ID   PHO5_CAEEL              Reviewed;         422 AA.
AC   Q10944;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 3.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Putative acid phosphatase 5;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=pho-5; ORFNames=B0361.7;
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).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
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; FO080185; CCD61822.1; -; Genomic_DNA.
DR   RefSeq; NP_498604.2; NM_066203.7.
DR   AlphaFoldDB; Q10944; -.
DR   SMR; Q10944; -.
DR   STRING; 6239.B0361.7; -.
DR   iPTMnet; Q10944; -.
DR   EPD; Q10944; -.
DR   PaxDb; Q10944; -.
DR   PeptideAtlas; Q10944; -.
DR   EnsemblMetazoa; B0361.7.1; B0361.7.1; WBGene00015161.
DR   EnsemblMetazoa; B0361.7.2; B0361.7.2; WBGene00015161.
DR   GeneID; 176030; -.
DR   KEGG; cel:CELE_B0361.7; -.
DR   UCSC; B0361.7; c. elegans.
DR   CTD; 176030; -.
DR   WormBase; B0361.7; CE32100; WBGene00015161; pho-5.
DR   eggNOG; KOG3720; Eukaryota.
DR   GeneTree; ENSGT00940000168803; -.
DR   HOGENOM; CLU_030431_1_1_1; -.
DR   InParanoid; Q10944; -.
DR   OMA; YDFENIW; -.
DR   OrthoDB; 1221585at2759; -.
DR   PhylomeDB; Q10944; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   PRO; PR:Q10944; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00015161; Expressed in adult organism and 4 other tissues.
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; -; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..422
FT                   /note="Putative acid phosphatase 5"
FT                   /id="PRO_0000023968"
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        279
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   DISULFID        152..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        205..302
FT                   /evidence="ECO:0000250"
FT   DISULFID        338..342
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  48409 MW;  3E29FACB4FAE0CAC CRC64;
     MLLLLVLLIG ASGINAVVYK EVPIQANTDT LEYVHTVWRH GDRTPAELLF PDDITKWPEG
     LGELTEQGAA QQYRLGQWLK RRYGSWLGEK FNRNAIYIRS SDYNRTLMSA QANMAGLFPP
     KYPIAGGLMW QPIPVHTISK PTDKELYEEA SCPTAEIEMN AQWKSTKANG IRKKFARELS
     FFSQKLNLPN MELKATWRIF DNLFCEKQNN ITWPSWMNSS IFERVDQLYN EVSQLEFHTD
     TLRRLRGGTL LEEIFHRFSD KASGSLGKEA KFYAYSAHDS TIAALLATLG VFYDIYPKYA
     TCLLIEMHKL ANETRLIRVF HKNETDIDRL IEYSIPGCDD PCTLQKLGDD LKKYFPEDWE
     AECGLKTSFQ FIYLVIISIL VISTVCSCTM LFVEKQKRKI LRFPVDGLRD DTAPMLGGDD
     SD