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Database: UniProt
Entry: B9SFW1_RICCO
LinkDB: B9SFW1_RICCO
Original site: B9SFW1_RICCO 
ID   B9SFW1_RICCO            Unreviewed;       324 AA.
AC   B9SFW1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Phosphatidic acid phosphatase, putative {ECO:0000313|EMBL:EEF37504.1};
DE            EC=1.3.1.74 {ECO:0000313|EMBL:EEF37504.1};
GN   ORFNames=RCOM_0724080 {ECO:0000313|EMBL:EEF37504.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   EMBL; EQ973947; EEF37504.1; -; Genomic_DNA.
DR   RefSeq; XP_002524880.1; XM_002524834.2.
DR   AlphaFoldDB; B9SFW1; -.
DR   STRING; 3988.B9SFW1; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   InParanoid; B9SFW1; -.
DR   OrthoDB; 25293at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd03390; PAP2_containing_1_like; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF187; PHOSPHATIDIC ACID PHOSPHATASE TYPE 2_HALOPEROXIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:EEF37504.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          114..254
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   324 AA;  36280 MW;  A21B4BFE1783ECFD CRC64;
     MDALVLSLVE LGKMPEVWLG SHTVRSHGVK VARIHLQDWI ILLLLIVIDV ILNIIEPFHR
     FVGQGMMTDL TYPLKPNTVP VWTVPILAGI LPLAIFFVYY CYRKDIYDFH HAMLGLLFSL
     LITGVITDAI KDAVGRPRPN FFWRCFPDGN EAFDPVSKNV ICHGDAAVVK EGYKSFPSGH
     TSWSFAGLTY LAWYISGKLK VFDRRGHIAK LCVVLLPVLI ATLVGISRVD DYWHHWTDVF
     AGALIGTTVA ACCYLQSFPY PNDAEGWAPH AFFEMIAERK SQAAGRRANS IRKRGSTDVE
     AAFMPFDFEM ETPASRSSQG TSLD
//
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