ID   POPA_AMABI              Reviewed;         761 AA.
AC   E2JFG1;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Prolyl oligopeptidase A {ECO:0000303|PubMed:20889720};
DE            EC=3.4.21.26 {ECO:0000305|PubMed:20889720};
GN   Name=POPA {ECO:0000303|PubMed:20889720};
OS   Amanita bisporigera (Destroying angel).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=87325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=20889720; DOI=10.1128/ec.00161-10;
RA   Luo H., Hallen-Adams H.E., Scott-Craig J.S., Walton J.D.;
RT   "Colocalization of amanitin and a candidate toxin-processing prolyl
RT   oligopeptidase in Amanita basidiocarps.";
RL   Eukaryot. Cell 9:1891-1900(2010).
CC   -!- FUNCTION: Housekeeping prolyl oligopeptidase (POP) that behaves like a
CC       conventional POP by cleaving peptide bonds on the C-terminal side of
CC       prolyl residues within peptides that are up to approximately 30 amino
CC       acids long (By similarity). {ECO:0000250|UniProtKB:H2E7Q7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48147}.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; HQ225840; ADN19204.1; -; mRNA.
DR   AlphaFoldDB; E2JFG1; -.
DR   SMR; E2JFG1; -.
DR   BRENDA; 3.4.21.26; 12947.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Serine protease.
FT   CHAIN           1..761
FT                   /note="Prolyl oligopeptidase A"
FT                   /id="PRO_0000443714"
FT   ACT_SITE        606
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        690
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        726
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ   SEQUENCE   761 AA;  86914 MW;  6975DD956A3FDD62 CRC64;
     MHRFLQPVRE RLRSALARYF GSRIMSSTQW TPNMYPSARR SDHIDTYRSE TRGEVKVPDP
     YHWLEEYSEE TDKWTSDQEE FTRTYLDSNP DRKKLEDAFR KSMDYPKFSA PFLNDDKRWY
     WFYNTGLQAQ TVICRSKDET LPDFSESDYV GETFFDPNLL SSDGTASLSM YDFSHCGKYF
     AYGISLSGSD FSTIYVRSTS SPLAPGNNSI RNDDGRLPDE LRYVKFSSIS WTKDSKGFFY
     QRYPGTGTVN GQNGIQTQGD RDAMIYYHRI GTSQSDDILV HEDQEHPDWV FGAEVTEDGK
     YVALYTMKDT SRKNLLWIAD LGQNEVGRNM KWNKICNVFD SEYDLIGNDG SLLYIRTNKA
     APQYKIVTLD IEKPELGFKE FIPEDPKAYL SQVKIFNKDR LALVYKRNVI GELYVYNNTG
     SRLMRLARDF VGSMTVTARE TEPWFFATLT GFNTPGIVCR YNIQRPEEQR WSVYRTAKVK
     GLNPNDFEAR QVWYDSYDGT KIPMFIVRHK NTQFNGTAPA IQYGYGGFNI SINPFFSPTI
     LTFLQKYGAI LAVPNIRGGG EFGETWHDAG IREKRANVYD DFIAATQFLV KNKYAAGGKV
     AINGGSNGGL LVAACVNRAR EGTFGAAIAE VGVLDLLKFP KFTIGKAWIS DYGDPEDPRD
     FDYIYTHSPL HNIPKNMVLP PTMLLTADHD DRVVPMHSFK YAAMLQYTLP HNRHPLLLRV
     DKKAGHGGGK STEKRLQEAA DKWGFAAQSM GLAWKDRQAN L