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PENV_PENRW
ID   PENV_PENRW              Reviewed;         832 AA.
AC   B6HTR9;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Vacuolar transmembrane transporter penV {ECO:0000303|PubMed:22777282};
GN   Name=penV {ECO:0000303|PubMed:22777282}; ORFNames=Pc22g22150;
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, AND SUBCELLULAR LOCATION.
RX   PubMed=22777282; DOI=10.1007/s00253-012-4256-0;
RA   Fernandez-Aguado M., Teijeira F., Martin J.F., Ullan R.V.;
RT   "A vacuolar membrane protein affects drastically the biosynthesis of the
RT   ACV tripeptide and the beta-lactam pathway of Penicillium chrysogenum.";
RL   Appl. Microbiol. Biotechnol. 97:795-808(2013).
CC   -!- FUNCTION: Vacuolar transmembrane transporter that participates in the
CC       first stage of the beta-lactam biosynthesis (the formation of the ACV
CC       tripeptide), probably taking part in the supply of amino acids from the
CC       vacuolar lumen to the vacuole-anchored ACV synthetase.
CC       {ECO:0000269|PubMed:22777282}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:22777282};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a drastic reduction in the production of
CC       penicillin and its biosynthetic intermediates delta-(L-alpha-
CC       aminoadipyl-L-cysteinyl-D-valine) and isopenicillin N.
CC       {ECO:0000269|PubMed:22777282}.
CC   -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR   EMBL; AM920437; CAP99503.1; -; Genomic_DNA.
DR   RefSeq; XP_002566110.1; XM_002566064.1.
DR   STRING; 1108849.XP_002566110.1; -.
DR   EnsemblFungi; CAP99503; CAP99503; PCH_Pc22g22150.
DR   GeneID; 8308377; -.
DR   KEGG; pcs:Pc22g22150; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g22150; -.
DR   eggNOG; KOG1134; Eukaryota.
DR   HOGENOM; CLU_002458_0_0_1; -.
DR   OMA; QGIGMFP; -.
DR   OrthoDB; 395194at2759; -.
DR   BioCyc; PCHR:PC22G22150-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005227; F:calcium activated cation channel activity; IEA:InterPro.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR045122; Csc1-like.
DR   InterPro; IPR032880; Csc1_N.
DR   InterPro; IPR027815; PHM7_cyt.
DR   InterPro; IPR003864; RSN1_7TM.
DR   PANTHER; PTHR13018; PTHR13018; 1.
DR   Pfam; PF14703; PHM7_cyt; 1.
DR   Pfam; PF02714; RSN1_7TM; 1.
DR   Pfam; PF13967; RSN1_TM; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..832
FT                   /note="Vacuolar transmembrane transporter penV"
FT                   /id="PRO_0000455150"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        560..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        587..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        623..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        650..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        687..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        713..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          152..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..772
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   832 AA;  94489 MW;  26352879203881BE CRC64;
     MSLTASAASA ALTLLADGPD DGSKRPWRPN DPVKEQRDLY TQFVISTALG LSAFLAFCIL
     RPKWTELYAA RRRQRNAASR LPELPDTLFG WIPVLHQITE EEVLQSAGLD AYVFLSFFKF
     AIRFLLAVFI FAVAIILPMH YKYTGQYGVP GWDNPPGNKT TSPIDGSEKE KPVTDPAYLW
     IYVLFAYVFS GLAIYMLLDE TKVIIRTRQT YLGNQTSTTD RTIRLSGIPH DLGTEDKIKE
     FVEGLRVGKV ESITVCRKWR ELDELIDERM KVIRELERAW TKHIGYKRPK NDGNALPLTE
     QQPRDADDER SGLLSGHDNE HVSGYSNERP KVRIWYGLFK LRFRMIDAID YYEEKLRKID
     EYIQNAREKE YRTTEIAFVT MESIAASQML VQAILDPHPM QMFARLAPAP ADVIWKNTYL
     SRTRRMVQSW SITFVIGFLT VFWSVLLVPI ASLLELKTLE TIVPRLAEFL QEHPIIKSLV
     QTGLPTLAFS LLTVAVPYLY EWLSNNQGMV SRGDVELSVI SKNFFFSFFN LFLLFTVFGT
     ASGFYGFWES LRDAFKDSTT IALALANSLE GLAPFYINLL ILQGLGLFPF RLLEFGSVAL
     YPFQFLSART PREYAELSTP PKFSYGFSIP QTILILVICV VYSVFPSSWL ICLFGLIYFT
     VGKFIYKYQL LYAMDHQQHS TGRAWPMICN RVFVGLLVHQ LAMIGVLALR RAITRSLLLV
     PLLGFTVWFS YWFGRTYEPL MKFIALKSIN RDQPGGGDIS PSPSSTLSPP SGLDRDSLPI
     RIGGQDLELR LKKYVNPSLI VPLHAAWLPG RNPARGNGNG ASAFEVHQTQ NV
 
 
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