ID   PPAT_XENLA              Reviewed;         420 AA.
AC   Q3KQG9; Q52KY6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Testicular acid phosphatase homolog;
DE            EC=3.1.3.2;
DE   AltName: Full=Acid phosphatase 4 {ECO:0000250|UniProtKB:Q9BZG2};
DE   Flags: Precursor;
GN   Name=acp4 {ECO:0000250|UniProtKB:Q9BZG2};
GN   Synonyms=acpt {ECO:0000250|UniProtKB:Q9BZG2};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; BC094140; AAH94140.1; -; mRNA.
DR   EMBL; BC106212; AAI06213.1; -; mRNA.
DR   RefSeq; NP_001087080.1; NM_001093611.1.
DR   AlphaFoldDB; Q3KQG9; -.
DR   SMR; Q3KQG9; -.
DR   DNASU; 446918; -.
DR   GeneID; 446918; -.
DR   KEGG; xla:446918; -.
DR   CTD; 446918; -.
DR   Xenbase; XB-GENE-960834; acp4.S.
DR   OrthoDB; 1221585at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 446918; Expressed in liver and 15 other tissues.
DR   GO; GO:0016021; C:integral component of 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; -; 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.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..420
FT                   /note="Testicular acid phosphatase homolog"
FT                   /id="PRO_0000259644"
FT   TOPO_DOM        25..385
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        407..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        286
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        156..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..309
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..348
FT                   /evidence="ECO:0000250"
FT   CONFLICT        171
FT                   /note="E -> D (in Ref. 1; AAH94140)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   420 AA;  48860 MW;  F9EA0D73B4470B0F CRC64;
     MKRAVVILWL PLAFTNLYIL TTFCQRTDNL TFVVAVFRHG DRAPIDTYPN DPHKEKLWPN
     GLQQLTQEGM RQQYELGRFL RRRYDHFLSS TYNRQEIYVR STDYDRTLMS AQASLAGLYP
     PNGSQLWHRD IHWQPIPVHT VPASQDRLLK FPSKDCPRYY ELMRETIQQP EYQDKVNSWK
     DFMERIANYT GYRAETTISR WVWKVYDTLF CQKSHNISLP SWATADVVKT LKEISAFDVK
     THVEMHKTNE KARLTGGILV DALLRNFSDV VNKSLPLKML MYSAHDSTLI ALQGALKVYN
     GLHPPYSSCH IIEFYKEADG THSVRMFYRN ETVREPYELA LPGCDSPCPL LNFTQLMAPV
     ISMDWKKDCA SDGSLQYRIG SENNTVLALS ICVGILGLTL TVMLFCLWRT YKLPVRRYQR