDHVFH SGWEGVDPTQ
LLRRERLPTD QISLYPYVDT SAFTVLDTAA LPRTYEMFTT LGLRHLVVVD RSNCAVGMIT
RKDLVSDNLS AVLESQGAPA PANGVPPSVV LAAALACLRK PFHPTPAQVA EVAQQSSTRN
LDVSSPLRRH HYGQDRESEP SSHAPPPLHS REASFAQVVR RVSLLRVPSP FPPSTGN
//
