ASTH_ASPOR
ID ASTH_ASPOR Reviewed; 564 AA.
AC Q2UEK9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=MFS-type transporter astH {ECO:0000303|PubMed:27628599};
DE AltName: Full=Astellolide biosynthesis cluster protein H {ECO:0000303|PubMed:27628599};
GN Name=astH {ECO:0000303|PubMed:27628599}; ORFNames=AO090026000577;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27628599; DOI=10.1038/srep32865;
RA Shinohara Y., Takahashi S., Osada H., Koyama Y.;
RT "Identification of a novel sesquiterpene biosynthetic machinery involved in
RT astellolide biosynthesis.";
RL Sci. Rep. 6:32865-32865(2016).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of astellolides, drimane-type sesquiterpene esters
CC that show antimicrobial, anti-inflammatory, and anti-tumor activities
CC (PubMed:27628599). Seems not to be involved in astellolides
CC translocation (PubMed:27628599). {ECO:0000269|PubMed:27628599}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is regulated by the secondary metabolite
CC regulator cclA. {ECO:0000269|PubMed:27628599}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of astellolides.
CC {ECO:0000269|PubMed:27628599}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {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; AP007159; BAE60006.1; -; Genomic_DNA.
DR RefSeq; XP_001822008.1; XM_001821956.1.
DR AlphaFoldDB; Q2UEK9; -.
DR SMR; Q2UEK9; -.
DR EnsemblFungi; BAE60006; BAE60006; AO090026000577.
DR GeneID; 5994036; -.
DR KEGG; aor:AO090026000577; -.
DR VEuPathDB; FungiDB:AO090026000577; -.
DR HOGENOM; CLU_000960_22_1_1; -.
DR OMA; WAINSYT; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..564
FT /note="MFS-type transporter astH"
FT /id="PRO_0000450122"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 26..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 564 AA; 60176 MW; 25404F8877464FB2 CRC64;
MTDISTGVQL KPGIGDGTVY NGNMSKDTLV NCSPDPENPE KGQASSPRTQ ISVDDNEEST
TEYPSSWKLA MIMISLCLAV FCLALDTTIM ATAIPKIADQ FNSLNDVGWY GSAYLLTTSA
LTLSFGKLYS FYSIKWVYLQ ALGMFEIGSL ICGATPNSLG LIIGRAIAGS GSAGIYSGSM
LIVARSAPLE RRPLLTGILG GLFGVASVVG PLIGGAFTDN LSWRWCFYIN LPLGAVTGLF
LILFFDGAKA TTQRATIRDQ LSQLDLLGSL CFLPAIICVL LALQWGGTTY PWHDGRIIAL
FTVFGVLLLA FAGVQWWRQE KATVPPRLIA NRNVWGAALF SFCLNASFII FTYYLPMWFQ
SIKGVTATQS GIMNLPMVLA VVIFSIISGG LVGALGYYTP FMVIAPLIAA IGAGLLSTLR
MDSNNASWIG YQILYGVGVG CGLQQPIVAV QGSLAPADLP TGTVIVMFMQ TIGGAIFMSV
GQNVFQNQLM RNLATQAPSV DAARVLQAGA TMLRKTVSSD LLPAALRAYN SAITEAFYVA
VAMAVLALPG ALVMQWISVK GRQL
