PPAL_BOVIN
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 03-AUG-2022, entry version 89.
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 PaxDb; Q0P5F0; -.
DR PRIDE; Q0P5F0; -.
DR Ensembl; ENSBTAT00000027968; ENSBTAP00000027968; ENSBTAG00000021002.
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 OrthoDB; 1221585at2759; -.
DR TreeFam; TF312893; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000021002; Expressed in monocyte and 104 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:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0016791; F: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; -; 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_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
