ID   PPAL_PONAB              Reviewed;         423 AA.
AC   Q5NVF6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Lysosomal acid phosphatase;
DE            Short=LAP;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=ACP2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR926080; CAI29707.1; -; mRNA.
DR   RefSeq; NP_001127113.1; NM_001133641.1.
DR   AlphaFoldDB; Q5NVF6; -.
DR   BMRB; Q5NVF6; -.
DR   SMR; Q5NVF6; -.
DR   STRING; 9601.ENSPPYP00000003798; -.
DR   Ensembl; ENSPPYT00000003945; ENSPPYP00000003798; ENSPPYG00000003310.
DR   GeneID; 100174154; -.
DR   KEGG; pon:100174154; -.
DR   CTD; 53; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   GeneTree; ENSGT00940000158446; -.
DR   HOGENOM; CLU_030431_0_0_1; -.
DR   InParanoid; Q5NVF6; -.
DR   OMA; QESDWPQ; -.
DR   OrthoDB; 1221585at2759; -.
DR   TreeFam; TF312893; -.
DR   Proteomes; UP000001595; Chromosome 11.
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..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..423
FT                   /note="Lysosomal acid phosphatase"
FT                   /id="PRO_0000352522"
FT   TOPO_DOM        31..380
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        402..423
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        42
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        159..370
FT                   /evidence="ECO:0000250"
FT   DISULFID        212..310
FT                   /evidence="ECO:0000250"
FT   DISULFID        345..349
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   423 AA;  48302 MW;  1A2CBFA5D8080E2B CRC64;
     MAGKRSGWSR AALLQLLLGV NLVVMPPTQA RSLRFVTLLY RHGDRSPVKT YPKDPYQEEE
     WPQGFGQLTK EGMLQHWELG QALRQRYHGF LNTSYHRQEV YVRSTDFDRT LMSAEANLAG
     LFPPNGMQRF NPNISWQPIP VHTVPITEDR LLKFPLGPCP RYEQLQNETR QTPEYQNESS
     RNAQFLDMVA NETGLTDLTL ETVWNVYDTL FCEQTHGLRL PPWASPQTMQ RLSRLKDFSF
     RFLFGIYQQA EKARLQGGVL LAQIRKNLTL MATTSQLPKL LVYSAHDTTL VALQMALDVY
     NGEQAPYASC HIFELYQEDS GNFSVEMYFR NESDKAPWPL SLPGCPHRCP LQDFLRLTEP
     VVPKDWQQEC QVASGPADTE VIVALAVCGS ILFLLIVLLL TVLFRMQAQP PGYRHVADGE
     DHA