PTSS1_XENTR
ID PTSS1_XENTR Reviewed; 465 AA.
AC B1H3H9;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
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};
GN Name=ptdss1;
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 MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) 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 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; BC161401; AAI61401.1; -; mRNA.
DR EMBL; BC166380; AAI66380.1; -; mRNA.
DR RefSeq; NP_001120508.1; NM_001127036.1.
DR AlphaFoldDB; B1H3H9; -.
DR GeneID; 100145636; -.
DR KEGG; xtr:100145636; -.
DR CTD; 9791; -.
DR Xenbase; XB-GENE-6455449; ptdss1.
DR InParanoid; B1H3H9; -.
DR OrthoDB; 818196at2759; -.
DR Reactome; R-XTR-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
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:0106258; F:L-serine-phosphatidylcholine phosphatidyltransferase activity; IEA:RHEA.
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..465
FT /note="Phosphatidylserine synthase 1"
FT /id="PRO_0000416033"
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..68
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..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..465
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 440..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 54786 MW; 7C3B5FD19139847E CRC64;
MVSAMRSRTL SKDDVNYKMH FRMINEQQVE DITIDFFYKP HTITLLTFTT VSLMYFAFTR
ENTSQEDNIW KGILSVIFFF LIISVLAFPN GPFTRPHPAI WRMVFGLSVL YFLFLVFLLF
LNVEQVKAVM YWLDPNLRYA TRESDVMEYA VNCHVITWER ILSHFDIFAF GHFWGWAMKA
LLIRSYGLCW TISITWEMTE LFFMHLLPNF AECWWDQVIL DILLCNGGGI LLGMVVCRFL
EMRTYHWASF KDIHTTTGKI KRAVLQFTPA SWIYVRWFDP KSSFQRVAGV YLFMIIWQLT
ELNTFFLKHI FVFQASHPLS WCRILFIGII TAPTVRQYYA YLTDTQCKRV GTQCWVFGAI
AFLEATVCIK FGQDLFSKTH LLYVFLWLFS VAVITFLCLY GMVWYADYCG QREKTFSECE
DSTYNTDIPW HHIDKPVEAP VKQNEGTSRR KNRHKGKVTN GVGKK
