SSU1_ARTOC
ID SSU1_ARTOC Reviewed; 375 AA.
AC C5G0E3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Sulfite efflux pump SSU1;
GN Name=SSU1; ORFNames=MCYG_08415;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
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 -!- FUNCTION: Sulphite efflux pump required for the secretion of sulphite
CC as a reducing agent. In the presence of sulphite, cystine in keratin is
CC directly cleaved to cysteine and S-sulphocysteine, and thereby, reduced
CC proteins become accessible to hydrolysis by a variety of secreted
CC endo- and exoproteases. Excretion of sulphite mediated by an efflux
CC pump represents also an detoxification pathway for dermatophytes during
CC infection of the epidermal stratum corneum, hair and nails, which are
CC rich in cysteine (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC transporter (TDT) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEQ35596.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995708; EEQ35596.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002843332.1; XM_002843286.1.
DR AlphaFoldDB; C5G0E3; -.
DR SMR; C5G0E3; -.
DR STRING; 63405.XP_002843332.1; -.
DR EnsemblFungi; EEQ35596; EEQ35596; MCYG_08415.
DR GeneID; 9227334; -.
DR eggNOG; ENOG502QT02; Eukaryota.
DR HOGENOM; CLU_030057_6_3_1; -.
DR OrthoDB; 819178at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.50.10.150; -; 1.
DR InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
DR InterPro; IPR038665; Voltage-dep_anion_channel_sf.
DR Pfam; PF03595; SLAC1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..375
FT /note="Sulfite efflux pump SSU1"
FT /id="PRO_0000384414"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 375 AA; 41759 MW; AC6244EA55236D42 CRC64;
MPSGSGFQNI EEAGEKARRR DDWIAISNFH PGWFSVNMGT GITAILLQNL PYQFPGLHYI
AVVLFVLNVI IFFFFLTISI TRYALWPEKF KAMLAHPAHS MLLGTFPMGF ATIINCIIFI
CVPVWGDWAA RFAWGLWWVD ATVSIAICYF VPFMLMTKHT SSLETMTAAW LLPIVAPVVA
AASGGVVADA LKNDTHALIT ILVCYVMWGS AVPLAMVILV IYFQRLALHK LVPRAAIVSA
LLPIGPLGQG GFGLMQLGVV ARRVFPRLDF LAPIAGEIFY VMGAFIAMIM WGFGLIWLWF
ALASFTRGKF YFNIGWWAFT FPLGVFTTAT TQMGKEFNSV VFDVLGTFFS IVVAAMWVMV
FALTVYKSCT KELFK
