ID Q19460_CAEEL Unreviewed; 425 AA.
AC Q19460;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 2.
DT 27-MAR-2024, entry version 134.
DE SubName: Full=ACid Phosphatase family {ECO:0000313|EMBL:CAA91406.3};
GN Name=acp-3 {ECO:0000313|EMBL:CAA91406.3,
GN ECO:0000313|WormBase:F14E5.3};
GN ORFNames=CELE_F14E5.3 {ECO:0000313|EMBL:CAA91406.3}, F14E5.3
GN {ECO:0000313|WormBase:F14E5.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA91406.3, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA91406.3, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA91406.3,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
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 Evidence={ECO:0000256|ARBA:ARBA00000032};
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; BX284602; CAA91406.3; -; Genomic_DNA.
DR PIR; T20892; T20892.
DR RefSeq; NP_495776.1; NM_063375.1.
DR AlphaFoldDB; Q19460; -.
DR SMR; Q19460; -.
DR STRING; 6239.F14E5.3.1; -.
DR PaxDb; 6239-F14E5-3; -.
DR EnsemblMetazoa; F14E5.3.1; F14E5.3.1; WBGene00008801.
DR GeneID; 259901; -.
DR KEGG; cel:CELE_F14E5.3; -.
DR UCSC; F14E5.3; c. elegans.
DR AGR; WB:WBGene00008801; -.
DR WormBase; F14E5.3; CE28915; WBGene00008801; acp-3.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00970000196540; -.
DR HOGENOM; CLU_645972_0_0_1; -.
DR InParanoid; Q19460; -.
DR OMA; LIMAFME; -.
DR OrthoDB; 2883547at2759; -.
DR PhylomeDB; Q19460; -.
DR Reactome; R-CEL-1483166; Synthesis of PA.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008801; Expressed in adult organism and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR11567:SF202; LYSOPHOSPHATIDIC ACID PHOSPHATASE TYPE 6; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 48880 MW; 92C96B96462E5B0F CRC64;
MSIDTSLNDH STAQLQMPDP ETEKQDTNPS GNRKKKLFII VGLVSAVVAT IIGFFIFYYF
FSSPGSTPTT AQMVQDGSLL FTQVIFRHGA RAPGNEKQTD TKFFPRDYGQ LTDQGYNHSF
MMGRFLKKRY VDTGFLSSFV KPNEMEWRSR DINRCLSTAS TVAAGMFKTE NQIWLTVPIV
TNLGINDVLL NLPIRGCNFT RNSRIKQCPK TEKVNRDEMY AVLYECMGGN HSIFQEIKID
DCDRYINEYR NHVPVPEFVR DNFKTISEEY LKVRNFQNGI GNRKMIKARF GFLVHTLLEN
LVNAWKHHLA RIKSLKFKVY SSQDWLLGGV LDAFGVLDHI QSKSKEEPNY NTMIIMELWK
KNGKPIVKFY YKPEEITLEN HVLQDLTDII PGCSGKECAL KKFKSCCNDT RGELEDLQEL
CDSRI
//
