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Database: UniProt
Entry: Q9U5U3_DROSU
LinkDB: Q9U5U3_DROSU
Original site: Q9U5U3_DROSU 
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
//
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