ID   PLCX1_ARTBC             Reviewed;         305 AA.
AC   D4AK17;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=PI-PLC X domain-containing protein 1;
DE   Flags: Precursor;
GN   ORFNames=ARB_04618;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
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DR   EMBL; ABSU01000001; EFE37090.1; -; Genomic_DNA.
DR   RefSeq; XP_003017735.1; XM_003017689.1.
DR   AlphaFoldDB; D4AK17; -.
DR   EnsemblFungi; EFE37090; EFE37090; ARB_04618.
DR   GeneID; 9522581; -.
DR   KEGG; abe:ARB_04618; -.
DR   eggNOG; KOG4306; Eukaryota.
DR   HOGENOM; CLU_037358_2_1_1; -.
DR   OMA; NGHPEYC; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   SUPFAM; SSF51695; SSF51695; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal; Transducer.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..305
FT                   /note="PI-PLC X domain-containing protein 1"
FT                   /id="PRO_5003053779"
FT   DOMAIN          25..189
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   305 AA;  33966 MW;  2A729CB34DA308B8 CRC64;
     MSMSTLRHFL WLGALLLATI QVSALPTAQD LICNGHPEYC DRRYSELSFV GAHNSPFVGP
     LLQHNQDISV TEQLDFGIRF LQGQTHKNDD GVFSMCHTSC ILEDAGSVSS YLQTVKTWLD
     SHPNEVVTLL ITNGDGLDIK EFDDAFNAVN GIKDYTFAPK SKLALGDWPT LRELITTGKR
     LIVFVDSKAD TNRFPYLLDE FSYYFETPFS TTDENFPQCK LDRPAGGKPD GQMYLVNHTL
     NVNVFGIFLP DRFKAGRTNA AVGQGSIGAQ VDLCNSIYHR KPNVVLLDFI TEGDVLKAER
     TMNGL