ID   PPCEL_XENLA             Reviewed;         707 AA.
AC   Q32N48;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Prolyl endopeptidase-like;
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q8C167};
DE   AltName: Full=Prolylendopeptidase-like;
GN   Name=prepl;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine peptidase whose precise substrate specificity remains
CC       unclear (By similarity). Does not cleave peptides after a arginine or
CC       lysine residue (By similarity). Regulates trans-Golgi network
CC       morphology and sorting by regulating the membrane binding of the AP-1
CC       complex (By similarity). May play a role in the regulation of synaptic
CC       vesicle exocytosis (By similarity). {ECO:0000250|UniProtKB:Q4J6C6}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4J6C6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q4J6C6}.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; BC108840; AAI08841.1; -; mRNA.
DR   RefSeq; NP_001167499.1; NM_001174028.1.
DR   AlphaFoldDB; Q32N48; -.
DR   SMR; Q32N48; -.
DR   ESTHER; xenla-q32n48; S9N_PREPL_Peptidase_S9.
DR   MEROPS; S09.015; -.
DR   DNASU; 100381109; -.
DR   GeneID; 100381109; -.
DR   KEGG; xla:100381109; -.
DR   CTD; 100381109; -.
DR   Xenbase; XB-GENE-6466521; prepl.L.
DR   OrthoDB; 1124637at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 100381109; Expressed in ovary and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..707
FT                   /note="Prolyl endopeptidase-like"
FT                   /id="PRO_0000314866"
FT   ACT_SITE        538
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT   ACT_SITE        624
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT   ACT_SITE        670
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
SQ   SEQUENCE   707 AA;  80168 MW;  580DA8CFB1557915 CRC64;
     MMRNLAQQVG LFVCRISSGT SAWNSVISAS YFSAGITRYS RSTVYRGYKA WQNLLDSEKR
     RWQRACAKYQ GLVTSLEKRL CDMHQSYSTG DEKGMIIYED YIYFQDNGCI CRYKPNTGED
     SLEVLLISED LGLGDYEIQK IRVSPKQKFM AVTLKGYERE ESTCVVVKLD NGPQVTHCIE
     NVFSCEWATD RMLLHTSQVN VQCRQVFATD FSDANGAAQL VYTENDPRFF VDLYCTRDKR
     FITINSNSKS TSEVRLIDNR CPFEPPVLVQ KRIAGVIYYI EHSNGCLYML RRHGEAAEYK
     ILKAAVSSGM KHWEPVYEVQ ERTKLVDMEM LKDHCLLFLK NHNQLSLEVI GLPSGAVLQS
     IKLPAWACAL ELDHQAEYGA GTVGFSLSSP VHPPVHFEYS LRKKQLSVDT NHSSDGIHQF
     HTLRLEAKSK DGTSVPLTLL YKDSEKQMRQ RPLLIHVYGA YGMDLNMSFK VEKRMLVEEG
     WLLAYCHVRG GGELGCNWHS EGVLDKKLNG LEDLGSCISH LHGLGYSQPH YSAVEAASAG
     GVLAGALCNS APRLFRAVVL EAPFLDVLNT MMNVSLPLTI EEQEEWGNPL SDEKYHRYIK
     SYCPYQNITP QNYPCVRITA YENDQRVPIQ GLLGYITRLR KAARDYCHES GTSESRIPHI
     YLDVHPGGSH CDSLSWEESL RKVATQLAFL HMELKLDIPR RCKGSTQ