PTSS_DROME
ID PTSS_DROME Reviewed; 498 AA.
AC Q9VPD3; M9PIC3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Phosphatidylserine synthase {ECO:0000303|PubMed:31869331, ECO:0000312|FlyBase:FBgn0287585};
DE EC=2.7.8.29 {ECO:0000269|PubMed:31869331};
GN Name=Pss {ECO:0000303|PubMed:31869331, ECO:0000312|FlyBase:FBgn0287585};
GN Synonyms=l(3)77CDf {ECO:0000312|FlyBase:FBgn0287585},
GN ptdss1 {ECO:0000312|FlyBase:FBgn0287585};
GN ORFNames=CG4825 {ECO:0000312|FlyBase:FBgn0287585};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS A AND B).
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAL39547.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39547.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39547.1};
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 [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=31869331; DOI=10.1371/journal.pgen.1008548;
RA Yang X., Liang J., Ding L., Li X., Lam S.M., Shui G., Ding M., Huang X.;
RT "Phosphatidylserine synthase regulates cellular homeostasis through
RT distinct metabolic mechanisms.";
RL PLoS Genet. 15:e1008548-e1008548(2019).
CC -!- FUNCTION: Catalyzes a base-exchange reaction in which the polar head
CC group of phosphatidylethanolamine (PE) is replaced by L-serine.
CC {ECO:0000269|PubMed:31869331}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a
CC 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine;
CC Xref=Rhea:RHEA:27606, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:64612; EC=2.7.8.29;
CC Evidence={ECO:0000269|PubMed:31869331};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC {ECO:0000269|PubMed:31869331}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Z1X2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0287585};
CC IsoId=Q9VPD3-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0287585};
CC IsoId=Q9VPD3-2; Sequence=VSP_060726;
CC -!- DISRUPTION PHENOTYPE: Lethal at the first instar larval stage
CC (PubMed:31869331). RNAi-mediated knockdown in salivary glands reduces
CC phosphatidylserine (PS) levels and depletes Akt1 from the plasma
CC membrane contributing to cell growth defects probably by affecting the
CC insulin pathway; causes a shift from phospholipid synthesis to neutral
CC lipid synthesis, which results in ectopic lipid accumulation in third
CC instar larval salivary glands; reduces mitochondrial PS levels thereby
CC impairing mitochondrial protein import and mitochondrial integrity
CC (PubMed:31869331). {ECO:0000269|PubMed:31869331}.
CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF51622.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94811.1; -; Genomic_DNA.
DR EMBL; AY069402; AAL39547.1; -; mRNA.
DR RefSeq; NP_001262118.1; NM_001275189.1. [Q9VPD3-2]
DR RefSeq; NP_649242.1; NM_140985.4. [Q9VPD3-1]
DR AlphaFoldDB; Q9VPD3; -.
DR STRING; 7227.FBpp0077872; -.
DR GlyGen; Q9VPD3; 1 site.
DR PaxDb; Q9VPD3; -.
DR PRIDE; Q9VPD3; -.
DR DNASU; 40281; -.
DR EnsemblMetazoa; FBtr0078214; FBpp0077872; FBgn0287585. [Q9VPD3-1]
DR EnsemblMetazoa; FBtr0331566; FBpp0303956; FBgn0287585. [Q9VPD3-2]
DR GeneID; 40281; -.
DR KEGG; dme:Dmel_CG4825; -.
DR UCSC; CG4825-RA; d. melanogaster. [Q9VPD3-1]
DR FlyBase; FBgn0287585; Pss.
DR VEuPathDB; VectorBase:FBgn0287585; -.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR HOGENOM; CLU_037661_3_0_1; -.
DR InParanoid; Q9VPD3; -.
DR OMA; QYYMYVT; -.
DR OrthoDB; 818196at2759; -.
DR PhylomeDB; Q9VPD3; -.
DR BRENDA; 2.7.8.29; 1994.
DR Reactome; R-DME-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR BioGRID-ORCS; 40281; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40281; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR ExpressionAtlas; Q9VPD3; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106258; F:L-serine-phosphatidylcholine phosphatidyltransferase activity; ISS:FlyBase.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; ISS:FlyBase.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IMP:FlyBase.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:FlyBase.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Lipid metabolism; Membrane; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..498
FT /note="Phosphatidylserine synthase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000450822"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..122
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..239
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..339
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..402
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..498
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 459
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305|PubMed:10731132"
FT /id="VSP_060726"
SQ SEQUENCE 498 AA; 56835 MW; 617134A5D78F028E CRC64;
MKKRTNSRGT PTSSGDALLD TSFSSAGDAE RDHPAYKSGA ASAPATPTKR RDGSDGSVSS
AGARRKRKDE IAQTFVIVNE RPVDDISLDF FYKPHTITLL AVSVLAVMYF AFVRNEANVD
ENLWAGLLCI VFFFLIVSVI AFPNGPFTRP HPAVWRILFG CSVLYLLTLQ FLMFQNYPTI
RSIFYWIDPK LKNFHIDMEK EYGVNCSDIS WDRVKGHLDV FAWGHFLGWA FKAILIRHMG
ILWAISVMWE ITEITFAHLL PNFIECWWDA LILDVIICNG LGIWMGLKIC QILEMREYKW
ASIKDISTTT GKIKRAMLQF TPESWSAIRW LDPKSTAMRF AAVIQLVIFW QVTELNTFFL
KHIFEMPPDH FIVIGRLIFI GLFVAPSVRQ YYVYVTDTRC KRVGTQCWVY GAIMVSEAIL
CIKNGKELFE RTQAINIVLW LTVQVIISVA FVYLAVYWQQ RQLKKVSSTP AKTKETIPAS
SSSPSKGKLS PQKEKKLK
