VEA_PENRW
ID VEA_PENRW Reviewed; 561 AA.
AC B6H3B2;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Developmental and secondary metabolism regulator veA {ECO:0000305};
DE AltName: Full=Velvet complex subunit A {ECO:0000305};
GN Name=velA {ECO:0000303|PubMed:20543063}; ORFNames=PCH_Pc13g13200;
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, INTERACTION WITH LAEA; VELB AND KAPA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20543063; DOI=10.1128/ec.00077-10;
RA Hoff B., Kamerewerd J., Sigl C., Mitterbauer R., Zadra I., Kuernsteiner H.,
RA Kueck U.;
RT "Two components of a velvet-like complex control hyphal morphogenesis,
RT conidiophore development, and penicillin biosynthesis in Penicillium
RT chrysogenum.";
RL Eukaryot. Cell 9:1236-1250(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21816879; DOI=10.1099/mic.0.051896-0;
RA Kamerewerd J., Zadra I., Kuernsteiner H., Kueck U.;
RT "PcchiB1, encoding a class V chitinase, is affected by PcVelA and PcLaeA,
RT and is responsible for cell wall integrity in Penicillium chrysogenum.";
RL Microbiology 157:3036-3048(2011).
RN [4]
RP FUNCTION.
RX PubMed=22439693; DOI=10.1089/omi.2011.0153;
RA Veiga T., Nijland J.G., Driessen A.J., Bovenberg R.A., Touw H.,
RA van den Berg M.A., Pronk J.T., Daran J.M.;
RT "Impact of velvet complex on transcriptome and penicillin G production in
RT glucose-limited chemostat cultures of a beta-lactam high-producing
RT Penicillium chrysogenum strain.";
RL OMICS 16:320-333(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP VOSA AND VELC.
RX PubMed=23264641; DOI=10.1128/ec.00272-12;
RA Kopke K., Hoff B., Bloemendal S., Katschorowski A., Kamerewerd J.,
RA Kueck U.;
RT "Members of the Penicillium chrysogenum velvet complex play functionally
RT opposing roles in the regulation of penicillin biosynthesis and
RT conidiation.";
RL Eukaryot. Cell 12:299-310(2013).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25557366; DOI=10.1002/jobm.201400588;
RA Wolfers S., Kamerewerd J., Nowrousian M., Sigl C., Zadra I.,
RA Kuernsteiner H., Kueck U., Bloemendal S.;
RT "Microarray hybridization analysis of light-dependent gene expression in
RT Penicillium chrysogenum identifies bZIP transcription factor PcAtfA.";
RL J. Basic Microbiol. 55:480-489(2015).
CC -!- FUNCTION: Component of the velvet transcription factor complex that
CC controls sexual/asexual developmental ratio in response to light,
CC promoting sexual development in the darkness while stimulating asexual
CC sporulation under illumination (PubMed:20543063). The velvet complex
CC acts as a global regulator for secondary metabolite gene expression
CC (PubMed:22439693). Controls the expression of the penicillin gene
CC cluster (PubMed:20543063, PubMed:22439693). Positively controls the
CC expression of the class V chitinase chiB1 (PubMed:21816879). Positively
CC controls the expression of the transcription factor atfA
CC (PubMed:25557366). Required for cell wall integrity and controls hyphal
CC branching (PubMed:20543063). {ECO:0000269|PubMed:20543063,
CC ECO:0000269|PubMed:21816879, ECO:0000269|PubMed:22439693,
CC ECO:0000269|PubMed:25557366}.
CC -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC laeA, veA and velB; velA acting as a bridging protein between laeA and
CC velB (PubMed:20543063). Interacts with kapA (PubMed:20543063).
CC Interacts with vosA and velc (PubMed:23264641).
CC {ECO:0000269|PubMed:20543063, ECO:0000269|PubMed:23264641}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20543063,
CC ECO:0000269|PubMed:23264641}. Cytoplasm {ECO:0000250|UniProtKB:C8VTV4}.
CC Note=Enriched in the nucleus in the dark (By similarity).
CC {ECO:0000250|UniProtKB:C8VTV4}.
CC -!- DOMAIN: The C-terminal PEST domain is a region rich in proline,
CC glutamic acid, serine and threonine residues that is required for the
CC light-dependent regulation of development and secondary metabolism (By
CC similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC -!- DISRUPTION PHENOTYPE: Substantially down-regulates penicillin
CC biosynthesis genes pcbAB, pcbC, and penDE (PubMed:20543063). Up-
CC regulates expression of laeA (PubMed:20543063). Leads to light-
CC independent conidial formation, dichotomous branching of hyphae, and
CC pellet formation in shaking cultures (PubMed:20543063). Decreases the
CC expression of the class V chitinase chiB1 (PubMed:21816879). Decreases
CC the expression of the transcription factor atfA (PubMed:25557366).
CC {ECO:0000269|PubMed:20543063, ECO:0000269|PubMed:21816879,
CC ECO:0000269|PubMed:25557366}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; AM920428; CAP92389.1; -; Genomic_DNA.
DR RefSeq; XP_002559734.1; XM_002559688.1.
DR AlphaFoldDB; B6H3B2; -.
DR SMR; B6H3B2; -.
DR STRING; 1108849.XP_002559734.1; -.
DR PRIDE; B6H3B2; -.
DR EnsemblFungi; CAP92389; CAP92389; PCH_Pc13g13200.
DR GeneID; 8311426; -.
DR KEGG; pcs:Pc13g13200; -.
DR VEuPathDB; FungiDB:PCH_Pc13g13200; -.
DR eggNOG; ENOG502QVY9; Eukaryota.
DR HOGENOM; CLU_022491_2_0_1; -.
DR OMA; NFFLYAT; -.
DR OrthoDB; 1171722at2759; -.
DR BioCyc; PCHR:PC13G13200-MON; -.
DR Proteomes; UP000000724; Contig Pc00c13.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.3960; -; 1.
DR InterPro; IPR021740; Velvet.
DR InterPro; IPR037525; Velvet_dom.
DR InterPro; IPR038491; Velvet_dom_sf.
DR PANTHER; PTHR33572; PTHR33572; 1.
DR Pfam; PF11754; Velvet; 2.
DR PROSITE; PS51821; VELVET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..561
FT /note="Developmental and secondary metabolism regulator
FT veA"
FT /id="PRO_0000435906"
FT DOMAIN 25..233
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..485
FT /note="PEST"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT REGION 491..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..44
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT COMPBIAS 325..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 61987 MW; 45B666DE9B05B943 CRC64;
MANRPSLMPP HNETEHSVSR ITREGKQLTY KLSVMQQPER ARACGAGAKS SADRRPVDPP
PVVELRIFES DPANDTQKTD ITFAYNANFF LYATLETARP IAHGRVGGPQ SCPVLTGVPV
AGVAYLDRPS QAGYFIFPDL SVRHEGRYRL SFHLYEEIKD AKDADKDSTL PLPNQIPLSA
TSKPGIPQAF LHFRLEVKSV PFTVYSAKKF PGLATSTSLS RIIAEQGCRV RIRRDVRMRR
RGDKRDEDYE FGEERAAAYA RSSDRFTTPD RYAASMDRPR SNSNGSNIES PYGFVPPDRR
PSAPDYGFQC PQPYQRPMPP APMSHSQTPS YQSHLSFGST PSHYPAPHMP PTPPPVAPQG
IYSPQHAYAQ IRHPSNGSEY EGTPIAYPAP QIPVERGGYP KPPMSSYAMD PPKPNSYMDP
RMPEPSLYPS TPNVPVSRPQ TPNLPAMPPP KPLSNDYANH VVPSVECTSP GGSGGGGYDN
VRGKRMVYQT GPTYGKRSHE DTFGLDDRSM QNGMRPDTEP YPAYRDFSGE SRAALMAEMG
IQLSYKRANG KIVMKAPPSS T
