CNSL_PENEN
ID CNSL_PENEN Reviewed; 482 AA.
AC A0A0A2K5R6;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=MFS-type transporter cnsL {ECO:0000303|PubMed:25571861};
DE AltName: Full=Communesin biosynthesis cluster protein L {ECO:0000303|PubMed:25571861};
GN Name=cnsL {ECO:0000303|PubMed:25571861}; ORFNames=PEX2_055460;
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8;
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).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=25571861; DOI=10.1002/anie.201411297;
RA Lin H.C., Chiou G., Chooi Y.H., McMahon T.C., Xu W., Garg N.K., Tang Y.;
RT "Elucidation of the concise biosynthetic pathway of the communesin indole
RT alkaloids.";
RL Angew. Chem. Int. Ed. 54:3004-3007(2015).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of communesins, a prominent class of indole alkaloids
CC with great potential as pharmaceuticals (PubMed:25571861). With the MFS
CC transporter cnsO, is most likely responsible for cummunesins secretion
CC and thereby may contribute to intrinsic resistance (Probable).
CC {ECO:0000269|PubMed:25571861, ECO:0000305|PubMed:25571861}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC permease family. {ECO:0000255}.
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DR EMBL; JQFZ01000090; KGO59705.1; -; Genomic_DNA.
DR RefSeq; XP_016600818.1; XM_016742820.1.
DR AlphaFoldDB; A0A0A2K5R6; -.
DR EnsemblFungi; KGO59705; KGO59705; PEX2_055460.
DR GeneID; 27678239; -.
DR HOGENOM; CLU_001265_0_5_1; -.
DR OrthoDB; 619250at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 3.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..482
FT /note="MFS-type transporter cnsL"
FT /id="PRO_0000446467"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 482 AA; 53180 MW; EB6A3AA5F39951C1 CRC64;
MAADQVTISD EPKGGGVTAD AAVKAIKAGR NKDVDIAAQI VSDYADQMDG DTWSVEEERK
LIRRIDWRLI PTLFVCATLS GLDKTAISAA AVYNIKTDLN LTGAEYSWIG SAPFFGGLLF
MGPLAYCLQR VPAVPFFAFN VLCWGILEMS VTMVVSMWYR PEEQPKRNSI ILNVVAPIIN
GFVAWVVGYY KGPYERWKII FLLVGALTIV TSVVVYFVLP NNPLEAKFLT PREKYIVIQR
KAADNTGIES KTFKMEQVWE AIFDIKTWLI WIAIAALQVP NGGLTTFNTL IISGLGFDSL
QTSLLAMPPG AMSTLSGIGL SYLAATTRRY RTAIVTVSIL LPLFGAVLCY ALPRTNLAGQ
LVGLYILYTY WAPYVTLVSV YQANVAGHTK KITLYAWFYI AWATGNIIGP QTFRADQAPE
YTGGTVAMII CYVVAMFAIT AYGVVCHLSN KKRAEAIEAR TAADHDWLDM TDKENVGFKY
TT