ID W5MGT7_LEPOC Unreviewed; 291 AA.
AC W5MGT7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Phospholipid phosphatase 7 (inactive) {ECO:0000313|Ensembl:ENSLOCP00000007596.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007596.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000007596.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01035497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006640848.1; XM_006640785.2.
DR AlphaFoldDB; W5MGT7; -.
DR Ensembl; ENSLOCT00000007605.1; ENSLOCP00000007596.1; ENSLOCG00000006288.1.
DR GeneID; 102683686; -.
DR KEGG; loc:102683686; -.
DR CTD; 84814; -.
DR eggNOG; KOG4268; Eukaryota.
DR GeneTree; ENSGT00940000157147; -.
DR HOGENOM; CLU_072573_4_0_1; -.
DR InParanoid; W5MGT7; -.
DR OMA; WAFCVGF; -.
DR OrthoDB; 1221241at2759; -.
DR Proteomes; UP000018468; Linkage group LG21.
DR Bgee; ENSLOCG00000006288; Expressed in muscle tissue and 7 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
DR CDD; cd03391; PAP2_containing_2_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 PANTHER; PTHR14969:SF17; INACTIVE PHOSPHOLIPID PHOSPHATASE 7; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 157..268
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 32330 MW; 0EC09385D56F3FE9 CRC64;
MPAHQSRSRT RDRNNVLNRP EFMSLNQPLR NSPAEVRSSL RRHNVQAGQA KHTQVPQPDY
PTQEPSDNVK DRRESLKLPE DDCMQLNPSF KGIAMNSLLA IDICMSKRLG VCAYSTSSWG
SVRSMVTLLA ITGHGIPWIC GTLLCLTRSS TLAGQEVLVN LLLALVLDVM TVAGVQKLVK
RKGPWEISPS FLDYVAMDVY SFPAAHASRA AMVAKFLLNH LVLAVPLRIL LVIWAFLVGV
SRVMLGRHHL TDVGCGFALG FLHYYLVEMV WLSSNTCQTL ISISTLSPFF K
//
