ID I1JQE7_SOYBN Unreviewed; 406 AA.
AC I1JQE7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN Name=100807865 {ECO:0000313|EnsemblPlants:KRH68080};
GN ORFNames=GLYMA_03G207000 {ECO:0000313|EMBL:KRH68080.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH68080.1};
RN [1] {ECO:0000313|EMBL:KRH68080.1, ECO:0000313|EnsemblPlants:KRH68080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH68080};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH68080.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH68080}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH68080};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH68080.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH68080.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC {ECO:0000256|ARBA:ARBA00038324}.
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DR EMBL; CM000836; KRH68080.1; -; Genomic_DNA.
DR RefSeq; XP_006577115.1; XM_006577052.2.
DR AlphaFoldDB; I1JQE7; -.
DR SMR; I1JQE7; -.
DR STRING; 3847.I1JQE7; -.
DR PaxDb; 3847-GLYMA03G36520-1; -.
DR EnsemblPlants; KRH68080; KRH68080; GLYMA_03G207000.
DR GeneID; 100807865; -.
DR Gramene; KRH68080; KRH68080; GLYMA_03G207000.
DR KEGG; gmx:100807865; -.
DR eggNOG; KOG2822; Eukaryota.
DR HOGENOM; CLU_043042_0_0_1; -.
DR InParanoid; I1JQE7; -.
DR OMA; CDYIGNC; -.
DR OrthoDB; 2958177at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR CDD; cd03388; PAP2_SPPase1; 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 PANTHER; PTHR14969:SF28; DIHYDROSPHINGOSINE 1-PHOSPHATE PHOSPHATASE LCB3-RELATED; 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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..219
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 406 AA; 44583 MW; 2252A212D185CB6F CRC64;
MEGEGAAVWQ GAVLGGIIFW LVSASYLNAT RKLRSFLQPW VTHHVDTQTP IILKIQSYGF
GFLDALFSGL SCVVSVPFYT AFLPLLFWSG HGKLARQMTL LMAFCDYIGN CTKDVVSAPR
PASPPVKRVT ATKDEEDNAL EYGLPSSHTL NTVCLSGYLL RYVLTHTQIQ GAYVTYLGVS
LACMLVFLIG LGRIYLGMHS VVDVLAGLLI GLVVLAFWLM VDEYIDSFVI SGQNVTSFWA
ALSFLLLFAY PTPELPTPSF EYHTAFDGVA LGIVSGVQQT YHQFHHANVP RLFSSELTIP
VFLGRMLLGI PTILIVKFCS KALAKWTIPV VANTLGIPIK STGYIPTLNG SVTGKKSDKL
KQGYLQKLLS QHKAFDVDTG IRFVQYAGLA WSVVDLVPSL FSYMSL
//
