ID F6T6M4_CALJA Unreviewed; 493 AA.
AC F6T6M4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00015118};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN Name=DNPEP {ECO:0000313|Ensembl:ENSCJAP00000045339.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000045339.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000045339.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000045339.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000256|ARBA:ARBA00011395}.
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR AlphaFoldDB; F6T6M4; -.
DR STRING; 9483.ENSCJAP00000045339; -.
DR Ensembl; ENSCJAT00000061059.4; ENSCJAP00000045339.3; ENSCJAG00000011753.6.
DR eggNOG; KOG2596; Eukaryota.
DR GeneTree; ENSGT00390000003164; -.
DR InParanoid; F6T6M4; -.
DR OMA; GPILKVN; -.
DR TreeFam; TF300487; -.
DR Proteomes; UP000008225; Chromosome 6.
DR Bgee; ENSCJAG00000011753; Expressed in heart and 6 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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 CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 493 AA; 54390 MW; A36D31937A64553B CRC64;
MGLSLSAAFV LNSWLAGYHK VAMTGKASKD AVHTAAKELL KFVNSSPSPF HAVAECRNRL
LQAGFSELKE TEKWDIKPEC KYFMTRNSST IIAFAVGGQY VPGNGFSLIG AHTDSPCLRV
KRRSRRSQVG FQQVGVETYG GGIWSTWFDR DLTLAGRLIV KCPTSGQLEQ RLVHVERPIL
RIPHLAIHLQ RNINENFGPN TEMHLVPILA TAVQEELEKG TPEPGPLNST DERHHSVLMT
LLCTHLDLSP KDIIEMELCL ADTQPAVLGG AYDEFIFAPR LDNLHSCFCA LQALIDSCAG
PGSLAMDPHV RMITLYDNEE VGSESAQGAQ SLLTELVLRR ISASYYHPTA FEEAIPKSFL
ISADMAHAVH PNYLDKHEEN HRPLFHKGPV IKVNSKQRYA SNAVSEALIR EVANKVNVPL
QDLMVRNDSP CGTTIGPILA SRLGLRVLDL GSPQLAMHSI REMACTTGVL QTLTLFKGFF
ELFPSLSHNL LVD
//