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Database: UniProt
Entry: A0A178EE45_9PLEO
LinkDB: A0A178EE45_9PLEO
Original site: A0A178EE45_9PLEO 
ID   A0A178EE45_9PLEO        Unreviewed;       575 AA.
AC   A0A178EE45;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Sphingosine-1-phosphate phosphohydrolase {ECO:0000313|EMBL:OAL54276.1};
GN   ORFNames=IQ07DRAFT_583573 {ECO:0000313|EMBL:OAL54276.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54276.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL54276.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54276.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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; KV441638; OAL54276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EE45; -.
DR   STRING; 765867.A0A178EE45; -.
DR   InParanoid; A0A178EE45; -.
DR   OrthoDB; 2958177at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:OAL54276.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        82..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..232
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  63940 MW;  55F366178B8E1226 CRC64;
     MCPQHDVPTV DAAAADSTAQ PPRELDEEPR LDAGNKHLDH YAERLPAWRN ALRNRLIPIV
     RWETPWLALM QDKIRSPALD SYFAYTANLG THTFFMIFLP IQFWCGYTSV GRATVFMLAA
     GVYWTGFLKD LLCLPRPLSP PLARISMSGS AALEYGFPSS HSANAVSVAF YAIYMLRQSA
     HEYHPNMNLA LQGLFYFYAV SIILGRLYCG MHGFLDVIIG SIMGALITAF QLLYGDWMDS
     WIFSGSYQDI FIATLTVCIL VRINPEPADD CPCFDDSVSF SGVVIGINIG AWHFAKSGYA
     LPDAYPSSVP FSLQEMGLFK ATIRILLGVV VIFVWRATMK PALFTILPPV FRILEQARLN
     LPRAFFLNAS KYTSIQPFTD DDNVIPPASE LPHMLKNLAH PRKRSVSVGP QSAADAYETL
     AYRNRRRRES VNSLEGAVPE EATWSPTPGL KLQSNGFDKT KAVLGTGLLP TPMASRVHSY
     EQMMGTGRVY ASKKNNATPP EIDTDVAGEV LQFTQSPSEE ENEKREIFMK LTKPRVRYDV
     EVVTKLIVYT GIAWIAVGGN PILFELVGLG MGVRP
//
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