PLB1_CRYNJ
ID PLB1_CRYNJ Reviewed; 637 AA.
AC P0CP74; Q55ID9; Q5K7X8; Q9P8L1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Phospholipase B;
DE EC=3.1.1.5;
DE AltName: Full=Lysophospholipase;
DE Flags: Precursor;
GN Name=PLB1; Synonyms=PLB; OrderedLocusNames=CNM00920;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Exhibits phospholipase B (PLB), lysophospholipase (LPL) and
CC lysophospholipase/transacylase (LPTA) activities. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; AE017353; AAW46882.1; -; Genomic_DNA.
DR RefSeq; XP_568399.1; XM_568399.1.
DR AlphaFoldDB; P0CP74; -.
DR SMR; P0CP74; -.
DR STRING; 5207.AAW46882; -.
DR PaxDb; P0CP74; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; P0CP74; -.
DR OMA; FGTWDPT; -.
DR OrthoDB; 564952at2759; -.
DR Proteomes; UP000002149; Chromosome 13.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..637
FT /note="Phospholipase B"
FT /id="PRO_0000024635"
FT DOMAIN 46..572
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
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 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 637 AA; 68594 MW; ADBEEF88100BA6B1 CRC64;
MSIITTAFAL SLLATTAFAV PPETPRIELQ AERGLGDQSY APWQVDCPSN VTWIRNATTG
LGTGERAYIE AREKLVQPAI EQMMAARGLE TPPRTPVIGV ALAGGGYRAM LTGLGGIMGM
MNESTEASQS ETGGWLDGVS YWSGLSGGSW ATGSFMSNGG QLPTTLLENL WNIDSNLVFP
DDGKLSFYTN LYTETNAKSD LGFPVQITDI WGLAIGSHVL PEPYQLSNTP NLTFSSLPSV
VAALGNASLP MPIIVAADRK RREAGELVIA ENATVWEFTP YEFGSWAFGS QYKSPGAFTP
IEYLGTSVDD GSPNGTCWKG FDQLSFVMGT SATLFNGAFL ELNGTDSGLL TNLITAFLAD
LGEDQADISR IPNSFSNYNS GENPIYNLTY ITLVDAGETN QNIPLEPLLV PTRDVDAIVA
FDSSYDSDYI WPNGTALRTT YERAKILAEH ENTRVLMPEV PSMNGFVNGG YNSRPTFFGC
NDTTTPVIIY IPSYPWSFAA NTSTYQLSYE NNEANEMLLN GMRSLTLNHS VPTWPTCFAC
ALTDRSFMYT SENRSTTCQE CFDTWCWAGD DNTTEPANYE PVINSVPPWL IANNLSIGMA
DAPGSNESTA GTASSGAAKM GVGMGMVALT AGLGLML
