ID   PPAL_XENLA              Reviewed;         432 AA.
AC   B1H1P9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Lysosomal acid phosphatase;
DE            Short=LAP;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=acp2;
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=Liver;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) 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   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P11117};
CC       Single-pass membrane protein {ECO:0000255}; Lumenal side
CC       {ECO:0000250|UniProtKB:P11117}. Lysosome lumen
CC       {ECO:0000250|UniProtKB:P11117}. Note=The soluble form arises by
CC       proteolytic processing of the membrane-bound form.
CC       {ECO:0000250|UniProtKB:P11117}.
CC   -!- PTM: The membrane-bound form is converted to the soluble form by
CC       sequential proteolytic processing. First, the C-terminal cytoplasmic
CC       tail is removed. Cleavage by a lysosomal protease releases the soluble
CC       form in the lysosome lumen (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; BC160691; AAI60691.1; -; mRNA.
DR   RefSeq; NP_001121203.1; NM_001127731.1.
DR   AlphaFoldDB; B1H1P9; -.
DR   SMR; B1H1P9; -.
DR   GeneID; 100158274; -.
DR   KEGG; xla:100158274; -.
DR   CTD; 100158274; -.
DR   Xenbase; XB-GENE-6253082; acp2.S.
DR   OMA; HSACHFF; -.
DR   OrthoDB; 1221585at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 100158274; Expressed in intestine and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
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; Lysosome; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..432
FT                   /note="Lysosomal acid phosphatase"
FT                   /id="PRO_0000356291"
FT   TOPO_DOM        33..384
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        44
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        161..373
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..313
FT                   /evidence="ECO:0000250"
FT   DISULFID        348..352
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  48243 MW;  7EB42A5E3837E245 CRC64;
     MADGSCLGSG PQLGLIALLV VLLFSAVPLA QSRELRFVTL VYRHGDRSPV HGYPTDVHKE
     SVWPQGYGQL TQVGMKQHWD LGQELRARYK GFLNESYNRH EIYVRSTDVD RTLMSAEANL
     AGLYPPEGPQ IFNPNITWQP IPIHTIPESE DQLLKFPISP CPAYVKLQEE TRQSAEYINM
     TTTYKAFLQM VANKTGLSDC TLESVWSVYD TLFCEKTHNF SLPTWATADV LSKLNKLKDF
     SFVFLFGVHE RVKKARLQGG VLVDQILKNM TAAANNASNG LKLLAYSAHD STLGALQLAL
     DVYNGKQAPY ASCHIFELYK EDSGNFTVQM YFRNESGKTP YPVSLPGCAH ACPLQDFQSL
     LQPILAQDWE EECQTTSFIM TEETIIGLTI GAIALFIIIV VLMLLSCNEP KDDGYQHVSD
     EGDDHETKGL AM