ID H2R643_PANTR Unreviewed; 471 AA.
AC H2R643;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
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:ENSPTRP00000048734.2,
GN ECO:0000313|VGNC:VGNC:168};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000048734.2, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000048734.2, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000048734.2}
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 EMBL; AACZ04056567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009442645.1; XM_009444370.2.
DR RefSeq; XP_009442646.1; XM_009444371.2.
DR RefSeq; XP_016806055.1; XM_016950566.1.
DR RefSeq; XP_016806058.1; XM_016950569.1.
DR AlphaFoldDB; H2R643; -.
DR MEROPS; M18.002; -.
DR Ensembl; ENSPTRT00000056086.2; ENSPTRP00000048734.2; ENSPTRG00000012954.6.
DR GeneID; 459964; -.
DR CTD; 23549; -.
DR VGNC; VGNC:168; DNPEP.
DR eggNOG; KOG2596; Eukaryota.
DR GeneTree; ENSGT00390000003164; -.
DR HOGENOM; CLU_019532_2_0_1; -.
DR OrthoDB; 1156at2759; -.
DR TreeFam; TF300487; -.
DR Proteomes; UP000002277; Chromosome 2B.
DR Bgee; ENSPTRG00000012954; Expressed in testis and 21 other cell types or tissues.
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 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:UP000002277};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 471 AA; 52057 MW; 4DA7BE57E75C9FAE CRC64;
MNGKARQEAV QTAAKELLKF VNRSPSPFHA VAECRKRLLQ AGFSELKETE KWNIKPESKY
FMTRNSSTII AFAVGGQYVP GNGFSLIGAH TDSPCLRVKR RSRRSQVGFQ QVGVETYGGG
IWSTWFDRDL TLAGRVIVKC PTSGRLEQQL VHVERPILRI PHLAIHLQRN INENFGPNTE
MHLVPILATA IQEELEKGTP EPGPLNAVDE RHHSVLMSLL CAHLGLSPKD IVEMELCLAD
TQPAVLGGAY DEFIFAPRLD NLHSCFCALQ ALIDSCTGPG SLATEPHVRM ITLYDNEEVG
SESAQGAQSL LTELVLRRIS ASCQHPTAFE EAIPKSFMIS ADMAHAVHPN YLDKHEENHR
PLFHKGPVIK VNSKQRYASN AVSEALIREV ANKVKVPLQD LMVRNDTPCG TTIGPILASR
LGLRVLDLGS PQLAMHSIRE MACTTGVLQT LTLFKGFFEL FPSLSHNLLV D
//
