PTSS2_CRIGR
ID PTSS2_CRIGR Reviewed; 474 AA.
AC O08888;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Phosphatidylserine synthase 2;
DE Short=PSS-2;
DE Short=PtdSer synthase 2;
DE EC=2.7.8.29 {ECO:0000269|PubMed:12912985, ECO:0000269|PubMed:3084470, ECO:0000269|PubMed:9235902};
DE AltName: Full=Serine-exchange enzyme II;
GN Name=PTDSS2; Synonyms=PSS2, PSSB;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Ovary;
RX PubMed=9235902; DOI=10.1074/jbc.272.31.19133;
RA Kuge O., Saito K., Nishijima M.;
RT "Cloning of a Chinese hamster ovary (CHO) cDNA encoding phosphatidylserine
RT synthase (PSS) II, overexpression of which suppresses the
RT phosphatidylserine biosynthetic defect of a PSS I-lacking mutant of CHO-K1
RT cells.";
RL J. Biol. Chem. 272:19133-19139(1997).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3084470; DOI=10.1016/s0021-9258(17)38451-x;
RA Kuge O., Nishijima M., Akamatsu Y.;
RT "Phosphatidylserine biosynthesis in cultured Chinese hamster ovary cells.
RT II. Isolation and characterization of phosphatidylserine auxotrophs.";
RL J. Biol. Chem. 261:5790-5794(1986).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12912985; DOI=10.1074/jbc.m307270200;
RA Kuge O., Hasegawa K., Ohsawa T., Saito K., Nishijima M.;
RT "Purification and characterization of Chinese hamster phosphatidylserine
RT synthase 2.";
RL J. Biol. Chem. 278:42692-42698(2003).
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 (PubMed:12912985, PubMed:9235902). Catalyzes the
CC conversion of phosphatatidylethanolamine and does not act on
CC phosphatidylcholine (PubMed:12912985, PubMed:9235902). Shows a
CC substrate specificity for phosphatatidylethanolamine and does not act
CC on phosphatidylcholine (By similarity). Can utilize both
CC phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate
CC and the latter is six times better utilized, indicating the importance
CC of an ester linkage at the sn-1 position (By similarity). Although it
CC shows no sn-1 fatty acyl preference, exhibits significant preference
CC towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at
CC the sn-2 position (By similarity). {ECO:0000250|UniProtKB:Q9Z1X2,
CC ECO:0000269|PubMed:12912985, ECO:0000269|PubMed:9235902}.
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:12912985, ECO:0000269|PubMed:3084470,
CC ECO:0000269|PubMed:9235902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000305|PubMed:9235902};
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 -!- ACTIVITY REGULATION: Inhibited by excess phosphatidylserine, but not by
CC phosphatidylcholine nor phosphatidylethanolamine.
CC {ECO:0000269|PubMed:12912985}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=89 uM for L-serine {ECO:0000269|PubMed:12912985};
CC Vmax=0.29 nmol/h/ng enzyme for L-serine
CC {ECO:0000269|PubMed:12912985};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein
CC {ECO:0000255}. Membrane {ECO:0000269|PubMed:12912985}. Note=Highly
CC enriched in the mitochondria-associated membrane (MAM).
CC {ECO:0000250|UniProtKB:Q9Z1X2}.
CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC {ECO:0000305}.
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DR EMBL; AB004109; BAA20355.1; -; mRNA.
DR RefSeq; NP_001233636.1; NM_001246707.1.
DR AlphaFoldDB; O08888; -.
DR STRING; 10029.NP_001233636.1; -.
DR Ensembl; ENSCGRT00001002796; ENSCGRP00001002183; ENSCGRG00001002279.
DR GeneID; 100689448; -.
DR KEGG; cge:100689448; -.
DR CTD; 81490; -.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR OrthoDB; 818196at2759; -.
DR BRENDA; 2.7.8.29; 1309.
DR UniPathway; UPA00948; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..474
FT /note="Phosphatidylserine synthase 2"
FT /id="PRO_0000056831"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..74
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..291
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..474
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GV22"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1X2"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVG9"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 55005 MW; 81942E4310F538C2 CRC64;
MRRAERRVAG GSGSGSPLLE GRRSTESEVY DDGTNTFFWR AHTLTVLFIL TCSLGYVTLL
EETPQDTAYN TKRGIVASIL VFLCFGVTQA KDGPFSRPHP AYWRFWLCVS VVYELFLIFI
LFQTVQDGRQ FLKYVDPRLG VPLPERDYGG NCLIYDADNK TDPFHNIWDK LDGFVPAHFI
GWYLKTLMIR DWWMCMIISV MFEFLEYSLE HQLPNFSECW WDHWIMDVLI CNGLGIYCGM
KTLEWLSLKT YKWQGLWNIP TYKGKMKRIA FQFTPYSWVR FEWKPASSLH RWLAVCGIIL
VFLLAELNTF YLKFVLWMPP EHYLVLLRLV FFVNVGGVAM REIYDFMDEL KPHRKLGQQA
WLVAAITVTE LLIVVKYDPH TLTLSLPFYI SQCWTLGSIL VLTWTVWRFF LRDITMRYKE
TRRQKQQSHQ GRAINNGDGH PGPDDDLLGT GTAEEEGSTN DSVPAEKEGA SAAS
