PHO1_CAEEL
ID PHO1_CAEEL Reviewed; 449 AA.
AC Q19076;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Intestinal acid phosphatase {ECO:0000312|WormBase:EGAP2.3};
DE EC=3.1.3.2 {ECO:0000269|PubMed:15733671, ECO:0000269|PubMed:1652526};
DE Flags: Precursor;
GN Name=pho-1 {ECO:0000312|WormBase:EGAP2.3};
GN ORFNames=EGAP2.3 {ECO:0000312|WormBase:EGAP2.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND BLOCKAGE OF
RP N-TERMINUS.
RX PubMed=1652526; DOI=10.1016/s0012-1606(05)80013-2;
RA Beh C.T., Ferrari D.C., Chung M.A., McGhee J.D.;
RT "An acid phosphatase as a biochemical marker for intestinal development in
RT the nematode Caenorhabditis elegans.";
RL Dev. Biol. 147:133-143(1991).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF MET-70 AND ASP-181.
RX PubMed=15733671; DOI=10.1016/j.ydbio.2004.12.012;
RA Fukushige T., Goszczynski B., Yan J., McGhee J.D.;
RT "Transcriptional control and patterning of the pho-1 gene, an essential
RT acid phosphatase expressed in the C. elegans intestine.";
RL Dev. Biol. 279:446-461(2005).
CC -!- FUNCTION: Acid phosphatase required for normal growth and development.
CC Specifically required for normal gut differentiation.
CC {ECO:0000269|PubMed:15733671}.
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 Evidence={ECO:0000269|PubMed:15733671, ECO:0000269|PubMed:1652526};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for alpha-naphthyl phosphate {ECO:0000269|PubMed:1652526};
CC pH dependence:
CC Optimum pH is 3.5 with alpha-naphthyl phosphate as substrate.
CC {ECO:0000269|PubMed:1652526};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1652526}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:1652526}; Single-
CC pass membrane protein {ECO:0000255}. Membrane
CC {ECO:0000305|PubMed:15733671}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:15733671}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine, specifically on the
CC edge of the gut lumen, in the 14 posterior cells of the intestine.
CC {ECO:0000269|PubMed:15733671, ECO:0000269|PubMed:1652526}.
CC -!- DEVELOPMENTAL STAGE: Expressed from late embryogenesis onwards
CC (PubMed:1652526, PubMed:15733671). Temporally expressed in anterior and
CC posterior cells of the intestine in newly hatched larvae
CC (PubMed:15733671). {ECO:0000269|PubMed:15733671,
CC ECO:0000269|PubMed:1652526}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:1652526}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a maternal
CC effect phenotype whereby the majority of F1 progeny of the RNAi-treated
CC animals survive to adulthood, however 80-100% of F2 embryos arrest
CC during embryogenesis. {ECO:0000269|PubMed:15733671}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; BX284602; CCD66681.1; -; Genomic_DNA.
DR PIR; T15933; T15933.
DR RefSeq; NP_494983.1; NM_062582.3.
DR AlphaFoldDB; Q19076; -.
DR SMR; Q19076; -.
DR IntAct; Q19076; 1.
DR STRING; 6239.EGAP2.3.1; -.
DR EPD; Q19076; -.
DR PaxDb; Q19076; -.
DR PeptideAtlas; Q19076; -.
DR EnsemblMetazoa; EGAP2.3.1; EGAP2.3.1; WBGene00004020.
DR GeneID; 173896; -.
DR KEGG; cel:CELE_EGAP2.3; -.
DR UCSC; EGAP2.3.1; c. elegans.
DR CTD; 173896; -.
DR WormBase; EGAP2.3; CE04325; WBGene00004020; pho-1.
DR eggNOG; KOG3720; Eukaryota.
DR HOGENOM; CLU_030431_2_0_1; -.
DR InParanoid; Q19076; -.
DR OMA; LMCTLDA; -.
DR OrthoDB; 1221585at2759; -.
DR PhylomeDB; Q19076; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q19076; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004020; Expressed in larva and 3 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; HDA:WormBase.
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.
PE 1: Evidence at protein level;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..449
FT /note="Intestinal acid phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_5004187044"
FT TOPO_DOM 20..428
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT ACT_SITE 321
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT MUTAGEN 70
FT /note="M->I: Maternal effect lethal and loss of phosphatase
FT activity; when associated with N-181."
FT /evidence="ECO:0000269|PubMed:15733671"
FT MUTAGEN 181
FT /note="D->N: Maternal effect lethal and loss of phosphatase
FT activity; when associated with I-70."
FT /evidence="ECO:0000269|PubMed:15733671"
SQ SEQUENCE 449 AA; 50316 MW; 04533AB3830D30E4 CRC64;
MVSAISIVAI FALEGFVTTY SDGTKDLVFV QTLWRHGDRS PTKTFKTDPF QEDAWQFGGG
GWGQLSPAGM KQHLNLGKML RNRYVTNYNF LPNKYNAKQI YVRSTDVNRT IISAMSNLLG
QYGQNDNSST PGLDYPDVDG WPAGYVPIAV HTVDDDTDHL GNMESTCPFK DQVWELAKTS
DEVKSFVNSA DVQAVLGNLT NYCGQPVDID NLWIITNALY IEQIYYNATL RTKNNWFTDA
FYAKADAIND QVQLFQNGIF KTVPNIVNGH DVGVLTRKVR GGPILNDMVM HINLKLMCQG
QTTPNCTWIN NLKNYIYSAH DTTIYAFFSA LLIEEYAVKP SGGYPLYSAA VLLELYIDSV
DKKPYFKMVY HEQDGSGFKD VTMGIQGCPQ NSSYCDLDIL RNFANTIKPD QPIDQWCLTD
LNKSSSFATV SMLFIAAILA INNNFLGLF
