VPEG_ARATH
ID VPEG_ARATH Reviewed; 494 AA.
AC Q39119; Q93VM0; Q9SB73;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Vacuolar-processing enzyme gamma-isozyme;
DE EC=3.4.22.34 {ECO:0000250|UniProtKB:Q84LM2};
DE AltName: Full=Asparaginyl endopeptidase gamma-VPE {ECO:0000305};
DE AltName: Full=Gamma-VPE;
DE Flags: Precursor;
GN OrderedLocusNames=At4g32940; ORFNames=F26P21.60;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=8589932;
RA Kinoshita T., Nishimura M., Hara-Nishimura I.;
RT "The sequence and expression of the gamma-VPE gene, one member of a family
RT of three genes for vacuolar processing enzymes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 36:1555-1562(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION BY
RP SENESCENCE; WOUNDING; ETHYLENE 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 [6]
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:10417725). 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:10417725,
CC ECO:0000269|PubMed:14688293}.
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:8589932}. Lytic
CC vacuole {ECO:0000269|PubMed:10417725}. Note=Localized in lytic vacuoles
CC of wounded leaves. {ECO:0000269|PubMed:10417725}.
CC -!- TISSUE SPECIFICITY: Specific to vegetative organs, especially in
CC senescent tissues. Also expressed in seeds and root tips.
CC {ECO:0000269|PubMed:10417725, ECO:0000269|PubMed:14688293}.
CC -!- INDUCTION: By senescence, wounding, jasmonic acid (JA), ethylene and
CC salicylic acid (SA). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18924.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D61395; BAA18924.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL031804; CAA21203.1; -; Genomic_DNA.
DR EMBL; AL161582; CAB80011.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86150.1; -; Genomic_DNA.
DR EMBL; AF370160; AAK43975.1; -; mRNA.
DR EMBL; AF424619; AAL11612.1; -; mRNA.
DR EMBL; AY059104; AAL15210.1; -; mRNA.
DR EMBL; AY133531; AAM91361.1; -; mRNA.
DR PIR; T05302; T05302.
DR RefSeq; NP_195020.1; NM_119448.4.
DR PDB; 5NIJ; X-ray; 2.75 A; A/B/C/D=56-494.
DR PDBsum; 5NIJ; -.
DR AlphaFoldDB; Q39119; -.
DR SMR; Q39119; -.
DR BioGRID; 14716; 2.
DR STRING; 3702.AT4G32940.1; -.
DR MEROPS; C13.006; -.
DR PaxDb; Q39119; -.
DR PRIDE; Q39119; -.
DR ProteomicsDB; 242737; -.
DR EnsemblPlants; AT4G32940.1; AT4G32940.1; AT4G32940.
DR GeneID; 829431; -.
DR Gramene; AT4G32940.1; AT4G32940.1; AT4G32940.
DR KEGG; ath:AT4G32940; -.
DR Araport; AT4G32940; -.
DR TAIR; locus:2123782; AT4G32940.
DR eggNOG; KOG1348; Eukaryota.
DR HOGENOM; CLU_024160_0_0_1; -.
DR InParanoid; Q39119; -.
DR OMA; ICNAGMT; -.
DR OrthoDB; 826971at2759; -.
DR PhylomeDB; Q39119; -.
DR BRENDA; 3.4.22.34; 399.
DR PRO; PR:Q39119; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39119; baseline and differential.
DR Genevisible; Q39119; AT.
DR GO; GO:0000323; C:lytic vacuole; IDA:TAIR.
DR GO; GO:0000326; C:protein storage vacuole; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0006624; P:vacuolar protein processing; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protease; Reference proteome; Signal;
KW Thiol protease; Vacuole.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..494
FT /note="Vacuolar-processing enzyme gamma-isozyme"
FT /id="PRO_0000026528"
FT ACT_SITE 177
FT /evidence="ECO:0000255"
FT ACT_SITE 219
FT /evidence="ECO:0000255"
FT SITE 266
FT /note="Required for post-translational maturation and
FT enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q84LM2"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:5NIJ"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:5NIJ"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:5NIJ"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 317..321
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 374..415
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 428..442
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 453..461
FT /evidence="ECO:0007829|PDB:5NIJ"
FT HELIX 466..477
FT /evidence="ECO:0007829|PDB:5NIJ"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:5NIJ"
SQ SEQUENCE 494 AA; 54336 MW; 9C8C47E644490984 CRC64;
MATTMTRVSV GVVLFVLLVS LVAVSAARSG PDDVIKLPSQ ASRFFRPAEN DDDSNSGTRW
AVLVAGSSGY WNYRHQADIC HAYQLLRKGG LKEENIVVFM YDDIANNYEN PRPGTIINSP
HGKDVYQGVP KDYTGDDVNV DNLFAVILGD KTAVKGGSGK VVDSGPNDHI FIFYSDHGGP
GVLGMPTSPY LYANDLNDVL KKKHALGTYK SLVFYLEACE SGSIFEGLLP EGLNIYATTA
SNAEESSWGT YCPGEEPSPP PEYETCLGDL YSVAWMEDSG MHNLQTETLH QQYELVKRRT
APVGYSYGSH VMQYGDVGIS KDNLDLYMGT NPANDNFTFA DANSLKPPSR VTNQRDADLV
HFWEKYRKAP EGSARKTEAQ KQVLEAMSHR LHIDNSVILV GKILFGISRG PEVLNKVRSA
GQPLVDDWNC LKNQVRAFER HCGSLSQYGI KHMRSFANIC NAGIQMEQME EAASQACTTL
PTGPWSSLNR GFSA
