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Database: UniProt
Entry: G8Y0E0_PICSO
LinkDB: G8Y0E0_PICSO
Original site: G8Y0E0_PICSO 
ID   G8Y0E0_PICSO            Unreviewed;       491 AA.
AC   G8Y0E0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Piso0_004776 protein {ECO:0000313|EMBL:CCE86293.1};
GN   Name=Piso0_004776 {ECO:0000313|EMBL:CCE86293.1};
GN   ORFNames=GNLVRS01_PISO0N00893g {ECO:0000313|EMBL:CCE86293.1};
OS   Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS   10061 / NRRL Y-12695) (Hybrid yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE86293.1, ECO:0000313|Proteomes:UP000005222};
RN   [1] {ECO:0000313|Proteomes:UP000005222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC   Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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; FO082046; CCE86293.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8Y0E0; -.
DR   STRING; 559304.G8Y0E0; -.
DR   eggNOG; KOG2822; Eukaryota.
DR   HOGENOM; CLU_019266_0_0_1; -.
DR   InParanoid; G8Y0E0; -.
DR   OMA; ADDCPCY; -.
DR   Proteomes; UP000005222; Chromosome N.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProt.
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:UP000005222};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        90..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        263..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        458..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..241
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          426..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  55392 MW;  5136378B10A033D3 CRC64;
     MSEPVKTELK NRGQRNRSWA EAVNDSLESE VTIFQSSPSN DSGNLDDEVY KKKLSPFRYY
     LRKKGLALVK EEQGVLENIQ KKFRNPFLDF YFAWSANLAS HTFYVLILPL PFWLGLPMIT
     RDLVQVLGLG IYFSGCLKDY MCLPRPRSPP LYRITMSSYT TKEYGFPSSH SANATAATLV
     FLWRLIENKE SFSSSMFVAL FIFSCIYYFS LILGRVYCGM HGFLDLASGA TIGLILFLLR
     FLLGDYLDNL MLYSFNDSWK GLIVRPLIEI TFYVLLIHWH VEPVDDCPCF DDSVAFIGVL
     IGLDISQGAL IAHLGAETKA YSMDLLKVPL DFGAVGIPYL MLRIIIGMLL VVAWKAAAKP
     AVFTILPPIY KFVGWYIPRK SYEPTALSRK TTKQIRSQSL SNIEKDKIMT EIDGIIHGFR
     YNVNQEEADP NSSSSQENES DKTGPVGGVF RPRYDVEIVG RLIIYAGISS VAIGGYMYAI
     NFLGKLFNGI V
//
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