ID   PGPI_RAT                Reviewed;         209 AA.
AC   Q76IC5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Pyroglutamyl-peptidase 1;
DE            EC=3.4.19.3;
DE   AltName: Full=5-oxoprolyl-peptidase;
DE   AltName: Full=Pyroglutamyl aminopeptidase I;
DE            Short=PAP-I;
DE   AltName: Full=Pyroglutamyl-peptidase I;
DE            Short=PGP-I;
DE   AltName: Full=Pyrrolidone-carboxylate peptidase;
GN   Name=Pgpep1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=Fischer 344/DuCrj; TISSUE=Liver;
RX   PubMed=14600395; DOI=10.1248/bpb.26.1528;
RA   Abe K., Watanabe N., Kosaka T., Yamada M., Tokui T., Ikeda T.;
RT   "Hydrolysis of synthetic substrate, L-pyroglutamyl p-nitroanilide is
RT   catalyzed solely by pyroglutamyl aminopeptidase I in rat liver cytosol.";
RL   Biol. Pharm. Bull. 26:1528-1533(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline. {ECO:0000269|PubMed:14600395}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal pyroglutamyl group from a
CC         polypeptide, the second amino acid generally not being Pro.;
CC         EC=3.4.19.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU10076,
CC         ECO:0000255|PROSITE-ProRule:PRU10077, ECO:0000269|PubMed:14600395};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14600395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14600395}.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR   EMBL; BC098645; AAH98645.1; -; mRNA.
DR   EMBL; AB098134; BAD01533.1; -; mRNA.
DR   RefSeq; NP_973717.1; NM_201988.2.
DR   AlphaFoldDB; Q76IC5; -.
DR   SMR; Q76IC5; -.
DR   STRING; 10116.ENSRNOP00000026597; -.
DR   MEROPS; C15.010; -.
DR   jPOST; Q76IC5; -.
DR   PaxDb; Q76IC5; -.
DR   PRIDE; Q76IC5; -.
DR   Ensembl; ENSRNOT00000026597; ENSRNOP00000026597; ENSRNOG00000019639.
DR   GeneID; 290648; -.
DR   KEGG; rno:290648; -.
DR   UCSC; RGD:1303133; rat.
DR   CTD; 54858; -.
DR   RGD; 1303133; Pgpep1.
DR   eggNOG; KOG4755; Eukaryota.
DR   GeneTree; ENSGT00390000015368; -.
DR   HOGENOM; CLU_043960_3_1_1; -.
DR   InParanoid; Q76IC5; -.
DR   OMA; KLAYNHK; -.
DR   OrthoDB; 1248044at2759; -.
DR   PhylomeDB; Q76IC5; -.
DR   TreeFam; TF313278; -.
DR   BRENDA; 3.4.19.3; 5301.
DR   PRO; PR:Q76IC5; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000019639; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; Q76IC5; RN.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0008233; F:peptidase activity; IDA:RGD.
DR   GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00501; Peptidase_C15; 1.
DR   Gene3D; 3.40.630.20; -; 1.
DR   InterPro; IPR000816; Peptidase_C15.
DR   InterPro; IPR016125; Peptidase_C15-like.
DR   InterPro; IPR036440; Peptidase_C15-like_sf.
DR   InterPro; IPR029761; PGP-I_metazoa.
DR   InterPro; IPR033694; PGPEP1_Cys_AS.
DR   InterPro; IPR033693; PGPEP1_Glu_AS.
DR   PANTHER; PTHR23402; PTHR23402; 1.
DR   PANTHER; PTHR23402:SF16; PTHR23402:SF16; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; SSF53182; 1.
DR   PROSITE; PS01334; PYRASE_CYS; 1.
DR   PROSITE; PS01333; PYRASE_GLU; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..209
FT                   /note="Pyroglutamyl-peptidase 1"
FT                   /id="PRO_0000334693"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   209 AA;  22913 MW;  A9C058F7A7D71D5A CRC64;
     MEQPRKAVVV TGFGPFGEHA VNASWIAVQE LEKLGLGDSV DLHVYEIPVE YQTVQRLIPA
     LWEKHSPQLV VHVGVSGMAT TVTLEKCGHN KGYKGLDNCR FCPGSQCCVE DGPESIDSII
     DMDAVCKRVT TLGLDVSVTI SQDAGRYLCD FTYYTSLYRG RGRSAFVHVP PLGKPYNADQ
     LGRALRAIIE EMLGVLEQAE GDISCCHQL