PHO11_CAEEL
ID PHO11_CAEEL Reviewed; 413 AA.
AC Q09451;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Putative acid phosphatase 11;
DE EC=3.1.3.2;
GN Name=pho-11; ORFNames=C05C10.4;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z48178; CAA88205.1; -; Genomic_DNA.
DR PIR; T18945; T18945.
DR RefSeq; NP_496143.1; NM_063742.6.
DR AlphaFoldDB; Q09451; -.
DR SMR; Q09451; -.
DR BioGRID; 39869; 9.
DR IntAct; Q09451; 1.
DR MINT; Q09451; -.
DR STRING; 6239.C05C10.4.1; -.
DR EPD; Q09451; -.
DR PaxDb; Q09451; -.
DR PeptideAtlas; Q09451; -.
DR EnsemblMetazoa; C05C10.4.1; C05C10.4.1; WBGene00007331.
DR EnsemblMetazoa; C05C10.4.2; C05C10.4.2; WBGene00007331.
DR GeneID; 174547; -.
DR KEGG; cel:CELE_C05C10.4; -.
DR UCSC; C05C10.4.1; c. elegans.
DR CTD; 174547; -.
DR WormBase; C05C10.4; CE17370; WBGene00007331; pho-11.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000168803; -.
DR HOGENOM; CLU_030431_2_0_1; -.
DR InParanoid; Q09451; -.
DR OMA; QPGLTFV; -.
DR OrthoDB; 1221585at2759; -.
DR PhylomeDB; Q09451; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q09451; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007331; Expressed in larva and 3 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 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Reference proteome.
FT CHAIN 1..413
FT /note="Putative acid phosphatase 11"
FT /id="PRO_0000114469"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 315
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT DISULFID 381..387
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 46617 MW; BFFC70995EA903F0 CRC64;
MMISIFSLLA STAILVFANG QSNVKLEFVQ AMWRHGERAS QVDQYPIYEK DWIYGGGGLG
ELTAIGMGEM NELGWLIRKR YVTKLKFLTP KYASREVYFR STNFNRTIIS AQSLLYGLFP
PSLYDVKNVD YPYSPLTWFP GFTFVPVHVD GPDQCAASQN CPCTRYDLLQ GQMLTLPEVL
PKYTQVVLLN RRVGGYYNMT SGLDSFTTYP DTWKCQRAYF NRTMYAKLPW YNEELYYQAQ
VTYAPVKGFL EGNFENPAVT SSGLDVGLEI KKVRSGVIIN EVFNRANEKL NCAELGQNCT
SYLNKLKFYG YSIHDNNVYG VLVALGIPQI ANTLDGWPAY AAGIFMEFHR NTSTNERFFK
VLYREGDDTP ISDVTSQLPI CNGATLCPLG ALQTLAETLK PLPDITTLCK TPL
