ID   PHO10_CAEEL             Reviewed;         411 AA.
AC   Q09448;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Putative acid phosphatase 10;
DE            EC=3.1.3.2;
GN   Name=pho-10; ORFNames=C05C10.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; Z48178; CAA88204.2; -; Genomic_DNA.
DR   PIR; T18944; T18944.
DR   RefSeq; NP_496140.2; NM_063739.2.
DR   AlphaFoldDB; Q09448; -.
DR   SMR; Q09448; -.
DR   STRING; 6239.C05C10.1.1; -.
DR   PaxDb; 6239-C05C10-1; -.
DR   EnsemblMetazoa; C05C10.1.1; C05C10.1.1; WBGene00007328.
DR   GeneID; 182251; -.
DR   KEGG; cel:CELE_C05C10.1; -.
DR   UCSC; C05C10.1; c. elegans.
DR   AGR; WB:WBGene00007328; -.
DR   WormBase; C05C10.1; CE42840; WBGene00007328; pho-10.
DR   eggNOG; KOG3720; Eukaryota.
DR   GeneTree; ENSGT00940000168803; -.
DR   HOGENOM; CLU_030431_2_0_1; -.
DR   InParanoid; Q09448; -.
DR   OrthoDB; 5477542at2759; -.
DR   PhylomeDB; Q09448; -.
DR   Reactome; R-CEL-1483166; Synthesis of PA.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   PRO; PR:Q09448; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00007328; Expressed in embryo and 1 other cell type or tissue.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   CDD; cd07061; HP_HAP_like; 1.
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:SF181; ACID PHOSPHATASE 10-RELATED; 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.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Reference proteome.
FT   CHAIN           1..411
FT                   /note="Putative acid phosphatase 10"
FT                   /id="PRO_0000114468"
FT   ACT_SITE        33
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        379..385
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  46600 MW;  A18761D5232B00C3 CRC64;
     MFLSLFCVII VAVGCSSKDG NVKLEFVQAM WRHGERSALA DLYPIYEKDW VFGGGGLGEL
     TGRGMGEMNN LGRLIRERYV RKFNFLEPKY ASKEVYFRST NLNRTIISAM SLLYGLFPPS
     LYDIPNVDYP FTPLKWLPGL AFVPVHVDGS DQCAASQNCP CPRYDFLQQQ MLTLPEVQQA
     FQQVILLNRQ IAPLYNVTTG VDTFYVYPDT WKCQRAYFNK TMYDKLPWYN EQLYSKAEIT
     YAPIKGFLEG SFSQPAVTSN GLDVAFEIQQ VRSGVMINEI VSRASEKLNC VERGQNCTSY
     LNKLKFYGYS IHDNNVYAVL VALGIPHISA TEDGWPSYAA AIFFEFYRNS QTNKRLFKVL
     YRQDASSQIT DVTSQVPMCQ GVSMCPLSTF QHLADVLKPI PDINTVCNIT S
//