PTSS1_RAT
ID PTSS1_RAT Reviewed; 473 AA.
AC Q5PQL5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phosphatidylserine synthase 1;
DE Short=PSS-1;
DE Short=PtdSer synthase 1;
DE EC=2.7.8.29 {ECO:0000250|UniProtKB:P48651};
DE AltName: Full=Serine-exchange enzyme I;
GN Name=Ptdss1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 mainly the conversion
CC of phosphatidylcholine but also converts, in vitro and to a lesser
CC extent, phosphatidylethanolamine (By similarity).
CC {ECO:0000250|UniProtKB:P48651}.
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:P48651};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000250|UniProtKB:P48651};
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:0000250|UniProtKB:P48651};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45089;
CC Evidence={ECO:0000250|UniProtKB:P48651};
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; BC087129; AAH87129.1; -; mRNA.
DR RefSeq; NP_001012113.1; NM_001012113.1.
DR AlphaFoldDB; Q5PQL5; -.
DR STRING; 10116.ENSRNOP00000006317; -.
DR jPOST; Q5PQL5; -.
DR PaxDb; Q5PQL5; -.
DR PRIDE; Q5PQL5; -.
DR Ensembl; ENSRNOT00000087143; ENSRNOP00000072374; ENSRNOG00000052289.
DR GeneID; 314553; -.
DR KEGG; rno:314553; -.
DR UCSC; RGD:1308949; rat.
DR CTD; 9791; -.
DR RGD; 1308949; Ptdss1.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR InParanoid; Q5PQL5; -.
DR OrthoDB; 818196at2759; -.
DR PhylomeDB; Q5PQL5; -.
DR Reactome; R-RNO-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR PRO; PR:Q5PQL5; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106258; F:L-serine-phosphatidylcholine phosphatidyltransferase activity; ISO:RGD.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; ISO:RGD.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; ISO:RGD.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT CHAIN 2..473
FT /note="Phosphatidylserine synthase 1"
FT /id="PRO_0000416030"
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..186
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..355
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..473
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 430..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..473
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 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48651"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48651"
SQ SEQUENCE 473 AA; 55664 MW; 13C0700317D1EC1C CRC64;
MASCVGSRTL SKDDVNYRMH FRMINEQQVE DITIDFFYRP HTITLLSFTI ISLMYFAFTR
DDCVPEDNIW RGILSVIFFF LIISVLAFPN GPFTRPHPAL WRMVFGLSVL YFLFLVFLLF
LNFEQVKSLM YWLDPNLRYA TREADIMEYA VNCHVITWER IVSHFDIFAF GHFWGWAMKA
LLIRSYGLCW TISITWELTE LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL
EMRTYHWASF KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGI YLFMIIWQLT
ELNTFFLKHI FVFQASHPLS WCRILFIGCI TAPTVRQYYA YLTDTQCKRV GTQCWVFGVI
GFLEAIVCIK FGQDLFSKTQ ILYVVLWLLC VAFTTFLCLY GMVWYAEHYG HREKTYSECE
DGTYSPEISW YHGKGSKGSE DSPPKHSNNN ESHSSRRRNR HSKSKVTNGV GKK
