PPAL_RAT
ID PPAL_RAT Reviewed; 423 AA.
AC P20611;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Lysosomal acid phosphatase;
DE Short=LAP;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=Acp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2764916; DOI=10.1016/0006-291x(89)90779-1;
RA Himeno M., Fujita H., Noguchi Y., Kono A., Kato K.;
RT "Isolation and sequencing of a cDNA clone encoding acid phosphatase in rat
RT liver lysosomes.";
RL Biochem. Biophys. Res. Commun. 162:1044-1053(1989).
RN [2]
RP PROTEIN SEQUENCE OF 35-41; 154-161; 255-266 AND 349-364, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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; M27893; AAA40744.1; -; mRNA.
DR PIR; A33395; A33395.
DR AlphaFoldDB; P20611; -.
DR SMR; P20611; -.
DR STRING; 10116.ENSRNOP00000018620; -.
DR GlyGen; P20611; 9 sites.
DR jPOST; P20611; -.
DR PaxDb; P20611; -.
DR PRIDE; P20611; -.
DR UCSC; RGD:2021; rat.
DR RGD; 2021; Acp2.
DR eggNOG; KOG3720; Eukaryota.
DR InParanoid; P20611; -.
DR PhylomeDB; P20611; -.
DR PRO; PR:P20611; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
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:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:RGD.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:RGD.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IDA:RGD.
DR GO; GO:0048102; P:autophagic cell death; IDA:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; NAS:RGD.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; IDA:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT CHAIN 31..423
FT /note="Lysosomal acid phosphatase"
FT /id="PRO_0000023962"
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 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 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; 48320 MW; 6F4C4819CADD4496 CRC64;
MAGRQSGWSQ AALLQFLLGM CLMVMPPIQA RSLRFVTLLY RHGDRSPVKA YPKDPYQEEK
WPQGFGQLTK EGMLQHWELG QALRQRYHGF LNASYHRQEV YVRSTDFDRT LMSAEANLAG
LFPPTEVQHF NPNISWQPIP VHTVPITEDR LLKFPLGPCP RYEQLQNETR QTPEYQNMSI
QNAQFLDMVA NETGLMNLTL ETIWNVYDTL FCEQTHGLLL PPWASPQTVQ ALSQLKDFSF
LFLFGIHDQV QKARLQGGVL LAQILKNLTL MATTSQFPKL LVYSAHDTTL VALQMALNVY
NGKQAPYASC HIFELYQEDN GNFSVEMYFR NDSKKAPWPL TLPGCPHRCP LQDFLRLTEP
VIPKDWQKEC QLASDTADTE VIVALAVCGS ILFLLIVLLL TVLFRMQAQP PGYHHVADRE
DHA
