PTSS1_CRIGR
ID PTSS1_CRIGR Reviewed; 471 AA.
AC Q00576;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Phosphatidylserine synthase 1;
DE Short=PSS-1;
DE Short=PtdSer synthase 1;
DE EC=2.7.8.29 {ECO:0000269|PubMed:1748687, ECO:0000269|PubMed:3084470, ECO:0000269|PubMed:9539713};
DE AltName: Full=Serine-exchange enzyme I;
GN Name=PTDSS1; Synonyms=PSSA;
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=1748687; DOI=10.1016/s0021-9258(18)54410-0;
RA Kuge O., Nishijima M., Akamatsu Y.;
RT "A Chinese hamster cDNA encoding a protein essential for phosphatidylserine
RT synthase I activity.";
RL J. Biol. Chem. 266:24184-24189(1991).
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, AND MUTAGENESIS OF
RP ARG-95.
RX PubMed=9539713; DOI=10.1073/pnas.95.8.4199;
RA Kuge O., Hasegawa K., Saito K., Nishijima M.;
RT "Control of phosphatidylserine biosynthesis through phosphatidylserine-
RT mediated inhibition of phosphatidylserine synthase I in Chinese hamster
RT ovary cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4199-4203(1998).
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:1748687, PubMed:3084470, PubMed:9539713).
CC Catalyzes mainly the conversion of phosphatidylcholine (PubMed:1748687,
CC PubMed:3084470, PubMed:9539713). Also converts, in vitro and to a
CC lesser extent, phosphatidylethanolamine (PubMed:1748687,
CC PubMed:3084470, PubMed:9539713). {ECO:0000269|PubMed:1748687,
CC ECO:0000269|PubMed:3084470, ECO:0000269|PubMed:9539713}.
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:1748687, ECO:0000269|PubMed:3084470,
CC ECO:0000269|PubMed:9539713};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000305|PubMed:3084470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + L-serine = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + choline; Xref=Rhea:RHEA:45088,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:1748687,
CC ECO:0000269|PubMed:3084470, ECO:0000269|PubMed:9539713};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45089;
CC Evidence={ECO:0000305|PubMed:3084470};
CC -!- ACTIVITY REGULATION: Inhibited by exogenous phosphatidylserine.
CC {ECO:0000269|PubMed:9539713}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99LH2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q99LH2}. Note=Highly enriched in the
CC mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q99LH2}.
CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC {ECO:0000305}.
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DR EMBL; D10234; BAA01084.1; -; mRNA.
DR AlphaFoldDB; Q00576; -.
DR STRING; 10029.XP_007620671.1; -.
DR PRIDE; Q00576; -.
DR Ensembl; ENSCGRT00001021627; ENSCGRP00001017383; ENSCGRG00001017439.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
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:0106258; F:L-serine-phosphatidylcholine phosphatidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT CHAIN 2..471
FT /note="Phosphatidylserine synthase 1"
FT /id="PRO_0000056828"
FT TOPO_DOM 2..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..72
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..160
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..309
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..380
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 426..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT MUTAGEN 95
FT /note="R->K: Resistant to inhibition by exogenous
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:9539713"
SQ SEQUENCE 471 AA; 55350 MW; 6D995F2FBA53A29F CRC64;
MASCVGSRTL SKDDVNYRMH FRMINEQQVE DITIDFFYRP HTITLLSFTI VSLMYFAFTR
DDSVPEDNIW RGILSVIFFF LIISVLAFPN GPFTRPHPAL WRMVFGLSVL YFLFLVFLLF
LNFEQVKSLM YWLDPNLRYA TREADIMEYA VNCHVITWER IVSHFDIFAF GHFWGWAMKA
LLIRSYGLCW TISITWELTE LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL
EMRTYHWASF KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGV YLFMIIWQLT
ELNTFFLKHI FVFQASHPLS WCRILFIGCI TAPTVRQYYA YLTDTQCKRV GTQCWVFGVI
GFLEAIVCIK FGQDLFSKTQ ILYVVFWLLC VAFTTFLCLY GMVWYAEHYG HREKTYSECE
DGTPEISWHH GKGSKGSEDS PPKHSSNNES HSSRRRNRHS KSKVTNGVGK K
