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Database: UniProt
Entry: A0A0L0BQU1_LUCCU
LinkDB: A0A0L0BQU1_LUCCU
Original site: A0A0L0BQU1_LUCCU 
ID   A0A0L0BQU1_LUCCU        Unreviewed;       580 AA.
AC   A0A0L0BQU1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=2-phosphoxylose phosphatase 1 {ECO:0000256|ARBA:ARBA00040357};
DE   AltName: Full=Acid phosphatase-like protein 2 {ECO:0000256|ARBA:ARBA00041499};
GN   ORFNames=FF38_04665 {ECO:0000313|EMBL:KNC22397.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC22397.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC22397.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC22397.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC22397.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC         beta-D-2-O-P-Xyl]-L-seryl-[protein] + H2O = 3-O-(beta-D-GlcA-(1->3)-
CC         beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:56512, Rhea:RHEA-COMP:12573, Rhea:RHEA-
CC         COMP:14559, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:132093,
CC         ChEBI:CHEBI:140495; Evidence={ECO:0000256|ARBA:ARBA00036311};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000032};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNC22397.1}.
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DR   EMBL; JRES01001507; KNC22397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0BQU1; -.
DR   STRING; 7375.A0A0L0BQU1; -.
DR   EnsemblMetazoa; KNC22397; KNC22397; FF38_04665.
DR   OMA; DWEWNYY; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF125; 2-PHOSPHOXYLOSE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   580 AA;  65849 MW;  418E9ABBB5296B85 CRC64;
     MFLKELIRFS TQHRTLYCYL ILSIWIFLLI AGMYKYIGRS SSSLSYILNG KSQYYASVMT
     AAPSRETSNF AKYKARCTSL SQINRLDDGG ILDGWKLQGV LLVIRHGDRG PMSHVRNIPH
     LDCGITGDNL VNKYRSFLYN STSASGSNHM YWNKVGPFHS FPLLPLAEKE CLLGQLTYKG
     IAQLLHVGET LHQIYAHPLG LWYKQSNSQY GKNVMNSTPY STLLNSDEVV VYSTRVRRTF
     QSALALLYTF LPTDKWLALN VKESHSIAFC FSDCACPQAD SLRKELIKMQ KQRLTQQPMV
     ANVMHWIGNQ LLQHTPNGIN DPNEVVDAML TVMCHDAPWP CRNVNGSERT VVSTKANDVD
     LNDVINIDQD DMAIGEGGRV EDIASNLIEL HNGNLEAPTA TAEGCIESHH VSTLMSFSNW
     QSTREVHHAY YKRIGLMRAY GMIRHIVSYM LRMISGDRTK FVLYSGHDWT LQYLTAALGI
     QTDNTFIAYA ARLAFEVYKS EAHTDYYFRV VYDGHDVTKQ IDFCEGGKSL RVTRDSRGNK
     ADLCPIENII RFLHEDYFGP LNATNFKDAC ILQQQKPNEF
//
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