ID R0JD98_ANAPL Unreviewed; 328 AA.
AC R0JD98;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Lysosomal acid phosphatase {ECO:0000256|ARBA:ARBA00039422};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646};
DE Flags: Fragment;
GN ORFNames=Anapl_15814 {ECO:0000313|EMBL:EOA94911.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA94911.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
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 EMBL; KB744512; EOA94911.1; -; Genomic_DNA.
DR AlphaFoldDB; R0JD98; -.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
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; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA94911.1"
FT NON_TER 328
FT /evidence="ECO:0000313|EMBL:EOA94911.1"
SQ SEQUENCE 328 AA; 37407 MW; 2849C854281AF593 CRC64;
QIFIRSTDYD RTLMSAEANL AGLYPPERQQ MFNPNISWQP IPVHTVPESG ERLLKFPLSP
CPRYEQLQNE TRHSAEYVNK TRDNLQFLQM VANETGIRDV SLETVWSVYD TLFCEQAHKM
DLPPWVTPDV MSQLKQLKDF GFEFLFGIHH RVEKARLQGG VLLDHIRKNL TKAANASAHQ
HLKLLAYSAH DTTLVALQMA LDVYNKIQAP YASCHLFELY QEDDGDFSVE MFFRNESGKE
PFPLTIPGCQ HKCPLHKFLE LTDPVVPQNW EQECQVASSM QETGLFVGLA VCGSVLLLLI
ILLLTVLLRV QSQPPGYRHV SNEGEEQA
//
