CLZ19_COCLU
ID CLZ19_COCLU Reviewed; 526 AA.
AC A0A345BJP9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=MFS-type transporter clz19 {ECO:0000303|PubMed:28605916};
DE AltName: Full=Squalestatin S1 biosynthesis cluster protein clz19 {ECO:0000303|PubMed:28605916};
DE AltName: Full=Zaragozic acid A biosynthesis cluster protein 19 {ECO:0000303|PubMed:28605916};
GN Name=clz19 {ECO:0000303|PubMed:28605916};
OS Cochliobolus lunatus (Filamentous fungus) (Curvularia lunata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX NCBI_TaxID=5503;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 74067;
RX PubMed=28605916; DOI=10.1021/acs.orglett.7b01534;
RA Liu N., Hung Y.S., Gao S.S., Hang L., Zou Y., Chooi Y.H., Tang Y.;
RT "Identification and heterologous production of a benzoyl-primed
RT tricarboxylic acid polyketide intermediate from the zaragozic acid A
RT biosynthetic pathway.";
RL Org. Lett. 19:3560-3563(2017).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid
CC A), a heavily oxidized fungal polyketide that offers potent cholesterol
CC lowering activity by targeting squalene synthase (SS).
CC {ECO:0000305|PubMed:28605916}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {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; MF806533; AXF50662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345BJP9; -.
DR SMR; A0A345BJP9; -.
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 InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..526
FT /note="MFS-type transporter clz19"
FT /id="PRO_0000452629"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 526 AA; 56950 MW; EE2A815EF71F80D2 CRC64;
MNVDTTSPQA PLAGVESKQD GASNEATAKA ESTTHDQNES SSFDERPVHS ALSERQRSAL
LAVASFAAAI SPASTTTYYP AITTLANDLD VSITQINLSL PAYQIFQGLA PTVAAAFSDR
FGRRPVYLVS LSINMAANLG LALQKNYASL MVLRCLQSSS SGGTVALGQA VMDDLITSEE
RGRYMAYLTL GLVMGPALGP LIGGLLSQYL GWRAIFWFLM ILGGFFFLMV LTFFRETNRS
IVGDGSVPPQ KWNRSLVQIF RKDKLIANPE SLAKKRISVN PLASIQILRN KENFIVCMYG
ALLFGGYASV ISIFATQLEE RYGYSQVQVG LCYLPFGVGS ILSRWTAGKM IDWNFKREAD
KQGFKIVKNR QQDLSRYDIE KARLTVSFPM IFATCGFVVA YGWLMQYDTH VASVLVVVFL
IANVFTGVLI ANSALLNDLN PGNGAALGAA MNLTRCLMGA GGVAAVTPLI NKIGIGYTAT
ATAGVWVVTL PALYLVYSKG YTWRKAALEA SSQDRRENPD VASGSP