DNPEP_CAEEL
ID DNPEP_CAEEL Reviewed; 470 AA.
AC Q19087;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0000312|WormBase:F01F1.9b};
DE EC=3.4.11.21 {ECO:0000269|PubMed:23427264};
GN Name=dnpp-1 {ECO:0000312|WormBase:F01F1.9b};
GN ORFNames=F01F1.9 {ECO:0000312|WormBase:F01F1.9b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF HIS-92; HIS-166; GLU-331 AND HIS-437.
RX PubMed=23427264; DOI=10.1091/mbc.e12-10-0730;
RA Li X., Chen B., Yoshina S., Cai T., Yang F., Mitani S., Wang X.;
RT "Inactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores
RT endocytic sorting and recycling in tat-1 mutants.";
RL Mol. Biol. Cell 24:1163-1175(2013).
CC -!- FUNCTION: Aminopeptidase with specificity towards an acidic amino acid
CC at the N-terminus. Plays a role in membrane trafficking and is
CC specifically involved in the recycling and degradation of endocytic
CC cargo. {ECO:0000269|PubMed:23427264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000269|PubMed:23427264};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9ULA0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9ULA0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.58 mM for H-Asp-NHMec (at pH 7.5)
CC {ECO:0000269|PubMed:23427264};
CC KM=8.854 mM for H-Glu-NHMec (at pH 7.5)
CC {ECO:0000269|PubMed:23427264};
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000250|UniProtKB:Q9ULA0}.
CC -!- INTERACTION:
CC Q19087; Q19087: dnpp-1; NbExp=3; IntAct=EBI-367822, EBI-367822;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23427264}.
CC Note=Diffuse expression in the cytosol. {ECO:0000269|PubMed:23427264}.
CC -!- TISSUE SPECIFICITY: Expressed in various cell types and tissues
CC including the pharynx, neurons, body wall muscle, intestine and vulva.
CC {ECO:0000269|PubMed:23427264}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the embryonic stage to adulthood.
CC {ECO:0000269|PubMed:23427264}.
CC -!- DISRUPTION PHENOTYPE: Animals are viable. Suppresses the abnormal
CC formation of intestinal vacuoles phenotype in mutants lacking the
CC phospholipid-transporting ATPase tat-1 or its chaperone chat-1.
CC {ECO:0000269|PubMed:23427264}.
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR EMBL; BX284603; CCD65992.1; -; Genomic_DNA.
DR PIR; T15946; T15946.
DR RefSeq; NP_498265.1; NM_065864.5.
DR AlphaFoldDB; Q19087; -.
DR SMR; Q19087; -.
DR BioGRID; 41044; 35.
DR IntAct; Q19087; 2.
DR STRING; 6239.F01F1.9; -.
DR MEROPS; M18.002; -.
DR EPD; Q19087; -.
DR PaxDb; Q19087; -.
DR PeptideAtlas; Q19087; -.
DR EnsemblMetazoa; F01F1.9b.1; F01F1.9b.1; WBGene00017163.
DR GeneID; 175822; -.
DR UCSC; F01F1.9; c. elegans.
DR CTD; 175822; -.
DR WormBase; F01F1.9b; CE01235; WBGene00017163; dnpp-1.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; Q19087; -.
DR OMA; GPILKVN; -.
DR PhylomeDB; Q19087; -.
DR PRO; PR:Q19087; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017163; Expressed in material anatomical entity and 5 other tissues.
DR ExpressionAtlas; Q19087; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..470
FT /note="Aspartyl aminopeptidase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000173453"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULA0"
FT MUTAGEN 92
FT /note="H->F: In M3; results in loss of enzymatic activity;
FT when associated with F-166 and F-437."
FT /evidence="ECO:0000269|PubMed:23427264"
FT MUTAGEN 166
FT /note="H->F: In M3; results in loss of enzymatic activity;
FT when associated with F-92 and F-437."
FT /evidence="ECO:0000269|PubMed:23427264"
FT MUTAGEN 331
FT /note="E->L: In qx49; loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:23427264"
FT MUTAGEN 437
FT /note="H->F: In M3; results in loss of enzymatic activity;
FT when associated with F-92 and F-166."
FT /evidence="ECO:0000269|PubMed:23427264"
SQ SEQUENCE 470 AA; 51157 MW; 839830EE2F60F13F CRC64;
MAAALKPSAP EIRKAAQEFI NYLNKAVTPF HATQEVKDRL LQAGFTELPE SGHWDIQPTS
KYFVTKNRSA ILAFAVGGSY KPGSGFSIVV GHTDSPCLRV KPISHQKSDK FLQVGVSTYG
GGIWRTWFDR DLSVAGLVIV KNGEKLQHKL IDVKKPVLFI PNLAIHLETD RTTFKPNTET
ELRPILETFA AAGINAPQKP ESTGFADPRN ITNNHHPQFL GLIAKEAGCQ PEDIVDLDLY
LYDTNKAAIV GMEDEFISGA RLDNQVGTYT AISGLLESLT GESFKNDPQI RIAACFDNEE
VGSDSAMGAS SSFTEFVLRR LSAGGSTTAF EEAIGKSMLI SADQAHATHP NYSAKHEENH
RPAFHGGVVV KVNVNQRYAT TSTTHAALKQ VAFEAQVPLQ VVVVRNDSPC GSTVGPILAT
KLGLQTVDVG CPQLAMHSIR EFADTSSIYQ ATTLYSTFYE RLSTVLSNMQ
