ID Q9U5U3_DROSU Unreviewed; 447 AA.
AC Q9U5U3;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Acid phosphatase-1 {ECO:0000313|EMBL:CAB59936.1};
DE EC=3.1.3.2 {ECO:0000313|EMBL:CAB59936.1};
GN Name=Acph-1 {ECO:0000313|EMBL:CAB59936.1,
GN ECO:0000313|FlyBase:FBgn0013885};
OS Drosophila subobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7241 {ECO:0000313|EMBL:CAB59936.1};
RN [1] {ECO:0000313|EMBL:CAB59936.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J58ST/100 {ECO:0000313|EMBL:CAB59936.1};
RX PubMed=10511564;
RA Navarro-Sabate A., Aguade M., Segarra C.;
RT "The relationship between allozyme and chromosomal polymorphism inferred
RT from nucleotide variation at the Acph-1 gene region of Drosophila
RT subobscura.";
RL Genetics 153:871-889(1999).
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; AJ389438; CAB59936.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9U5U3; -.
DR FlyBase; FBgn0013885; Dsub\Acph-1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
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:SF110; ACID PHOSPHATASE 1, ISOFORM B; 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.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CAB59936.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..447
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004335104"
FT TRANSMEM 407..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 447 AA; 51047 MW; 29E545BE7C27C326 CRC64;
MWNHSHQLCC AKALLVIGVL CVLSFGIGNA VHIPTYGSSE GETRPPPDQL ATLPGELKFA
HVIFRHGDRT PVDPYPTDPW NNRKFWPTGW GQLTNLGKEQ HYELGKWLRN RYKSLLGSRY
TNEDIFVQST DVDRTLMSAQ SDLAGLYEPQ GDDIWNPRID WQPVPVHTVP EKDDSILAAK
ASCPAYDYEL ATLEATSEFQ ALYVRYRELL SYLTQNSGRL VKSFIDAQYL NNTLFIEKLY
NMTLPVWAEK VYGKEELTYV SNFAFSIATF TRSMARLKTG PLLKDIFERF DKKLNNQLKP
DRSLWIYSAH DTTIANVLNS LKLFELHSPP YAACIMLEMR VDDSNTPLVS VFYKNTTAEP
LPLDIPGCGL SCPLKTLVKL YQDVLPGNWE RECKRSTMMM TYEEANLGAA TGILIFIITV
LLCASYGLMV YYRRRHYNLY TSYSQMA
//