PGPI_MOUSE
ID PGPI_MOUSE Reviewed; 209 AA.
AC Q9ESW8;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
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; Synonyms=Pgpi;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12651114; DOI=10.1016/s1046-5928(02)00632-0;
RA Dando P.M., Fortunato M., Strand G.B., Smith T.S., Barrett A.J.;
RT "Pyroglutamyl-peptidase I: cloning, sequencing, and characterisation of the
RT recombinant human enzyme.";
RL Protein Expr. Purif. 28:111-119(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline. {ECO:0000250}.
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};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
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DR EMBL; AJ278829; CAC03615.1; -; mRNA.
DR EMBL; AK003373; BAB22746.1; -; mRNA.
DR EMBL; AK012658; BAB28388.1; -; mRNA.
DR EMBL; AK047835; BAC33170.1; -; mRNA.
DR EMBL; AK049632; BAC33848.1; -; mRNA.
DR EMBL; BC051938; AAH51938.1; -; mRNA.
DR CCDS; CCDS22377.1; -.
DR RefSeq; NP_075706.1; NM_023217.4.
DR AlphaFoldDB; Q9ESW8; -.
DR SMR; Q9ESW8; -.
DR BioGRID; 211533; 1.
DR STRING; 10090.ENSMUSP00000070778; -.
DR MEROPS; C15.010; -.
DR iPTMnet; Q9ESW8; -.
DR PhosphoSitePlus; Q9ESW8; -.
DR SwissPalm; Q9ESW8; -.
DR EPD; Q9ESW8; -.
DR jPOST; Q9ESW8; -.
DR MaxQB; Q9ESW8; -.
DR PaxDb; Q9ESW8; -.
DR PeptideAtlas; Q9ESW8; -.
DR PRIDE; Q9ESW8; -.
DR ProteomicsDB; 289479; -.
DR Antibodypedia; 28025; 108 antibodies from 22 providers.
DR DNASU; 66522; -.
DR Ensembl; ENSMUST00000070173; ENSMUSP00000070778; ENSMUSG00000056204.
DR GeneID; 66522; -.
DR KEGG; mmu:66522; -.
DR UCSC; uc009mbc.2; mouse.
DR CTD; 54858; -.
DR MGI; MGI:1913772; Pgpep1.
DR VEuPathDB; HostDB:ENSMUSG00000056204; -.
DR eggNOG; KOG4755; Eukaryota.
DR GeneTree; ENSGT00390000015368; -.
DR HOGENOM; CLU_043960_3_1_1; -.
DR InParanoid; Q9ESW8; -.
DR OMA; KLAYNHK; -.
DR OrthoDB; 1248044at2759; -.
DR PhylomeDB; Q9ESW8; -.
DR TreeFam; TF313278; -.
DR BRENDA; 3.4.19.3; 3474.
DR SABIO-RK; Q9ESW8; -.
DR BioGRID-ORCS; 66522; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9ESW8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ESW8; protein.
DR Bgee; ENSMUSG00000056204; Expressed in right kidney and 224 other tissues.
DR ExpressionAtlas; Q9ESW8; baseline and differential.
DR Genevisible; Q9ESW8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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_0000184762"
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; 22934 MW; F8CD222CD61AE853 CRC64;
MEQPRKAVVV TGFGPFGEHT VNASWIAVQE LEKLGLGDSV DLHVYEIPVE YQTVQRLIPA
LWEKHSPQLV VHVGVSGMAT TVTLEKCGHN KGYKGLDNCR FCPGSQCCVE DGPESIDSII
DMDAVCKRVT TLGLDVSVTI SQDAGRYLCD FTYYTSLYQG RGRSAFVHVP PLGKPYNADQ
LGRALRAIIE EMLGVLEQAE GDISCCRQL
