ID   PLB1_TORDE              Reviewed;         649 AA.
AC   Q11121;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Lysophospholipase;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B;
DE   Flags: Precursor;
OS   Torulaspora delbrueckii (Yeast) (Candida colliculosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Torulaspora.
OX   NCBI_TaxID=4950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=YL-32;
RX   PubMed=8001766; DOI=10.1111/j.1574-6968.1994.tb07257.x;
RA   Watanabe Y., Yashiki Y., Sultana G.N., Maruyama M., Kangawa K., Tamai Y.;
RT   "Cloning and sequencing of phospholipase B gene from the yeast Torulaspora
RT   delbrueckii.";
RL   FEMS Microbiol. Lett. 124:29-34(1994).
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   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D32134; BAA06860.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11121; -.
DR   SMR; Q11121; -.
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; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Secreted; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..649
FT                   /note="Lysophospholipase"
FT                   /id="PRO_0000024645"
FT   DOMAIN          34..584
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        563
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   649 AA;  71111 MW;  CC6901D168D01459 CRC64;
     MNLKEWLLFS DAVFFAQGTL AWSPSNSYTP ANVSCDEDIN LIRQASGPSD NETEWLKKRD
     VYTREALRSF LDRATSNFSD SSLVSQLFSN ASDIPRIAVA CSGGGYRAML SGAGMLAAMD
     NRTDGANEHG LGGLLQSTTY LAGLSGGNWL VGTLAWNNWT SVQDIVNNMT EDDSIWDISN
     SIINPGGFMI VTTIKRWDHI SDAVEGKQDA GFNVSLTDIW GRALSYNFFP SLYRGGVAYT
     WSTLRDVEVF QNGEMPFPIS VADGRYPGTQ IIDLNATVFE FNPFEMGSWD PTLNAFTDVK
     YLGTKVSNGE PVNKGQCVAG YDNTGFIMGT SSSLFNQFLL QINSTSLPSF IKNLVTGFLD
     DLSEDEDDIA IYAPNPFKDT SYIQDNFSKS ISESDYLYLV DGGEDNQNIP LVPLVQDERN
     VDVIFALDNS ADTDYYWPDG ASLVSTYERQ FSSQGLNMSF PYVPDKRTFV NLGLADKPSF
     FGCDAQNLTD LNYIPPLVVY IPNARHSYNS NTSTFKLSYT DDERLKMIKN GFEAATRGNL
     TDDSSFMGCV ACAVMRRKQQ SLNATLPEEC STCFTNYCWN GTIDDTPVSG LDNSDFDPTA
     ASSAYSAYNT ESYSSSSATG SKKNGAGLPA TPTSFTSILT LLTAIAGFL