ID   PPAL_BOVIN              Reviewed;         423 AA.
AC   Q0P5F0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=Lysosomal acid phosphatase;
DE            Short=LAP;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=ACP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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; BC120138; AAI20139.1; -; mRNA.
DR   RefSeq; NP_001069526.1; NM_001076058.2.
DR   AlphaFoldDB; Q0P5F0; -.
DR   SMR; Q0P5F0; -.
DR   STRING; 9913.ENSBTAP00000027968; -.
DR   GlyCosmos; Q0P5F0; 8 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000027968; -.
DR   Ensembl; ENSBTAT00000027968.4; ENSBTAP00000027968.3; ENSBTAG00000021002.4.
DR   GeneID; 535407; -.
DR   KEGG; bta:535407; -.
DR   CTD; 53; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021002; -.
DR   VGNC; VGNC:52601; ACP2.
DR   eggNOG; KOG3720; Eukaryota.
DR   GeneTree; ENSGT00940000158446; -.
DR   HOGENOM; CLU_030431_0_0_1; -.
DR   InParanoid; Q0P5F0; -.
DR   OMA; QESDWPQ; -.
DR   TreeFam; TF312893; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000021002; Expressed in monocyte and 104 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11567:SF180; LYSOSOMAL ACID PHOSPHATASE; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 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_0000352520"
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;  A22B7E4B74CA57F6 CRC64;
     MAGRRFGWSR AALLQLILGV NLMVMPRTQA RTLRFVTLLY RHGDRSPVKA YPKDPHQEDK
     WPQGFGQLTK EGMLQHWELG QALRQRYHGF LNTSYHRQEV YVRSTDFDRT LMSAEANLAG
     LFPPDGIQRF NPNISWQPIP VHTVPVAEDR LLKFPLGPCP RFEQLQNETR RMPEYQNESV
     QNAQFLDMVA NETGLTDLSL ETVWNVYDTL FCEQTHGLPL PPWASPQTMQ RLSRLKDFSF
     RFLFGIYKQA EKARLQGGVL LAQIRKNLTL MATTSQLPKL LVYSAHDTTL VALHMALGVY
     NGEQAPYASC HMFELYQEDS GNFSVEMYFR NESHRAPWPL TLPGCSHRCP LQDFLRLTEP
     VVPKDWLQEC QLAGGPADTE VIVALAVCGS ILFLLIVLLL TVLFRVQAQP PGYRHVPDGE
     DHA
//