ID   PPCEL_CHICK             Reviewed;         732 AA.
AC   Q5ZKL5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Prolyl endopeptidase-like;
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q4J6C6};
DE   AltName: Full=Prolylendopeptidase-like;
GN   Name=PREPL; ORFNames=RCJMB04_10c4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720069; CAG31728.1; -; mRNA.
DR   RefSeq; NP_001026224.1; NM_001031053.1.
DR   AlphaFoldDB; Q5ZKL5; -.
DR   SMR; Q5ZKL5; -.
DR   STRING; 9031.ENSGALP00000040816; -.
DR   ESTHER; chick-q5zkl5; S9N_PREPL_Peptidase_S9.
DR   MEROPS; S09.015; -.
DR   PaxDb; Q5ZKL5; -.
DR   GeneID; 421405; -.
DR   KEGG; gga:421405; -.
DR   CTD; 9581; -.
DR   VEuPathDB; HostDB:geneid_421405; -.
DR   eggNOG; KOG2237; Eukaryota.
DR   InParanoid; Q5ZKL5; -.
DR   OrthoDB; 1124637at2759; -.
DR   PhylomeDB; Q5ZKL5; -.
DR   PRO; PR:Q5ZKL5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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..732
FT                   /note="Prolyl endopeptidase-like"
FT                   /id="PRO_0000314865"
FT   ACT_SITE        575
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT   ACT_SITE        661
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT   ACT_SITE        707
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q4J6C6"
SQ   SEQUENCE   732 AA;  84313 MW;  B9FE3D9A11CCAAE1 CRC64;
     MCWTAKSFVR WLSSSVKYYP KDNHLQALCL CTKTKLNKCH ILDWSRSPCN SAVPPGRILS
     WRLFSCKEGT KDLCKREKIA SVTASELLYK DLLKSEQENW NKISRSYKAM TKRIKEKIEE
     LHNKYTLHLE SPRMRFGGNV YFEENGYILC SKADDDKGNV HILFSTEDMG FSGAYIKRIR
     ISPDERYLAT SLQSENSEEA TCVIMKLGDV PFVEEVIPNV FSFEWATNDV LYYTSQKNLK
     CQNVFMTTFT NEKYTKLVYT EQDARFFVDI YCTKDRRFLT INSNSKTTSE VWLIDCRHPF
     KLPVLVQART KGVIYHVEHR NNELYILTSY GEPAEYKLMK ASVASTGMEN WQLVYALEEK
     TKLIDLEMFR DHCIMFLQKA GYLYLNVIAF VSHSVQSIQL PTWACAFELE SHPEHASSTC
     YFQLTSPVHP PRRFAYSFKE NNLIEQAAEE VPIIMNCHTT RLLAKSKDET LVPITVFHNV
     NSKELHRKPL LVHVYGAYGI DLNMSFKEEK LMLIEEGWIL AYCHVRGGGE LGLRWHKDGC
     QQNKLKGLHD LKACIMLLHE LGFSQPKYTA LTAVSAGGVL AGAICNSDPE LIRAVVLQAP
     FVDVLNTMMK THLPLSIEEQ EEWGNPLADE KCMKYIKNYC PYHNIKPQCY PSVFITAYEN
     DQRVPLTGIL RYVQKLRKAT LDHASRTRKK GNWIPNIILD IQASGSHCDS SWEDSLNEVA
     RHLAFLKKEL QV