ID A0A2I3H9G2_NOMLE Unreviewed; 464 AA.
AC A0A2I3H9G2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cytosol aminopeptidase {ECO:0000256|ARBA:ARBA00014190};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.13.23 {ECO:0000256|ARBA:ARBA00023625};
DE AltName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000256|ARBA:ARBA00030997};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000256|ARBA:ARBA00031564};
DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|ARBA:ARBA00033172};
DE AltName: Full=Proline aminopeptidase {ECO:0000256|ARBA:ARBA00030930};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605};
GN Name=LAP3 {ECO:0000313|Ensembl:ENSNLEP00000040294.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000040294.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000040294.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000040294.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000256|ARBA:ARBA00023511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000256|ARBA:ARBA00023511};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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; ADFV01181643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01181644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01181645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01181646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01181647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3H9G2; -.
DR STRING; 61853.ENSNLEP00000040294; -.
DR Ensembl; ENSNLET00000053801.1; ENSNLEP00000040294.1; ENSNLEG00000016606.3.
DR GeneTree; ENSGT00530000063255; -.
DR InParanoid; A0A2I3H9G2; -.
DR OMA; MVTMKAD; -.
DR Proteomes; UP000001073; Chromosome 20.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963:SF52; CYTOSOL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 307..314
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 464 AA; 50113 MW; B0F392B7CB63448F CRC64;
MFLMPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD
KLIAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN
IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGR
PKSWIEEQAM GSFLSVAKGS DEPPVFLEIH YKGSPNANEP PLVFVGKGIT FDSGGISIKA
SANMDLMRAD MGGAATICSA IVSAAKLNLP INIIGLAPLC ENMPSGKANK PGDVVRAKNG
KTIQVDNTDA EGRLILADAL CYAHTFNPKV ILNAATLTGA MDVALGSGAT GVFTNSSWLW
NKLFEASIET GDRVWRMPLF EHYTRQVVDC QLADVNNIGK YRSAGACTAA AFLKEFVTHP
KWAHLDIAGV MTNKDEVPYL RKGMTGRPTR TLIEFLLRFS QDNA
//
