ID   DNPEP_RICCO             Reviewed;         491 AA.
AC   B9RAJ0;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable aspartyl aminopeptidase;
DE            EC=3.4.11.21;
GN   ORFNames=RCOM_1506700;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale;
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-283.
RX   PubMed=17672910; DOI=10.1186/1471-2229-7-42;
RA   Lu C., Wallis J.G., Browse J.;
RT   "An analysis of expressed sequence tags of developing castor endosperm
RT   using a full-length cDNA library.";
RL   BMC Plant Biol. 7:42-42(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-302.
RA   Kroon J.T., Kunst L., Slabas A.R., Smith M.A.;
RT   "Genomic Resources for Castor Bean (Ricinus communis); Generation of a
RT   normalized cDNA library from developing castor seed and sequencing of
RT   Expressed Sequence Tags.";
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Likely to play an important role in intracellular protein and
CC       peptide metabolism. {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   -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEF51817.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EV523896; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ973773; EEF51817.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; EV523896; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GE636502; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B9RAJ0; -.
DR   SMR; B9RAJ0; -.
DR   MEROPS; M18.A01; -.
DR   InParanoid; B9RAJ0; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
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   Protease; Reference proteome; Zinc.
FT   CHAIN           1..491
FT                   /note="Probable aspartyl aminopeptidase"
FT                   /id="PRO_0000416986"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         389
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         455
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  53907 MW;  F50A244121BA1A8F CRC64;
     MAKQDSQTEG ISIDSDLINF LNASPTAFHA IDEAKKRLKH SGYVQVSERD DWKLELGKRY
     FFTRNHSTIV AFAIGKKYVA GNGFYVVGAH TDSPCIKLKP VSKVTKSGYL EVGVQPYGGG
     LWHTWFDRDL AVAGRVIVRE EKHGSVSYSH RLVRIEEPIM RVPTLAIHLD RNVNTDGFKV
     NTQSHLLPVL ATSVKAELSK VVAENGTVGN DEETDGMKSS KGTTNANSKH HSLLLQMIAG
     QIGCNGSDIC DFELQACDTQ PSVIAGAAKE FIFSGRLDNL CMSFCSLKAL IDATASDSHL
     ENESGVRMVA LFDHEEVGSD SAQGAGSPVM FDALSRITST FNSDSKLLRK AIQKSFLVSA
     DMAHALHPNY ADKHEENHQP RMHGGLVIKH NANQRYATNS VTSFLFKEIA SKHNLPVQDF
     VVRNDMPCGS TIGPILASGV GIRTVDVGAP QLSMHSIREM CAVDDVKYSY EHFKAFFEDF
     SHLDSKITVD M