PENM_PENRW
ID PENM_PENRW Reviewed; 508 AA.
AC B6HN82;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=MFS-type transporter penM {ECO:0000303|PubMed:24480587};
GN Name=penM {ECO:0000303|PubMed:24480587}; ORFNames=Pc21g09220;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=24480587; DOI=10.1016/j.ymben.2014.01.004;
RA Fernandez-Aguado M., Martin J.F., Rodriguez-Castro R., Garcia-Estrada C.,
RA Albillos S.M., Teijeira F., Ullan R.V.;
RT "New insights into the isopenicillin N transport in Penicillium
RT chrysogenum.";
RL Metab. Eng. 22:89-103(2014).
CC -!- FUNCTION: MFS-type transporter involved in penicillin production, most
CC likely through the translocation of isopenicillin N from the cytosol to
CC the peroxisomal lumen across the peroxisomal membrane.
CC {ECO:0000269|PubMed:24480587}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:24480587}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Probably recruited to the peroxisomal membrane by
CC pex19. {ECO:0000305|PubMed:24480587}.
CC -!- DOMAIN: The peroxisomal targeting signal allows recruitment to the
CC peroxisomal membrane by pex19. {ECO:0000305|PubMed:24480587}.
CC -!- DISRUPTION PHENOTYPE: Leads to a decrease in benzylpenicillin
CC production. {ECO:0000269|PubMed:24480587}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AM920436; CAP95819.1; -; Genomic_DNA.
DR RefSeq; XP_002567961.1; XM_002567915.1.
DR TCDB; 2.A.1.2.86; the major facilitator superfamily (mfs).
DR EnsemblFungi; CAP95819; CAP95819; PCH_Pc21g09220.
DR GeneID; 8304087; -.
DR KEGG; pcs:Pc21g09220; -.
DR VEuPathDB; FungiDB:PCH_Pc21g09220; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_1_1_1; -.
DR OMA; YVIWTIA; -.
DR OrthoDB; 1146947at2759; -.
DR BioCyc; PCHR:PC21G09220-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Glycoprotein; Membrane; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="MFS-type transporter penM"
FT /id="PRO_0000455151"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
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 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..307
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000305|PubMed:24480587"
FT COMPBIAS 32..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 508 AA; 55202 MW; DA23E3D85E639A6B CRC64;
MKDGEETPSV DGSTSASNRE KLGTDLEIGP VDLSDGGKEE KVKDPNLVDW DGPDDPENPL
NWTSKRKITA TCSIALITFL TPLGSSMFAP GVGQLVKDFN VTSTELSSFV VSVYLLGYCF
GPLIIAPLSE LYGRQYVYHV CNILYVIWTI ACAFAPEIGS LVVFRFFAGL AGSCPLTIGA
GSIADMFVQE QRGGAMAAWA LGPLIGPVVG PVAGAYLAQA KGWRWSFYVL AMAAGAITIS
SLFSIRESYA PTLLARKTKK LQKETGNMNL RSALDTGRTP KELFLYSIVR PTKMLFRSPI
VFLLSLYVGV IYGYLYLLFT TITSVFQQQY NFSQGAVGLT YLGLGVGSLI GLFLIGATSD
RLLNYLAAKN GEKKPEYRLP PMVPGAIFVP ISLFMYGWTA YYQTHWIVPI IGTSFLGTGM
MITFMCVSTY LVDAFTNYAA SVMAANTVFR SLAGALLPLA GPKMYAVLGL GWGNSLLGFI
ALAFCALPVI FWIYGERIRT SPKFQVTF
