PTSS2_XENTR
ID PTSS2_XENTR Reviewed; 474 AA.
AC Q08D11; F7D5B0;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 67.
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;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; AAMC01058853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01058854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC123999; AAI24000.1; -; mRNA.
DR RefSeq; NP_001072672.1; NM_001079204.1.
DR AlphaFoldDB; Q08D11; -.
DR STRING; 8364.ENSXETP00000056764; -.
DR PaxDb; Q08D11; -.
DR PRIDE; Q08D11; -.
DR DNASU; 780129; -.
DR Ensembl; ENSXETT00000056764; ENSXETP00000056764; ENSXETG00000027078.
DR GeneID; 780129; -.
DR KEGG; xtr:780129; -.
DR CTD; 81490; -.
DR Xenbase; XB-GENE-988429; ptdss2.
DR eggNOG; KOG2735; Eukaryota.
DR HOGENOM; CLU_037661_4_1_1; -.
DR InParanoid; Q08D11; -.
DR OMA; MKYIDPN; -.
DR OrthoDB; 818196at2759; -.
DR TreeFam; TF300012; -.
DR Reactome; R-XTR-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000027078; Expressed in egg cell and 12 other tissues.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..474
FT /note="Phosphatidylserine synthase 2"
FT /id="PRO_0000416037"
FT TOPO_DOM 1..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..126
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..403
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 448..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 45
FT /note="S -> R (in Ref. 2; AAI24000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 56214 MW; 663ABF502D43CFE1 CRC64;
MLRSDVRRVA AGRKASLDGL YCEELEVRGN RNLGNKFSHR GELRSSTESE VFDDGTNTFF
WRAHTLTVLF ILTCSLGYVT LLEETPQDTA YNAKRGIIAS ILVFLCFGVT QAKDGPFSRP
HPAYWRFWLC VSVVYELFLI FILFQTVHDG RQFMKFIDPK LGVPLPERDY GGNCLIYDPG
NKTDPYHNLW DKMDGFVPAH FLGWYIKTLM IRDWWMCMII SVMFEFLEYS LEHQLPNFSE
CWWDHWIMDV LVCNGFGIYC GMKTLEWLSM KPYKWQGLWN IPTYRGKMKR IAFQFTPYSW
VKFEWKPASS LRRWLAVCGI IFVFLLAELN TFYLKFVLWM PPEHYLVLLR LVFFVNVGGV
AMREIYDFMD DLKFHKKLGQ QAWMVAAITV TEFLIVVKYD PYTITLPLPF YVTQCWILGI
VLVLTWTVWR FFIRDITLRY KEIRQQKQHR NEEEKSHRNG DVNSEKDTNK HKKH
