PPAL_MOUSE
ID PPAL_MOUSE Reviewed; 423 AA.
AC P24638; Q8QZT5;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Lysosomal acid phosphatase;
DE Short=LAP;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=Acp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-423.
RX PubMed=2059337; DOI=10.1515/bchm3.1991.372.1.301;
RA Geier C., von Figura K., Pohlmann R.;
RT "Molecular cloning of the mouse lysosomal acid phosphatase.";
RL Biol. Chem. Hoppe-Seyler 372:301-304(1991).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; BC023343; AAH23343.1; -; mRNA.
DR EMBL; X57199; CAA40485.1; -; mRNA.
DR CCDS; CCDS16427.1; -.
DR PIR; S14742; S14742.
DR RefSeq; NP_031413.1; NM_007387.2.
DR AlphaFoldDB; P24638; -.
DR SMR; P24638; -.
DR BioGRID; 197928; 2.
DR STRING; 10090.ENSMUSP00000002172; -.
DR GlyConnect; 2489; 10 N-Linked glycans (4 sites).
DR GlyGen; P24638; 10 sites, 10 N-linked glycans (4 sites).
DR iPTMnet; P24638; -.
DR PhosphoSitePlus; P24638; -.
DR SwissPalm; P24638; -.
DR jPOST; P24638; -.
DR MaxQB; P24638; -.
DR PaxDb; P24638; -.
DR PeptideAtlas; P24638; -.
DR PRIDE; P24638; -.
DR ProteomicsDB; 289730; -.
DR Antibodypedia; 26620; 111 antibodies from 24 providers.
DR DNASU; 11432; -.
DR Ensembl; ENSMUST00000002172; ENSMUSP00000002172; ENSMUSG00000002103.
DR Ensembl; ENSMUST00000239169; ENSMUSP00000159053; ENSMUSG00000002103.
DR GeneID; 11432; -.
DR KEGG; mmu:11432; -.
DR UCSC; uc008kvf.2; mouse.
DR CTD; 53; -.
DR MGI; MGI:87882; Acp2.
DR VEuPathDB; HostDB:ENSMUSG00000002103; -.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000158446; -.
DR InParanoid; P24638; -.
DR OMA; QESDWPQ; -.
DR OrthoDB; 1221585at2759; -.
DR PhylomeDB; P24638; -.
DR TreeFam; TF312893; -.
DR BioGRID-ORCS; 11432; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Acp2; mouse.
DR PRO; PR:P24638; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P24638; protein.
DR Bgee; ENSMUSG00000002103; Expressed in spermatocyte and 268 other tissues.
DR ExpressionAtlas; P24638; baseline and differential.
DR Genevisible; P24638; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
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:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:MGI.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0048102; P:autophagic cell death; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT CHAIN 31..423
FT /note="Lysosomal acid phosphatase"
FT /id="PRO_0000023961"
FT TOPO_DOM 31..381
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..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 197
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 CARBOHYD 374
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"
FT CONFLICT 131
FT /note="N -> S (in Ref. 2; CAA40485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48509 MW; AFD7A5C90A4F2AF4 CRC64;
MAGRQTGWSQ AALLQFLLGM CLTVMPPIQA RSLRFVTLLY RHGDRSPVKT YPKDPYQEEK
WPQGFGQLTK EGMLQHWELG QALRQRYHGF LNTSYHRQEV YVRSTDFDRT LMSAEANLAG
LFPPNEVQHF NPNISWQPIP VHTVPITEDR LLKFPLGPCP RYEQLQNETR QTPEYQNRSI
QNAQFLNMVA NETGLTNVTL ETIWNVYDTL FCEQTHGLLL PPWASPQTVQ RLSQLKDFSF
LFLFGIHEQV QKARLQGGVL LAQILKNLTL MATTSQFPKL LVYSAHDTTL VALQMALNVY
NGKQAPYASC HIFELYQEDN GNFSVEMYFR NDSKKAPWPL ILPGCPHRCP LQDFLRLTEP
VIPKDWQKEC QLANDTADTE VIVALAVCGS ILFLLIVLLL TILFRMQAQP PGYHHVADRE
DHA
