ID E9AZY8_LEIMU Unreviewed; 1984 AA.
AC E9AZY8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Sulfate transporter-like protein {ECO:0000313|EMBL:CBZ28539.1};
GN ORFNames=LMXM_28_1690 {ECO:0000313|EMBL:CBZ28539.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ28539.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
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}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|ARBA:ARBA00008692}.
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; FR799581; CBZ28539.1; -; Genomic_DNA.
DR RefSeq; XP_003877010.1; XM_003876961.1.
DR GeneID; 13450713; -.
DR KEGG; lmi:LMXM_28_1690; -.
DR VEuPathDB; TriTrypDB:LmxM.28.1690; -.
DR OMA; PQEREFR; -.
DR OrthoDB; 2880581at2759; -.
DR PhylomeDB; E9AZY8; -.
DR Proteomes; UP000007259; Chromosome 28.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814:SF55; SODIUM-INDEPENDENT SULFATE ANION TRANSPORTER; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 438..532
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 637..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1984 AA; 215863 MW; EED1E0DBCBB922B8 CRC64;
MKYVYRFVPV SRWYRLLTPK IILSDGIAGF IVGVMIVPTC LSWSSLAGLP FSCGLIAALV
ASFSYGTFGQ CASLSIGPVA EITTLLISIP GIPVAERKDT FQSLGVQVGI LSMVLSFVDC
GTVIKTIFAK AVGDGYTCAA ALLAISAQLK VMFNVVPEDK GYGNFINTLI TLASQMSAKN
VYCFMIFMVY CTYLIQIKKA GLPLWIPHQL IVVVASTFVT WGLRLDQVLD LAIVRDIPAV
LSWPRFPPMN NLIGLGPYTL TITVIIFVQM YVVAQRVMPN IDPNTELFAG GITNLLVNLM
SGMPVSNSFS CSSVLIEQKV HTPLTAYATG AVVLITILFL TRLGVFYYLP KQALAAIVVS
SVWRLVNFSG PAQLWHYSRK DAGVWVLTFL LTLIGGITIG VLSGIAFSLI LVVLRIARPR
AVSVGFNMQT FRYGDIRKDP ELLVYPNILM WRFDAPLYFI NIGYFQERLI AAIAAEVRPI
DVVIVTCGKV VDIDAAALAS LPFILDYTAK SDPTRPRRII LTDIHGRLEK VLLASAALPI
YVPEEYDRIS IEQITASGKF PVVFRRLEEA IAFGQRCISE RYGNVDTAPY PNVSFLTDVV
METARLPTGD GCVPSFLSLL EAENASPTVA GGTAAAAAAP LTPNTPQIVV TSPDETSPRP
SRAEGGRGKA ARTEASIFSS QLPHNSPTTS VDLSGPNVDD DGDDGDDEDP PQQQQQDSLV
RHLATLKKLS TYSPDRELVG VLGVIRHGEV TPKQKKKLLF NDPTLLQLAF QGRDVRRTKR
SVDELTEFFA VVERLLLETP ASNMSSPGSA DMLDASFLGT TSPFTGRISA STAESWARVL
SIVRSHPDGL KIQVKARMTS TSGTVSFTES ERTSPQRYVH YGGSARWKVG GSVPSRHSSG
SGSADDDSGE PTVGLLVVKW GGVLTKSGIL QAHVMGEKLF ARFYAAGDLP LRRLVQFTRH
PLVTASDENR VVNTALVVAN ALTQTSGATL HRCDIVLNDG LTKTLGPVAK RLLQEEYRCF
ESLLHIESAA AARHFFHIPG FRQLLSIPPR DRLGLWVGSE HDDSDGSDNG ATHMFSQTVS
KNSENDRAPG LHGCPPPSSC RSRKRTACEG DPRSTQFNGA QDVTHGSRAF SILEQQQQQQ
QQQSYNCRRQ DEFYTPYQVL QELEELMTIL STLEFPVYLA KVPLSNYETL QELQRRYEAM
LKNFKGAKRR IRSGYKHSVH MMSSGDPKIP ASPGARTLRP AEPSGFDEDT EQQMLLEAME
ETGGSSDEDG FDAQLVGDTE LDPDLPPRRD PSAAGGTLAT AGPSHLTMPA LSGGRAGEPQ
HGRGNHSRCP APAQQRTRNG SGNGGHTQPR LLHTGSGPFH PLSGHDCGRG HYSRGLPGAA
PCFDVSDVSK LRDYGSYDVT YNLPLVLQLH ASMQEPVAAF QLRRFARALQ RFSEITEYLS
RIGENVLVGI NSSKRFIIGS LVSDGLLRRL HNDFQDLAMT DEERGVQELL LKAQAQYMAE
NGGVEQDVRH MIGLCSRLPC WRKKKRRADE HGGSAWRNDV WARETPQERE FRLRVPFISL
PKQEACTRAA AADFEGCTRL YFTSYLHVEG VLQCLFESAT VEGFSRPSKE EMEATHQLYM
RHLIFKIFRR RNVSYTDAEV ATAMRRLHLL FRSDVDYDQQ QRELRLGLAA IYHAMYYVSM
EVYLSLGDAD EAHAAILEDF PLFNLGRAGD GDEDGDTPSA ADTAANTAAG GGDSEEGEEL
VETMAAAGAP SAAGGGMGRT AAVPSSPLML SFAPSGGTSC VSSDPASYLT AAGGRNAAAF
SAASGGRSAE GFAVFARSPS HVQHLVPVPN DPDATATLVA DGAGSARLAT SPLSLSDAPE
RAVAGSGVES DSGEDKARSH VHRRVTNMST LALAPPPQRE PKLRSRSMTA VPANTQDLAK
EATVLMTPEA GRRTAMVQEM KHRVSNVTPM RRIHEGLNLN DFVLLMKEVE SAVRSQTASS
SSPH
//