ID G1U2T7_RABIT Unreviewed; 209 AA.
AC G1U2T7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|ARBA:ARBA00012915, ECO:0000256|PROSITE-ProRule:PRU10076};
DE EC=3.4.19.3 {ECO:0000256|ARBA:ARBA00012915, ECO:0000256|PROSITE-ProRule:PRU10076};
GN Name=PGPEP1 {ECO:0000313|Ensembl:ENSOCUP00000023690.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000023690.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000023690.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000023690.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000023690.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline. {ECO:0000256|ARBA:ARBA00002280}.
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:0000256|ARBA:ARBA00001770,
CC ECO:0000256|PROSITE-ProRule:PRU10076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
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DR RefSeq; XP_002724291.1; XM_002724245.3.
DR AlphaFoldDB; G1U2T7; -.
DR MEROPS; C15.010; -.
DR PaxDb; 9986-ENSOCUP00000023690; -.
DR Ensembl; ENSOCUT00000029570.3; ENSOCUP00000023690.2; ENSOCUG00000025762.3.
DR GeneID; 100351225; -.
DR KEGG; ocu:100351225; -.
DR CTD; 54858; -.
DR eggNOG; KOG4755; Eukaryota.
DR GeneTree; ENSGT00390000015368; -.
DR HOGENOM; CLU_043960_3_1_1; -.
DR OMA; KLAYNHK; -.
DR OrthoDB; 5490159at2759; -.
DR TreeFam; TF313278; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000025762; Expressed in kidney and 19 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00501; Peptidase_C15; 1.
DR Gene3D; 3.40.630.20; Peptidase C15, pyroglutamyl peptidase I-like; 1.
DR InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR InterPro; IPR033694; PGPEP1_Cys_AS.
DR InterPro; IPR033693; PGPEP1_Glu_AS.
DR PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR PANTHER; PTHR23402:SF16; PYROGLUTAMYL-PEPTIDASE 1; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
DR PROSITE; PS01333; PYRASE_GLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10076"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10077"
SQ SEQUENCE 209 AA; 23063 MW; 8E9B4F076702D312 CRC64;
MEQPRKAVVV TGFGPFGEHT VNASWIAVQE LEKLGLGDSV DLHVYEIPVE YKTVQRLIPA
LWEKHSPQLV VHVGVSGMAT TVTLEKCGHN KGYKGLDNRH FCPGSQCCVE DGPESIDSVI
DMDAVCERLT ELGLDVTVTI SQDAGRYLCD FTYYTSLYQG HGRSAFVHVP PLGKPYNADQ
LGRALRVIIA EMLGVLEQSD RQGSCCRQR
//
