WUN_DROME
ID WUN_DROME Reviewed; 379 AA.
AC Q9V576; P91661; Q8MKU5; Q8WT60; Q9U9Y7;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative phosphatidate phosphatase;
DE EC=3.1.3.4;
DE AltName: Full=Germ cell guidance factor;
DE AltName: Full=Phosphatidic acid phosphatase type 2;
DE AltName: Full=Protein wunen;
GN Name=wun; ORFNames=CG8804;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8985246; DOI=10.1038/385064a0;
RA Zhang N., Zhang J.P., Purcell K.J., Chen Y., Howard K.;
RT "The Drosophila protein Wunen repels migrating germ cells.";
RL Nature 385:64-67(1997).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-99.
RA Russell C., Bartos S., Phillips R.G., Whittle R.;
RT "Efficient functional dissection of enhancer sequences in Drosophila: a
RT novel P- and hobo-based construct acting as an enhancer-capture element.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=12856002; DOI=10.1038/sj.embor.embor900;
RA Burnett C., Howard K.;
RT "Fly and mammalian lipid phosphate phosphatase isoforms differ in activity
RT both in vitro and in vivo.";
RL EMBO Rep. 4:793-799(2003).
RN [8]
RP SUBUNIT, AND MUTAGENESIS OF ASP-327.
RX PubMed=14725715; DOI=10.1186/1471-2091-5-2;
RA Burnett C., Makridou P., Hewlett L., Howard K.;
RT "Lipid phosphate phosphatases dimerise, but this interaction is not
RT required for in vivo activity.";
RL BMC Biochem. 5:2-2(2004).
CC -!- FUNCTION: Responsible for guiding the germ cells early in the process
CC of migration from the lumen of the developing gut towards the overlying
CC mesoderm, where the germ cells enter the gonads. May be involved in
CC lipid metabolism. {ECO:0000269|PubMed:12856002,
CC ECO:0000269|PubMed:8985246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC -!- SUBUNIT: Homodimer. This complex seems not to be involved in substrate
CC recognition, it may confer only structural or functional stability.
CC {ECO:0000269|PubMed:14725715}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9V576-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9V576-2; Sequence=VSP_005084;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic gut in a pattern that guides
CC germ cells towards mesoderm (initially in hindgut and then on lower
CC side of gut). During extended germ band stage, expressed in ectoderm as
CC a medial band throughout the trunk. {ECO:0000269|PubMed:8985246}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; U73822; AAC47449.1; -; mRNA.
DR EMBL; AE013599; AAF58942.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM71066.1; -; Genomic_DNA.
DR EMBL; AF145595; AAD38570.1; -; mRNA.
DR EMBL; BT001729; AAN71484.1; -; mRNA.
DR EMBL; AY046533; AAL34392.1; -; Genomic_DNA.
DR RefSeq; NP_477193.1; NM_057845.5. [Q9V576-2]
DR RefSeq; NP_724787.1; NM_165674.3. [Q9V576-1]
DR AlphaFoldDB; Q9V576; -.
DR BioGRID; 61798; 7.
DR IntAct; Q9V576; 1.
DR STRING; 7227.FBpp0087635; -.
DR GlyGen; Q9V576; 2 sites.
DR PaxDb; Q9V576; -.
DR PRIDE; Q9V576; -.
DR DNASU; 35966; -.
DR EnsemblMetazoa; FBtr0088552; FBpp0087635; FBgn0016078. [Q9V576-1]
DR EnsemblMetazoa; FBtr0088553; FBpp0087636; FBgn0016078. [Q9V576-2]
DR GeneID; 35966; -.
DR KEGG; dme:Dmel_CG8804; -.
DR UCSC; CG8804-RA; d. melanogaster. [Q9V576-1]
DR CTD; 35966; -.
DR FlyBase; FBgn0016078; wun.
DR VEuPathDB; VectorBase:FBgn0016078; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000167256; -.
DR InParanoid; Q9V576; -.
DR OMA; YTMIYLA; -.
DR PhylomeDB; Q9V576; -.
DR Reactome; R-DME-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 35966; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35966; -.
DR PRO; PR:Q9V576; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0016078; Expressed in thoracico-abdominal ganglion (Drosophila) and 38 other tissues.
DR ExpressionAtlas; Q9V576; differential.
DR Genevisible; Q9V576; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005918; C:septate junction; IDA:FlyBase.
DR GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IDA:FlyBase.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; TAS:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0035233; P:germ cell repulsion; IMP:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; PTHR10165; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Glycoprotein; Hydrolase;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..379
FT /note="Putative phosphatidate phosphatase"
FT /id="PRO_0000220917"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10731138,
FT ECO:0000303|PubMed:8985246"
FT /id="VSP_005084"
FT MUTAGEN 327
FT /note="D->T: Loss of catalytic activity and dimerization."
FT /evidence="ECO:0000269|PubMed:14725715"
FT CONFLICT 152
FT /note="F -> L (in Ref. 4; AAC47449)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> G (in Ref. 4; AAC47449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42789 MW; AD3C4F06B3DD9ADA CRC64;
MPAVKIIMST ETSASETTPL RRSENETPDH KELAQSNSNS RQTTVNSNNN NYSNSVQVRL
QEQDRDSDSE QQQHTATITM DTNKRILCRV GLDVLILLCA GFPILLFFLL GEPYKRGFFC
DDESLKHPFH DSTVRNWMLY FIGAVIPVGV IFIVEVIISQ NKAKQDNGNA TSRRYVFMNY
ELPDWMIECY KKIGIYAFGA VLSQLTTDIA KYSIGRLRPH FIAVCQPQMA DGSTCDDAIN
AGKYIQEFTC KGVGSSARML KEMRLSFPSG HSSFTFFAMV YLALYLQARM TWRGSKLLRH
LLQFLFIMVA WYTALSRVSD YKHHWSDVLA GSLIGSISAL VVANYVSDLF QKPNTKPYLA
RTVQDMNASP AQAITITTN
