ID A4HHZ1_LEIBR Unreviewed; 272 AA.
AC A4HHZ1;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative dolichyl pyrophosphate phosphatase {ECO:0000313|EMBL:CAM40197.1};
DE EC=3.1.3.4 {ECO:0000313|EMBL:CAM40197.1};
GN ORFNames=LBRM_30_0480 {ECO:0000313|EMBL:CAM40197.1};
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM40197.1, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM40197.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM40197.1,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM40197.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM40197.1,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR799005; CAM40197.1; -; Genomic_DNA.
DR RefSeq; XP_001566681.1; XM_001566631.1.
DR AlphaFoldDB; A4HHZ1; -.
DR STRING; 5660.A4HHZ1; -.
DR GeneID; 5417573; -.
DR KEGG; lbz:LBRM_30_0480; -.
DR VEuPathDB; TriTrypDB:LbrM.30.0480; -.
DR VEuPathDB; TriTrypDB:LBRM2903_300010600; -.
DR InParanoid; A4HHZ1; -.
DR OMA; FWTEAIC; -.
DR Proteomes; UP000007258; Chromosome 30.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR14969:SF13; AT30094P; 1.
DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CAM40197.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007258};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..241
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 272 AA; 29947 MW; 7DE4184DE9C02F83 CRC64;
MSWSETVRFV WGYTHLSAVE LQQGEVLARA HRQGAAALAT PAKTPVASSG SPHWKSWAMT
EVLYRQHDLF SKLFGISSIG PVAMIVLLAG MTSAPCRERR IPAMNLILYL VLSVCLNVAL
KEVIRSPRPA HPAAGMNYTT MNGMPSDHAQ FMAGFSVYLL RRWAHTQRRR TEGRKAGHLQ
QRKSISASAA LTRSSPSYAL VGLLLFATLF IGAGRIYNGY HTVGQALVGW MVGIALALVC
TTVRVQRSFT WVSEKVLVPV MLVCTFWTEA IC
//
