PTSS2_DANRE
ID PTSS2_DANRE Reviewed; 452 AA.
AC E7EY42;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Phosphatidylserine synthase 2;
DE Short=PSS-2;
DE Short=PtdSer synthase 2;
DE EC=2.7.8.29 {ECO:0000250|UniProtKB:Q9Z1X2};
DE AltName: Full=Serine-exchange enzyme II;
GN Name=ptdss2; ORFNames=si:ch1073-158c2, si:ch1073-279O1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Catalyzes a base-exchange reaction in which the polar head
CC group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is
CC replaced by L-serine (By similarity). Catalyzes the conversion of
CC phosphatatidylethanolamine and does not act on phosphatidylcholine (By
CC similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen
CC and diacyl PE as substrate and the latter is six times better utilized,
CC indicating the importance of an ester linkage at the sn-1 position (By
CC similarity). Although it shows no sn-1 fatty acyl preference, exhibits
CC significant preference towards docosahexaenoic acid (22:6n-3) compared
CC with 18:1 or 20:4 at the sn-2 position (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z1X2}.
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:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + L-serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:41484,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:73007,
CC ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41485;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphoethanolamine + L-serine = 1-hexadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine +
CC ethanolamine; Xref=Rhea:RHEA:41488, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78261, ChEBI:CHEBI:78262;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41489;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphoserine + ethanolamine;
CC Xref=Rhea:RHEA:41500, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:78268, ChEBI:CHEBI:78269;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41501;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine +
CC ethanolamine; Xref=Rhea:RHEA:41492, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78265, ChEBI:CHEBI:78266;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41493;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenyl)-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-
CC sn-glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-L-serine
CC + ethanolamine; Xref=Rhea:RHEA:41496, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78263, ChEBI:CHEBI:78264;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41497;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + L-serine = 1-octadecanoyl-2-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:40795,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:75038,
CC ChEBI:CHEBI:78260; Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40796;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine;
CC Xref=Rhea:RHEA:41600, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:78340, ChEBI:CHEBI:78341;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41601;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenyl)-2-(5Z,8Z,11Z,14Z- eicosatetraenoyl)-sn-
CC glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine +
CC ethanolamine; Xref=Rhea:RHEA:41604, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78342, ChEBI:CHEBI:78343;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41605;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Highly enriched in the mitochondria-associated
CC membrane (MAM). {ECO:0000250|UniProtKB:Q9Z1X2}.
CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC {ECO:0000305}.
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DR EMBL; CU633741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU633764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001337112.2; XM_001337076.6.
DR AlphaFoldDB; E7EY42; -.
DR STRING; 7955.ENSDARP00000086456; -.
DR PaxDb; E7EY42; -.
DR PeptideAtlas; E7EY42; -.
DR Ensembl; ENSDART00000161593; ENSDARP00000138215; ENSDARG00000101018.
DR GeneID; 100004136; -.
DR KEGG; dre:100004136; -.
DR CTD; 81490; -.
DR ZFIN; ZDB-GENE-130424-2; ptdss2.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR HOGENOM; CLU_037661_4_1_1; -.
DR InParanoid; E7EY42; -.
DR OMA; MKYIDPN; -.
DR OrthoDB; 818196at2759; -.
DR PhylomeDB; E7EY42; -.
DR TreeFam; TF300012; -.
DR Reactome; R-DRE-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR PRO; PR:E7EY42; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000101018; Expressed in mature ovarian follicle and 20 other tissues.
DR ExpressionAtlas; E7EY42; baseline and differential.
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:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..452
FT /note="Phosphatidylserine synthase 2"
FT /id="PRO_0000416036"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..69
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..349
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..452
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 53229 MW; 0C837744DD2F9899 CRC64;
MAKGEWKRSG ADDLPLPGRS ECEVFDDGTN TFFWRAHTVT VLFILTCALV YVTLLEETPH
DTAYNTKRGI VASILVFLCF GVTQAKDGPF TRPHPAYWRF WLCVSVVYEL FLIFILFQTV
HDGRQFMKYI DPKLGVPLPE RGYGGNCLIY DPGHPTDPFH NIWDKMDGFV PAHFLGWYIK
TLMIRDWWMC MIISVMFEFL EYSLEHQLPN FSECWWDHWI MDVLVCNGLG IYCGMKTLGW
LSMKPYQWQG LWNIPTYKGK IKRIAFQFTP YSWVKFEWRP ASNLRRWLAV LGIIFMFLLA
ELNTFYLKFV MWMPPEHYLV LFRLVFFVNV GGVAMREIYD FMDDPKFHKK LGQQAWIVAA
ITVTEFLIVV KYDPNTIMLP IPFFITQCWI LGIALILVWT LWRFFIRDIT LRYKETRRRR
QEVSSERDGS SSAPSGRSKL NGSMDSVRHR KS
