ID A0A3Q1HKJ7_ANATE Unreviewed; 422 AA.
AC A0A3Q1HKJ7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Lysosomal acid phosphatase {ECO:0000256|ARBA:ARBA00039422};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000007985.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000007985.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 Evidence={ECO:0000256|ARBA:ARBA00000032};
CC -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000256|ARBA:ARBA00004227}.
CC Lysosome membrane {ECO:0000256|ARBA:ARBA00037852}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00037852}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00037852}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR AlphaFoldDB; A0A3Q1HKJ7; -.
DR STRING; 64144.ENSATEP00000007985; -.
DR Ensembl; ENSATET00000008112.2; ENSATEP00000007985.1; ENSATEG00000005610.2.
DR GeneTree; ENSGT00940000158446; -.
DR InParanoid; A0A3Q1HKJ7; -.
DR OMA; QESDWPQ; -.
DR OrthoDB; 5489935at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..422
FT /note="Lysosomal acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018608931"
FT TRANSMEM 375..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 422 AA; 47692 MW; CB02ACE5947CE9A5 CRC64;
MLSAVVLFIL MVGSVCVCEA AEERKLVYVT VLFRHGDRSP IKAYPTDPYQ ESDWPQGFGQ
LSQEGMMQHF ELGQFLRKRY KGFLNDSYDR HEVFVRSTDY DRTLMSAEAN LAGLYPPSGQ
QVFTPGLNWQ PIPVHTVPQS EERLLSFPLG DCPRYKQLMN QTEHSPEFLN VTKTYQDIID
LVRNKTGLNK TNVESVWSVY DTLFCESRHN KSAPAWVTPD VMEKLKVLKD FGFQVIFGVY
KQQEKSRLQG GILLGEIVKN LSKMAVPDPN QRQKLMMLSA HDTTVAALQA SLNVFNGKQP
PYASCQIFEL YRDTNGSVSV SLFYRNDSTV EPYAQQLPGC SLNCPLDDFV RITKLSISDD
RDKECQVPSK GTDRGVIIIL AVSGCLLLLF VSLLLGIMCW HKEPIGGRGY HHVLNHEGGE
YS
//