ID F2SLG4_TRIRC Unreviewed; 851 AA.
AC F2SLG4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=TERG_03694 {ECO:0000313|EMBL:EGD87443.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD87443.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361221}.
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DR EMBL; GG700650; EGD87443.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SLG4; -.
DR STRING; 559305.F2SLG4; -.
DR VEuPathDB; FungiDB:TERG_03694; -.
DR eggNOG; KOG0475; Eukaryota.
DR HOGENOM; CLU_003181_2_2_1; -.
DR InParanoid; F2SLG4; -.
DR OMA; CLDWTPW; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000008864; 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; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03684; ClC_3_like; 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; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 1.
DR Pfam; PF00571; CBS; 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; 2.
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:UP000008864};
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 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 234..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 336..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 446..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 505..526
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 532..554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 598..621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 664..726
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 755..812
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 93031 MW; 91E43A95538FB5C7 CRC64;
MADTINTDQP DDGLSQSFSQ GQESSEEPIT FKRRQKPPSR FGLHSIFGSA NDSPFSYHSR
LRSIDESPRG SRPGTANQNT REPGNGSGAS HKPGAPTDWY IEGPGRRVGY DDLTAIDWIF
EYTKERQRIR HLNANNPGLL GTFRQLLDVS QVWMVLVMTG LAVGLLAGCI DITSRWLADI
KVGYCKSGVE GGKFYLNRSF CCWGYDDPAN CKHWISWHDA FKISSKAGAF VAEYMVFIMY
SILFATCAAV LVTSYATHAK HSGIPEIKTI LGGFVIKKFM GLWTLMIKSV GLCLSVASGM
WLGKEGPLVH VACCCANVIM KPFGSLNHNE ARKREVLSAA AAAGISVAFG SPIGGVLFSL
EQLSYYFPDK TMWQSFVCAM AAAISLRAVN PFRTGNIVLY QVTDSQRWHP IEILLFILLG
IFGGLYGGLF IKLNMQISKW RKSRNFSFPV LEVLFVALIT GLINFPNSFM KAQLSDLLQA
LFAECSKTPA DEFGLCKGNS DFTGVFWALV FAGTLGFLLA SITFGLDIPA GVILPSLAIG
ALYGRALGTM VSVWQKSHPN SLLFSDCEPG APCVTPGTYA IVGAAAALGG ATRMTVSIVV
IMFELTGALT HVIPIMIAVM LSKWCGDIFG KRGIYESWIH LNEYPFLDQK DDTPPPDVPV
SQVMTSINDL TVITAVGHTV ESLRNLLSST SYRGFPVVSD MANPTLLGYI SRNELSYALN
VSSRHSGSLS PETQTFFSHQ PFADPAETLD LRPWMDQTPI TMNIHTNLLI VLNMFQRLGL
RYVLIVNRGR LEGFLTKKDI WYILNESSKA DPTSGIGGGM LRADGSGEAR GLLSRADNPM
LVSPVDDGNM L
//
