PEPE_XENLA
ID PEPE_XENLA Reviewed; 242 AA.
AC Q91642; Q5PQ56;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Alpha-aspartyl dipeptidase;
DE EC=3.4.13.21;
DE AltName: Full=Asp-specific dipeptidase;
DE AltName: Full=Dipeptidase E;
GN Name=aad-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8700860; DOI=10.1073/pnas.93.5.1924;
RA Brown D.D., Wang Z., Furlow J.D., Kanamori A., Schwartzman R.A., Remo B.F.,
RA Pinder A.;
RT "The thyroid hormone-induced tail resorption program during Xenopus laevis
RT metamorphosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1924-1929(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RX PubMed=10762256; DOI=10.1128/jb.182.9.2536-2543.2000;
RA Lassy R.A., Miller C.G.;
RT "Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a
RT serine hydrolase.";
RL J. Bacteriol. 182:2536-2543(2000).
CC -!- FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate
CC residues.
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; U37377; AAC59869.1; -; mRNA.
DR EMBL; BC087353; AAH87353.1; -; mRNA.
DR RefSeq; NP_001079269.1; NM_001085800.1.
DR PDB; 7C9B; X-ray; 1.40 A; A=1-242.
DR PDB; 7FFP; X-ray; 1.80 A; A=1-242.
DR PDBsum; 7C9B; -.
DR PDBsum; 7FFP; -.
DR AlphaFoldDB; Q91642; -.
DR SMR; Q91642; -.
DR MEROPS; S51.002; -.
DR MaxQB; Q91642; -.
DR DNASU; 378550; -.
DR GeneID; 378550; -.
DR KEGG; xla:378550; -.
DR CTD; 378550; -.
DR Xenbase; XB-GENE-480548; dpepe.L.
DR OMA; RDHDKYT; -.
DR OrthoDB; 1341849at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 378550; Expressed in intestine and 20 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dipeptidase; Hydrolase; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..242
FT /note="Alpha-aspartyl dipeptidase"
FT /id="PRO_0000209966"
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"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:7C9B"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:7C9B"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:7C9B"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7C9B"
SQ SEQUENCE 242 AA; 26952 MW; 4371D311853B2236 CRC64;
MMTMRRHLLL VSNSTLHGGG YLEHCQEHIL KFLGAQVKRV LFIPYALHDR DAYAKTARQK
FEALGYGLDS VHESPDPVDA VKKAEAIFIG GGNTFRLLKA LYDNDLIAAI RKRVLEDGVP
YIGSSAGTNV ATISINTTND MPIVYPPSLK ALELVPFNIN PHYLDPDGNS KHMGETREQR
ITQYHEEHDT PPVLGLREGC FLLVEGDKAT LLGITRARLF LRGKNPTEHE PGHDFSFLLG
HS
