ID A0A0A2JSP2_PENEN Unreviewed; 591 AA.
AC A0A0A2JSP2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE SubName: Full=Sulfate transporter {ECO:0000313|EMBL:KGO58467.1};
GN ORFNames=PEX2_069770 {ECO:0000313|EMBL:KGO58467.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO58467.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO58467.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO58467.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362052}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362052}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|RuleBase:RU362052}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362052}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO58467.1}.
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DR EMBL; JQFZ01000121; KGO58467.1; -; Genomic_DNA.
DR RefSeq; XP_016599961.1; XM_016744248.1.
DR AlphaFoldDB; A0A0A2JSP2; -.
DR STRING; 27334.A0A0A2JSP2; -.
DR GeneID; 27679668; -.
DR HOGENOM; CLU_003182_10_2_1; -.
DR OrthoDB; 6913at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0098661; P:inorganic anion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
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; SULFATE TRANSPORTER; 1.
DR PANTHER; PTHR11814:SF263; SULFATE TRANSPORTER YPR003C-RELATED; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 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|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362052};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362052}; Transport {ECO:0000256|RuleBase:RU362052}.
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 299..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 394..425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 452..582
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 591 AA; 64129 MW; 4BA2B725BA957F64 CRC64;
MAALTVASIY IPMALSLASN LAHAPPISGL YSFVIHPLVY AILGSCPLLV VGPEAAGSLL
TGAIVKASVM QGNSGEDDPT ETALIVGVAT ALSGGMILIA GLTRLGFLDN VLSRPFLRGF
ITAIGFVIFV DQLVPELGLA EYAKETGVSH GTSVEKLIFI FRYARECHGL TAIVSIVSFS
VIIMFRTLKK MLVPRIPQVI YFPDRFLVVA LSAVLAWHLD WESKGLEILG HTEVASGGLF
AFNWPFQPAN MKHVRTALSK SFIIALLGFF ESSVAAKGLG EGSSEGIKGM HMSANREMVA
LGVANVIGGC FSALPAFGGY GRSKLSSQTG ARSPMTSVFV SIITFICVLV LLPYLYYLPK
AVLCSMISVV AFTLVEECPH DLLFFFRLRG WSELVLMFLI FTTTIFYSLE LGMAMGMGLS
VIILIRHATA PRIQIMGKVL GTDARFDNAE LHPENVELVE GALIVKIPEP LTFANTGDLK
NRLRRLELYG STHAHPSLPR MRAPEHNKNI IFDVHGVTSI DGSGTQVLSE IVHAYAEQRV
RVFFCRLPNS SVFRMFERSG IVESCGGLTH FVPSVDEALR LAESENQTQE I
//