ID   ACP1_CAEBR              Reviewed;         426 AA.
AC   Q619N4; A8XJH9;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Putative acid phosphatase 1;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=acp-1 {ECO:0000312|WormBase:CBG14199};
GN   ORFNames=CBG14199 {ECO:0000312|WormBase:CBG14199};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE600983; CAP32804.3; -; Genomic_DNA.
DR   RefSeq; XP_002644366.1; XM_002644320.1.
DR   AlphaFoldDB; Q619N4; -.
DR   SMR; Q619N4; -.
DR   GeneID; 8586361; -.
DR   KEGG; cbr:CBG_14199; -.
DR   CTD; 8586361; -.
DR   WormBase; CBG14199; CBP38071; WBGene00034774; Cbr-acp-1.
DR   eggNOG; KOG3720; Eukaryota.
DR   HOGENOM; CLU_041834_0_0_1; -.
DR   InParanoid; Q619N4; -.
DR   OMA; VERCLMT; -.
DR   OrthoDB; 1221585at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
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_0000248566"
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:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        133..369
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   426 AA;  48455 MW;  5CA7D6B37BF30CE5 CRC64;
     MRVLFYVFPF VIFALSQAQL ISVHVIFRHG ARAPVLNVTS EEAKSYFYRG LGQLTDVCIE
     QAKLIGKVLK DRYVNTFVDA RMLPTQLLFR SSPVERCLMT IQTVGNTMFV NSTPPVQTVA
     KPDDFLLVPK LDCAFQIDEW TNFFNLTEND KKQAKKNPWF ISEKALRRAT AASQTLQQRS
     DENLPALILE KDAGLAVPSW FNEEAYKESL TVFYKALAVM SSVGEYKSSK GIRVKTGLLL
     DKILNDIQEK VRCHEKNQKG HISCDRHKLQ VFSTHDLLIL PFLDALGIRE AALGEDLPPK
     FLSAIIIETM LLDDIPFVKV FYRGDPRDIT LRDMTGLVRN CPPNQALCPV NLFTSCCGEF
     ITADPRRECY EEKADQQLHN WTMTTVSWIL IGISAFLLII LIIMSYLAVR YKNRSVVTIK
     KVCLEN