DNPEP_DICDI
ID DNPEP_DICDI Reviewed; 484 AA.
AC Q54M70;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Aspartyl aminopeptidase;
DE EC=3.4.11.21;
GN Name=dnpep; ORFNames=DDB_G0286149;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-17; 59-91; 153-162 AND 437-451, ACETYLATION AT MET-1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
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 ---------------------------------------------------------------------------
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; AAFI02000085; EAL64367.1; -; Genomic_DNA.
DR RefSeq; XP_637878.1; XM_632786.1.
DR AlphaFoldDB; Q54M70; -.
DR SMR; Q54M70; -.
DR STRING; 44689.DDB0266791; -.
DR MEROPS; M18.A01; -.
DR PaxDb; Q54M70; -.
DR EnsemblProtists; EAL64367; EAL64367; DDB_G0286149.
DR GeneID; 8625475; -.
DR KEGG; ddi:DDB_G0286149; -.
DR dictyBase; DDB_G0286149; dnpep.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; Q54M70; -.
DR OMA; GPILKVN; -.
DR PhylomeDB; Q54M70; -.
DR PRO; PR:Q54M70; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:dictyBase.
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 Acetylation; Aminopeptidase; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..484
FT /note="Aspartyl aminopeptidase"
FT /id="PRO_0000328103"
FT REGION 188..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 484 AA; 53354 MW; E22F08CB0A47009C CRC64;
MEQYLPQAKE FISFIDKSPS PYHAVQYFSE ILKSKGFIHL SEKQMWDIQP NKKYFFTRNQ
SCISAFAVGG KYKPGNGFNI AAAHTDSPNF KVRPVSKVES VGYQQVGVET YGGGLWYTWF
DRDLTVAGRV IVKSGDGSYE SKLVHIKKPI LRIPSLAIHL DRSVNTDGFK YNTQNHLVPM
IASKLSEPVE SKSTTTTTTT ESPKTSDPQD VNSSTTKHHA VLLELLSKEL GCSVGDIQNF
DLSVCDTQPA AIGGALDEFI FSPRCDNLGM SYCAMIGLLN VKESTLAQEE NVLNVILFDN
EEVGSSSPQG ACAPLINDTI SRVNSSMFAS TCKPHELNNF IDLTLRNSFL ISADMAHAIH
PNYTANHEPL HRPALNKGPV IKYNANLRYA SNGPTSFVIL DICKKNGIPI QEFLVKNDSP
CGSTIGPIIS GTYGIRTVDI GNPQLSMHSI RETCGVADIT HGINLIQKYF EQFTKLDIIK
SDLE
