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WETA_PENRW
ID   WETA_PENRW              Reviewed;         520 AA.
AC   Q01870; B6HRB1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Developmental regulatory protein wetA {ECO:0000305};
GN   Name=wetA {ECO:0000303|PubMed:8078481}; ORFNames=Pc22g03220;
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 [GENOMIC DNA], AND FUNCTION.
RX   PubMed=8078481; DOI=10.1007/bf00583905;
RA   Prade R.A., Timberlake W.E.;
RT   "The Penicillium chrysogenum and Aspergillus nidulans wetA developmental
RT   regulatory genes are functionally equivalent.";
RL   Mol. Gen. Genet. 244:539-547(1994).
RN   [2]
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   [3]
RP   INDUCTION.
RX   PubMed=18364746; DOI=10.1139/o07-148;
RA   Garcia-Rico R.O., Fierro F., Martin J.F.;
RT   "Heterotrimeric Galpha protein Pga1 of Penicillium chrysogenum controls
RT   conidiation mainly by a cAMP-independent mechanism.";
RL   Biochem. Cell Biol. 86:57-69(2008).
CC   -!- FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore
CC       development and conidium maturation (By similarity). They act
CC       individually and together to regulate their own expression and that of
CC       numerous other sporulation-specific genes (By similarity). Responsible
CC       for activating a set of genes whose products make up the final two
CC       conidial wall layers or direct their assembly and though this activity
CC       is responsible for acquisition of spore dormancy (PubMed:8078481).
CC       {ECO:0000250|UniProtKB:P22022, ECO:0000269|PubMed:8078481}.
CC   -!- INDUCTION: Expression is regulated by the heterotrimeric G protein pga1
CC       (PubMed:18364746). {ECO:0000269|PubMed:18364746}.
CC   -!- SIMILARITY: Belongs to the wetA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA56364.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X80058; CAA56364.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AM920437; CAP97610.1; -; Genomic_DNA.
DR   PIR; S46660; S46660.
DR   RefSeq; XP_002564365.1; XM_002564319.1.
DR   AlphaFoldDB; Q01870; -.
DR   STRING; 1108849.XP_002564365.1; -.
DR   EnsemblFungi; CAP97610; CAP97610; PCH_Pc22g03220.
DR   GeneID; 8311640; -.
DR   KEGG; pcs:Pc22g03220; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g03220; -.
DR   eggNOG; ENOG502S8IT; Eukaryota.
DR   HOGENOM; CLU_030750_0_0_1; -.
DR   OMA; MAYQEAW; -.
DR   OrthoDB; 638649at2759; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR040112; WetA.
DR   PANTHER; PTHR22934:SF23; PTHR22934:SF23; 2.
PE   2: Evidence at transcript level;
KW   Activator; Conidiation; Reference proteome; Sporulation; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..520
FT                   /note="Developmental regulatory protein wetA"
FT                   /id="PRO_0000065962"
FT   REGION          49..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        226
FT                   /note="P -> A (in Ref. 1; CAA56364)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="A -> G (in Ref. 1; CAA56364)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   520 AA;  56885 MW;  D8AAEC1AF1761521 CRC64;
     MFAQPYDHSF NDLFNQYVNM ETSAVDGKDS ALSDFDQLFP LDSLSSDCGD LPPTVSTPKR
     HQSPQPWSNE WSLQDDGAAA DHFAFHDTVH PSAISDVNLN NFEVPSRPTA SHGLSTSPST
     PPATPRRKPT QSALITPKSI RHRSPNERRS HLRKQSFSPS LMRSSNLSKA RMAYPEAWAQ
     RLQNFSLHGS EDRLPLSPPP SDVLIQHENM PTEQIMNQHG DSAERPSQYD ARLYQQSPSV
     SMPSPSIAMS ARQQQHYIAQ PSSSSLTNSS PSSADDIFSS SHSSDPHSLS SWQSDPLHAS
     SLSFTPDLQG QDSQWWSPMP SRVAQQQAAY LTSPTPVRTM QSVGSQNDMM QGGLMIQFNP
     SYDMSADHSF SSSNMLPATP QKFDTSFNTS QVHNVSRSPS LSPKAGTSPR DTRNGSISKP
     THRRTHSRKL SGQSMNAPKP AKASGSSSRG SNKSVSVSFV NFTAHDSKKI LTGVAPSGSS
     KTKARREQEA RDRRRKLSEA ALRAVRSAGG DVEALEAVLC
 
 
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