ID G2HHE6_PANTR Unreviewed; 519 AA.
AC G2HHE6; A0A2J8NW98;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Cytosol aminopeptidase {ECO:0000256|ARBA:ARBA00014190};
DE EC=3.4.11.1 {ECO:0000256|ARBA:ARBA00012565};
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|EMBL:JAA04696.1,
GN ECO:0000313|Ensembl:ENSPTRP00000027448.2, ECO:0000313|VGNC:VGNC:625};
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|EMBL:BAK63154.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000027448.2, 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|EMBL:BAK63154.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:BAK63154.1};
RX PubMed=21484476; DOI=10.1007/s10142-011-0220-9;
RA Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A.,
RA Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K.,
RA Kim D.S., Park H.S.;
RT "Major chimpanzee-specific structural changes in sperm development-
RT associated genes.";
RL Funct. Integr. Genomics 11:507-517(2011).
RN [3] {ECO:0000313|EMBL:JAA04696.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA04696.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA35009.1}, and Skin {ECO:0000313|EMBL:JAA31102.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSPTRP00000027448.2}
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=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
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 -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; AACZ04033682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK306160; BAK63154.1; -; mRNA.
DR EMBL; GABC01006642; JAA04696.1; -; mRNA.
DR EMBL; GABD01001998; JAA31102.1; -; mRNA.
DR EMBL; GABE01009730; JAA35009.1; -; mRNA.
DR RefSeq; NP_001233394.1; NM_001246465.1.
DR STRING; 9598.ENSPTRP00000027448; -.
DR MEROPS; M17.001; -.
DR PaxDb; 9598-ENSPTRP00000027448; -.
DR Ensembl; ENSPTRT00000029748.3; ENSPTRP00000027448.2; ENSPTRG00000015938.3.
DR GeneID; 461132; -.
DR KEGG; ptr:461132; -.
DR CTD; 51056; -.
DR VGNC; VGNC:625; LAP3.
DR eggNOG; KOG2597; Eukaryota.
DR GeneTree; ENSGT00530000063255; -.
DR HOGENOM; CLU_013734_1_2_1; -.
DR OMA; MVTMKAD; -.
DR OrthoDB; 2899215at2759; -.
DR TreeFam; TF314954; -.
DR Proteomes; UP000002277; Chromosome 4.
DR Bgee; ENSPTRG00000015938; Expressed in liver and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963:SF39; 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 2: Evidence at transcript level;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:BAK63154.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT DOMAIN 362..369
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 519 AA; 56166 MW; D960F8F5B9024585 CRC64;
MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD
KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN
IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS
GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI
EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV
DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE
ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL
DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA
//
