PEPE_DROME
ID PEPE_DROME Reviewed; 240 AA.
AC Q9VYH3; Q540X4;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable alpha-aspartyl dipeptidase;
DE EC=3.4.13.21;
DE AltName: Full=Asp-specific dipeptidase;
DE Short=Dipeptidase E;
GN ORFNames=CG2200;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate
CC residues. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-
CC Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor
CC does it cleave isoaspartyl peptides.; EC=3.4.13.21;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48224.1; -; Genomic_DNA.
DR EMBL; AY118855; AAM50715.1; -; mRNA.
DR RefSeq; NP_001285183.1; NM_001298254.1.
DR RefSeq; NP_572852.1; NM_132624.2.
DR AlphaFoldDB; Q9VYH3; -.
DR SMR; Q9VYH3; -.
DR BioGRID; 58644; 2.
DR DIP; DIP-21896N; -.
DR IntAct; Q9VYH3; 2.
DR STRING; 7227.FBpp0073552; -.
DR MEROPS; S51.002; -.
DR PaxDb; Q9VYH3; -.
DR PRIDE; Q9VYH3; -.
DR DNASU; 32258; -.
DR EnsemblMetazoa; FBtr0073721; FBpp0073552; FBgn0030447.
DR EnsemblMetazoa; FBtr0340301; FBpp0309262; FBgn0030447.
DR GeneID; 32258; -.
DR KEGG; dme:Dmel_CG2200; -.
DR UCSC; CG2200-RA; d. melanogaster.
DR FlyBase; FBgn0030447; CG2200.
DR VEuPathDB; VectorBase:FBgn0030447; -.
DR eggNOG; ENOG502QR7X; Eukaryota.
DR HOGENOM; CLU_071689_0_0_1; -.
DR InParanoid; Q9VYH3; -.
DR OMA; RDHDKYT; -.
DR OrthoDB; 1341849at2759; -.
DR PhylomeDB; Q9VYH3; -.
DR BioGRID-ORCS; 32258; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32258; -.
DR PRO; PR:Q9VYH3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030447; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VYH3; baseline and differential.
DR Genevisible; Q9VYH3; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03146; GAT1_Peptidase_E; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dipeptidase; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..240
FT /note="Probable alpha-aspartyl dipeptidase"
FT /id="PRO_0000209965"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 26598 MW; 3D918D9CB4F6D3E0 CRC64;
MASARNLLLL SSSRLHGHGY LEHARGQLED LFKSANVKTV LFVPYALRDH DKYTATVRDA
LQPWGFNVEG LHTKPDREQA LREAQAIFVG GGNTFVLLRS LYEMKLLDPI RELVLQRGLP
YVGSSAGTNV ATRSIHTTND MPVAYPPSFE ALALVPFNIN PHYLDPEAGS RHKGETRDER
LEEFVAYHGL PVLGLREGTS VRVQGEKAIL LGDRNAKLFK ADGGTEELAP LADLTFLLQK
