ID   DNPEP_PONAB             Reviewed;         471 AA.
AC   Q5RBT2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Aspartyl aminopeptidase {ECO:0000250|UniProtKB:Q9ULA0};
DE            EC=3.4.11.21 {ECO:0000250|UniProtKB:Q9ULA0};
GN   Name=DNPEP {ECO:0000250|UniProtKB:Q9ULA0};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Aminopeptidase with specificity towards an acidic amino acid
CC       at the N-terminus. Likely to play an important role in intracellular
CC       protein and peptide metabolism (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: One of the zinc ions is readily exchangeable with
CC       other divalent cations such as manganese, which strongly stimulates the
CC       enzymatic activity. {ECO:0000250}.
CC   -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR   EMBL; CR858551; CAH90778.1; -; mRNA.
DR   RefSeq; NP_001125438.1; NM_001131966.1.
DR   AlphaFoldDB; Q5RBT2; -.
DR   SMR; Q5RBT2; -.
DR   STRING; 9601.ENSPPYP00000014757; -.
DR   MEROPS; M18.002; -.
DR   GeneID; 100172346; -.
DR   KEGG; pon:100172346; -.
DR   CTD; 23549; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   InParanoid; Q5RBT2; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Phosphoprotein; Protease; Reference proteome; Zinc.
FT   CHAIN           1..471
FT                   /note="Aspartyl aminopeptidase"
FT                   /id="PRO_0000284911"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         199
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULA0"
SQ   SEQUENCE   471 AA;  52015 MW;  6976DC805C9B4BB8 CRC64;
     MNGKARQEAV QTAAKELLKF VNQGPSPFHA VAECRNRLLQ AGFSELKETE KWNIKPESKY
     FMTRNSSTII AFAVGGQYVP GNGFSLIGAH TDSPCLRVKR RSRRSQVGFQ QVGVETYGGG
     IWSTWFDRDL TLAGRVIVKC PTSGRLEQRL VHVERPILRI PHLAIHLQRN INENFGPNTE
     MHLVPILATA IQEELEKGTP EPGPLNAMDE RHHSVLMSLL CAHLGLSPKD IVEMELCLAD
     TQPAVLGGAY DEFIFAPRLD NLHSCFCALQ ALIDSCAGPG SLATEPHVRM ITLYDNEEVG
     SESAQGAQSL LTELVLRRIS ASCQHPTAFE EAIPKSFMIS ADMAHAVHPN YLDKHEENHR
     PLFHKGPVIK VNSKQRYASN AVSEALIREV ANKVKVPLQD LMVRNDTPCG TTIGPILASR
     LGLRVLDLGS PQLAMHSIRE MACTTGVLQT LTLFKGFFEL FPSLSHNLLV D