VPEA_ARATH
ID VPEA_ARATH Reviewed; 478 AA.
AC P49047; O82806; Q7GAI8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Vacuolar-processing enzyme alpha-isozyme;
DE EC=3.4.22.34 {ECO:0000250|UniProtKB:Q84LM2};
DE AltName: Full=Alpha-VPE;
DE AltName: Full=Asparaginyl endopeptidase alpha-VPE {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At2g25940; ORFNames=T19L18.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7579169; DOI=10.1007/bf00019120;
RA Kinoshita T., Nishimura M., Hara-Nishimura I.;
RT "Homologues of a vacuolar processing enzyme that are expressed in different
RT organs in Arabidopsis thaliana.";
RL Plant Mol. Biol. 29:81-89(1995).
RN [2]
RP SEQUENCE REVISION TO 70; 84 AND 91.
RA Kinoshita T., Nishimura M., Hara-Nishimura I.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION BY SENESCENCE; WOUNDING; ETHYLENE;
RP JASMONATE AND SALICYLIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=10417725; DOI=10.1046/j.1365-313x.1999.00497.x;
RA Kinoshita T., Yamada K., Hiraiwa N., Kondo M., Nishimura M.,
RA Hara-Nishimura I.;
RT "Vacuolar processing enzyme is up-regulated in the lytic vacuoles of
RT vegetative tissues during senescence and under various stressed
RT conditions.";
RL Plant J. 19:43-53(1999).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=14688293; DOI=10.1105/tpc.016378;
RA Gruis D., Schulze J., Jung R.;
RT "Storage protein accumulation in the absence of the vacuolar processing
RT enzyme family of cysteine proteases.";
RL Plant Cell 16:270-290(2004).
CC -!- FUNCTION: Asparagine-specific endopeptidase involved in the processing
CC of vacuolar seed protein precursors into the mature forms
CC (PubMed:7579169). Probably involved in post-translational proteolysis
CC of seed storage proteins in the protein storage vacuole of developing
CC seeds (PubMed:14688293). {ECO:0000269|PubMed:14688293,
CC ECO:0000269|PubMed:7579169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins and small molecule substrates at
CC -Asn-|-Xaa- bonds.; EC=3.4.22.34;
CC Evidence={ECO:0000250|UniProtKB:Q84LM2};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:7579169}.
CC -!- TISSUE SPECIFICITY: Specific to vegetative organs, especially in
CC senescent tissues. Expressed in developing seeds, rosette leaves,
CC cauline leaves and stems. Not expressed in the siliques. Also present
CC at the branching points of the roots and in vascular tissues.
CC {ECO:0000269|PubMed:10417725, ECO:0000269|PubMed:14688293,
CC ECO:0000269|PubMed:7579169}.
CC -!- INDUCTION: By senescence, wounding, ethylene and salicylic acid (SA).
CC {ECO:0000269|PubMed:10417725}.
CC -!- PTM: Auto-catalytic activation. {ECO:0000250|UniProtKB:Q84LM2}.
CC -!- DISRUPTION PHENOTYPE: No macroscopic phenotype, probably due to
CC functional redundancy. In plants lacking all vacuolar-processing enzyme
CC isozymes (e.g. alpha, beta, gamma and delta) shift of storage protein
CC accumulation from normally processed polypeptides to a finite number of
CC prominent alternatively processed polypeptides cleaved at sites other
CC than the conserved Asn residues targeted by VPE.
CC {ECO:0000269|PubMed:14688293}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; D61393; BAA09614.2; -; Genomic_DNA.
DR EMBL; AC004747; AAC31241.1; -; Genomic_DNA.
DR EMBL; AC005395; AAM15043.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07775.1; -; Genomic_DNA.
DR EMBL; AY058055; AAL24163.1; -; mRNA.
DR EMBL; AY090296; AAL90957.1; -; mRNA.
DR PIR; T02629; T02629.
DR RefSeq; NP_180165.1; NM_128154.5.
DR AlphaFoldDB; P49047; -.
DR SMR; P49047; -.
DR STRING; 3702.AT2G25940.1; -.
DR MEROPS; C13.006; -.
DR PaxDb; P49047; -.
DR PRIDE; P49047; -.
DR ProteomicsDB; 242566; -.
DR EnsemblPlants; AT2G25940.1; AT2G25940.1; AT2G25940.
DR GeneID; 817135; -.
DR Gramene; AT2G25940.1; AT2G25940.1; AT2G25940.
DR KEGG; ath:AT2G25940; -.
DR Araport; AT2G25940; -.
DR TAIR; locus:2043510; AT2G25940.
DR eggNOG; KOG1348; Eukaryota.
DR HOGENOM; CLU_024160_0_0_1; -.
DR InParanoid; P49047; -.
DR OMA; MQACPTI; -.
DR OrthoDB; 826971at2759; -.
DR PhylomeDB; P49047; -.
DR PRO; PR:P49047; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P49047; baseline and differential.
DR Genevisible; P49047; AT.
DR GO; GO:0000326; C:protein storage vacuole; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006624; P:vacuolar protein processing; ISS:TAIR.
DR InterPro; IPR043577; AE.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; PTHR12000; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500139; AE; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Signal; Thiol protease; Vacuole.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..478
FT /note="Vacuolar-processing enzyme alpha-isozyme"
FT /id="PRO_0000026526"
FT ACT_SITE 162
FT /evidence="ECO:0000255"
FT ACT_SITE 204
FT /evidence="ECO:0000255"
FT SITE 251
FT /note="Required for post-translational maturation and
FT enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q84LM2"
SQ SEQUENCE 478 AA; 52670 MW; D73D1F353E2FE898 CRC64;
MTTVVSFLAL FLFLVAAVSG DVIKLPSLAS KFFRPTENDD DSTKWAVLVA GSSGYWNYRH
QADVCHAYQL LKKGGVKEEN IVVFMYDDIA KNEENPRPGV IINSPNGEDV YNGVPKDYTG
DEVNVDNLLA VILGNKTALK GGSGKVVDSG PNDHIFIYYS DHGGPGVLGM PTSPNLYAND
LNDVLKKKYA SGTYKSLVFY LEACESGSIF EGLLPEGLNI YATTASNAEE SSWGTYCPGE
DPSPPSEYET CLGDLYSVAW IEDSEKHNLQ TETLHEQYEL VKKRTAGSGK SYGSHVMEFG
DIGLSKEKLV LFMGTNPADE NFTFVNENSI RPPSRVTNQR DADLVHFWHK YQKAPEGSAR
KVEAQKQVLE AMSHRLHVDN SILLIGILLF GLEGHAVLNK VRPSGEPLVD DWDCLKSLVR
AFERHCGSLS QYGIKHMRSI ANMCNAGIQM RQMEEAAMQA CPTIPTSPWS SLDRGFSA
