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Database: UniProt
Entry: A0A3Q1HKJ7_ANATE
LinkDB: A0A3Q1HKJ7_ANATE
Original site: A0A3Q1HKJ7_ANATE 
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
//
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