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
//