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 27-MAR-2024, entry version 133.
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.B0361.7.1; -.
DR GlyCosmos; Q10944; 5 sites, No reported glycans.
DR iPTMnet; Q10944; -.
DR EPD; Q10944; -.
DR PaxDb; 6239-B0361-7; -.
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 AGR; WB:WBGene00015161; -.
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; 5489935at2759; -.
DR PhylomeDB; Q10944; -.
DR Reactome; R-CEL-1483166; Synthesis of PA.
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 cell types or 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; 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:SF110; ACID PHOSPHATASE 1, ISOFORM B; 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 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
//
