ID   PPCEL_MACFA             Reviewed;         727 AA.
AC   A5LFV8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Prolyl endopeptidase-like;
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q4J6C6};
DE   AltName: Full=Prolylendopeptidase-like;
GN   Name=PREPL; ORFNames=QtsA-11414;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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 (By similarity). Interacts with the AP-1 complex (By
CC       similarity). {ECO:0000250|UniProtKB:Q4J6C6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q4J6C6}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:Q8C167}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q8C167}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q8C167}. Nucleus {ECO:0000250|UniProtKB:Q4J6C6}.
CC       Note=Co-localizes with AP-1 in the trans-Golgi network (By similarity).
CC       Co-localizes with MAP2 and ACTB on the cytoskeleton (By similarity).
CC       Co-localizes with STX6 and GOSR2 at the Golgi apparatus (By
CC       similarity). {ECO:0000250|UniProtKB:Q8C167}.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; AB168347; BAF63643.1; -; mRNA.
DR   AlphaFoldDB; A5LFV8; -.
DR   SMR; A5LFV8; -.
DR   STRING; 9541.XP_005576034.1; -.
DR   ESTHER; macfa-ppcel; S9N_PREPL_Peptidase_S9.
DR   MEROPS; S09.015; -.
DR   eggNOG; KOG2237; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
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; Cytoskeleton; Golgi apparatus; Hydrolase; Nucleus; Protease;
KW   Reference proteome; Serine protease.
FT   CHAIN           1..727
FT                   /note="Prolyl endopeptidase-like"
FT                   /id="PRO_0000314861"
FT   ACT_SITE        559
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT   ACT_SITE        645
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT   ACT_SITE        690
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
SQ   SEQUENCE   727 AA;  83993 MW;  4D192063150F8BDD CRC64;
     MQQKTKLFLQ ALKYSIPHLG KCMQKQHLNH YNFADHYYNR IKLKKYHLTK CLQNKPKISE
     LARNIPSRSF SCKDLQPVKQ ENEKPLPENM DAFEKVRTKL ETQPQEEYEI INVEVKHGGF
     VYYQEGCCLV RSKDEEADND NYEVLFNLEE LKLDQPFIDC IRVAPDEKYV AAKIRTEDSE
     ASTCVIIKLS DQPVMEASFP NVSSFEWVKD EEDEDVLFYT FQRNLRCHDV YRATFGDNKR
     NERFYTEKDP SYFVFLYLTK DSRFLTINIM NKTTSEVWLI DGLSPWDPPV LIQKRIHGVL
     YYVEHRDDEL YILTNVGEPT EFKLMRTAAD TPAIMNWDLF FTMKRNTKVI DLDMFKDHCV
     LFLKHSNLLY VNVIGLADDS VRSLKLPPWA CGFIMDTNSD PKNCPFQLCS PIRSPKYYTY
     KFAEGKLFEE TGHEDPITKT SRVLRLEAKS KDGKLVPMTV FHKTDSEDLQ KKPLLIHVYG
     AYGMDLKMNF RPERRVLVDD GWILAYCHVR GGGELGLQWH ADGRLTKKLN GLADLEACIK
     TLHGQGFSQP SLTTLTAFSA GGVLAGALCN CNPELLRAVT LEAPFLDVLN TMMDTTLPLT
     LEELEEWGNP SSDEKHKNYI KRYCPYQNIK PQHYPSVHIT AYENDERVPL KGIVSYTEKL
     KEAISEHAKD TGEGYQAPNI ILDIQPGGNH VIEDSHKKIT AQIKFLYEEL GLDSTSVFED
     LKKYLKF