ID   PLB1_PENCH              Reviewed;         612 AA.
AC   P39457;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Lysophospholipase;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B;
DE   Flags: Precursor; Fragment;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 10-20 AND 185-199.
RC   STRAIN=ATCC 34514 / NBRC 4640;
RX   PubMed=1722456; DOI=10.1111/j.1432-1033.1991.tb16433.x;
RA   Masuda N., Kitamura N., Saito K.;
RT   "Primary structure of protein moiety of Penicillium notatum phospholipase B
RT   deduced from the cDNA.";
RL   Eur. J. Biochem. 202:783-787(1991).
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR   EMBL; X60348; CAA42906.1; -; mRNA.
DR   PIR; S29318; S29318.
DR   AlphaFoldDB; P39457; -.
DR   SMR; P39457; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Secreted; Signal.
FT   SIGNAL          <1..9
FT                   /evidence="ECO:0000269|PubMed:1722456"
FT   CHAIN           10..612
FT                   /note="Lysophospholipase"
FT                   /id="PRO_0000024639"
FT   DOMAIN          24..571
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        477
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        526
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        532
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        571
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        25..?
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   612 AA;  65751 MW;  7C32F819C3C1ABE5 CRC64;
     DITFAGVQRA LPNAPDGYVP TSVSCPASRP TVRSAAKLST NETSWLEVRR GKTLSALKDF
     FGHVKVGDYD VGAYLDKHSG NSSSLPNIGI AVSGGGWRAL MNGAGAVKAF DSRTDNATAT
     GHLGGLLQSA TYISGLSGGS WLLGSIYINN FTTVDKLQTH EAGSVWQFGN SIIEGPDAGG
     IQLLDSAGYY KDLADAVDGK KKAGFDTTLT DIWGRALSYQ MFNASNGGLS YTWSSIADTP
     EFQDGDYPMP FVVADGRNPG ELVIGSNSTV YEFNPWEFGT FDPTIFGFVP LEYLGSKFEG
     GSLPSNESCI RGFDSAGFVI GTSSSLFNQF LLQINTTSLP SFIKDVFNGI LFDLDKSQND
     IASYDPNPFY KYNEHSSPYA AQKLLDVVDG GEDGQNVPLH PLIQPERHVD VIFAVDSSAD
     TDYFWPNGTS LVATYERSLN SSGIANGTAF PAVPDQNTFI NLGLSTRPSF FGCDSSNQTG
     PSPLVVYIPN APYSYHSNIS TFQLSTDDAE RDNIILNGYE VATMANSTLD DNWTACVACA
     ILSRSFERTG TTLPDICSQC FDRYCWNGTV NSTRPESYDP AFYLADNSMA SVSLPTMLST
     VVAAGLAMLI LV