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Database: UniProt
Entry: G3PJD3_GASAC
LinkDB: G3PJD3_GASAC
Original site: G3PJD3_GASAC 
ID   G3PJD3_GASAC            Unreviewed;       720 AA.
AC   G3PJD3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Phospholipid phosphatase related 3b {ECO:0000313|Ensembl:ENSGACP00000017712.1};
GN   Name=PLPPR3 {ECO:0000313|Ensembl:ENSGACP00000017712.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000017712.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000017712.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000017712.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   AlphaFoldDB; G3PJD3; -.
DR   STRING; 69293.ENSGACP00000017712; -.
DR   Ensembl; ENSGACT00000017747.1; ENSGACP00000017712.1; ENSGACG00000013397.1.
DR   eggNOG; KOG3030; Eukaryota.
DR   GeneTree; ENSGT00940000160280; -.
DR   InParanoid; G3PJD3; -.
DR   OMA; GNPWEWA; -.
DR   TreeFam; TF316040; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000013397; Expressed in telencephalon and 1 other cell type or tissue.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd03384; PAP2_wunen; 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:SF14; PHOSPHOLIPID PHOSPHATASE-RELATED PROTEIN TYPE 3; 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   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          129..273
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          427..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  77880 MW;  EBFAE8FBBC22B19E CRC64;
     MNSEKMKKKP PKDSLTLLPC FYFVELPIVA SSMVSLYFLE LTDVVQPAQV GFRCHDRELS
     MPYVDGGDEL IPLLMLLSLA FAGPAASIML VEGLIYCLQS RLKLRRPEGS INAGGCNFNS
     FLRRTVRFVG VHVFGLCATA LVTDIIQLST GYHTPFFLTV CKPNYTQVGV SCDRNVYITK
     DICSGHDQHA IVAARKTFPS QHATLSAFAA VYVSMYFNST ISDSTKLLKP VLVFAFAIAA
     ALTGLTQITQ HRSHPIDVYV GFLIGAFIAA YLAFHAVANF KSGDDVTMTA PPSLPKEDPL
     RALTERGHES VYNKGPASAS ESNDEIAPAP APMDRLEGLV PLQREKASMG SLKRASVDVE
     LLAPRSPMGK ETMLTFSNTL PRASMNPVQP VQPVQRRLKA VQVPMDPMRS QQLVTEWKQK
     SMEMRGLSVR DETEHSASED GSEVGSVGTD EGGSHVPIYQ TVAQSGRAPP GRNATPPPVG
     AKAVATPRPP QVPEAGPPPV SPKSALTRAK WLAIREKTSG EGSGRGATNQ PRLMQVIAMS
     KQQGLLPSSS SGEKSSETTS TCSGTSSTTD SPHYRPSPEQ QREGSGIITV DAHAPHHPVV
     QPQPPLQAPP LAGNGSPWEW AGAPNGGDPR DTYDLNSLTR GDSAARGSSF RPHSRGASPC
     AAVGHDPTSP HPQVETSADA QRREMAMRRK TALVLLDREI RNQTEQENYY KSLQGRRYKD
//
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