ID ACP1_CAEEL Reviewed; 426 AA.
AC Q23534;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Putative acid phosphatase 1;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=acp-1 {ECO:0000312|WormBase:ZK563.6};
GN ORFNames=ZK563.6 {ECO:0000312|WormBase:ZK563.6};
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-37, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; FO080346; CCD63046.1; -; Genomic_DNA.
DR PIR; T27918; T27918.
DR RefSeq; NP_508585.1; NM_076184.4.
DR AlphaFoldDB; Q23534; -.
DR SMR; Q23534; -.
DR BioGRID; 45568; 1.
DR IntAct; Q23534; 1.
DR STRING; 6239.ZK563.6.2; -.
DR GlyCosmos; Q23534; 2 sites, No reported glycans.
DR iPTMnet; Q23534; -.
DR EPD; Q23534; -.
DR PaxDb; 6239-ZK563-6-1; -.
DR PeptideAtlas; Q23534; -.
DR EnsemblMetazoa; ZK563.6.1; ZK563.6.1; WBGene00022770.
DR GeneID; 180627; -.
DR KEGG; cel:CELE_ZK563.6; -.
DR UCSC; ZK563.6.1; c. elegans.
DR AGR; WB:WBGene00022770; -.
DR WormBase; ZK563.6; CE28192; WBGene00022770; acp-1.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00970000196271; -.
DR HOGENOM; CLU_041834_0_0_1; -.
DR InParanoid; Q23534; -.
DR OMA; MFPNATP; -.
DR OrthoDB; 5477542at2759; -.
DR PhylomeDB; Q23534; -.
DR Reactome; R-CEL-1483166; Synthesis of PA.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q23534; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00022770; Expressed in material anatomical entity and 3 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF209; ACID PHOSPHATASE 1-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.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..426
FT /note="Putative acid phosphatase 1"
FT /id="PRO_0000248567"
FT TOPO_DOM 19..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..369
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 48431 MW; DCE8B129219A498C CRC64;
MRVLFYVSIL VIIASVHTQL ISVHVIFRHG ARAPVLNVTS EEAKSYFYRG LGQLTDEGFE
QARLMGKVLR DRYVNSFVDA RMLSSQLLFR SSPVERCLMT LQTVGNTMFP NATPPVQTVA
KPDDFLLVPK LDCDFQLGEW DNYFNLTESD KKMARKNPWF VSDKALRKAV TKTDFLQDRG
GENLPALILE KEAGLAVPSW FNEGAYKESL HVFYSALAVM SSVGEYKSSK GIRIKSGLLM
EKVFNDIQEK VRCHEKKEVS NIKCDIHKLQ VFSSHDLLIL PILETLGIRE EVLGKDMPPE
FMSTIIIETM IVDNSPVVKV LFRKNPREIT LRDVTGFVKN CPPGQPLCPV QRFTSCCNEF
ITSDPKSECY AETTVEKQSE WVMTPLSWII VAIAILLLIA LILMTYFVIR YKNRSIVNIK
KLSLEN
//
