PLB1_ARTBC
ID PLB1_ARTBC Reviewed; 643 AA.
AC D4ANV2;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Lysophospholipase ARB_05919 {ECO:0000305};
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:P39105};
DE AltName: Full=Phospholipase B {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_05919;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids
CC (By similarity). Phospholipase B may well contribute to pathogenicity
CC by abetting the fungus in damaging host cell membranes (By similarity).
CC {ECO:0000250|UniProtKB:P39105, ECO:0000250|UniProtKB:Q9UWF6}.
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 Evidence={ECO:0000250|UniProtKB:P39105};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; ABSU01000004; EFE34963.1; -; Genomic_DNA.
DR RefSeq; XP_003015608.1; XM_003015562.1.
DR AlphaFoldDB; D4ANV2; -.
DR SMR; D4ANV2; -.
DR STRING; 663331.D4ANV2; -.
DR EnsemblFungi; EFE34963; EFE34963; ARB_05919.
DR GeneID; 9525889; -.
DR KEGG; abe:ARB_05919; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR OMA; FGTWDPT; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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 Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..643
FT /note="Lysophospholipase ARB_05919"
FT /evidence="ECO:0000255"
FT /id="PRO_5001437818"
FT DOMAIN 50..597
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 643 AA; 68923 MW; C5A464D2DD1B5AD8 CRC64;
MMFIPATLGT FVLASLLPAT VGAGIPNAAA DVAVRALPNA PDGYAPAEVD CPSTKPAVRS
AAKLSQQEQD WLKKRRMKTT GAMADFFSRV KIEGFDAVAY LVGNADNVAK LPNVAIAVSG
GGYRALMNGA GALKAFDSRT DNSTEPGQLG GLLQSATYLS GLSGGGWLLG SMYVNNDSTI
TELQKGGSNS LWKFNRSILE GPDDGSSGVV DTAEYYKEMI KEISRKKAAG FETSITDIWG
RALSYQLINA PKGGPAYTWS SISQNSKFQS GDVPFPLLVA DGRNPGEKLI GGNATIFEFN
PYEFGTWDPT IFGFVPTQYI GSKFEAGTLP SDEKCVRGMD NAGFIMGTSS SLFNQFALHL
DSQDLPKVVK DSLRDFLSSL DEANNDIAEY KPNPFFGYAK STSPFAGVKS LPVVDGGEDK
QNIPFHPLIQ PARHVDVIFA IDSSADTELA WPNGDSIIAT YQRSLNSTGI ANGTSFPAIP
DNNTFINLGL NHNPTFFGCD SSNTTNPTPL IVYIPNSPYV THSNVSTFNL KYNTTQRDAI
ILNGYNVATM ANATRDGNWP TCVGCAMLSR SLERTKTAVP DACKQCFKMY CWDGTLNSTK
PDVYDPKLFL TEVDLQSAAK GLHASGKLSL VAAVVTLLSI LLV
