PTSS1_MOUSE
ID PTSS1_MOUSE Reviewed; 473 AA.
AC Q99LH2; O55024; Q3UV14; Q8C2S8;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphatidylserine synthase 1;
DE Short=PSS-1;
DE Short=PtdSer synthase 1;
DE EC=2.7.8.29 {ECO:0000269|PubMed:10432300, ECO:0000269|PubMed:10938271, ECO:0000269|PubMed:18343815, ECO:0000269|PubMed:9516423};
DE AltName: Full=Serine-exchange enzyme I;
GN Name=Ptdss1; Synonyms=Pssa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=9516423; DOI=10.1074/jbc.273.13.7293;
RA Stone S.J., Cui Z., Vance J.E.;
RT "Cloning and expression of mouse liver phosphatidylserine synthase-1 cDNA.
RT Overexpression in rat hepatoma cells inhibits the CDP-ethanolamine pathway
RT for phosphatidylethanolamine biosynthesis.";
RL J. Biol. Chem. 273:7293-7302(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Oviduct, Thymus, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10432300; DOI=10.1042/bj3420057;
RA Stone S.J., Vance J.E.;
RT "Cloning and expression of murine liver phosphatidylserine synthase (PSS)-
RT 2: differential regulation of phospholipid metabolism by PSS1 and PSS2.";
RL Biochem. J. 342:57-64(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10938271; DOI=10.1074/jbc.m002865200;
RA Stone S.J., Vance J.E.;
RT "Phosphatidylserine synthase-1 and -2 are localized to mitochondria-
RT associated membranes.";
RL J. Biol. Chem. 275:34534-34540(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18343815; DOI=10.1074/jbc.m800714200;
RA Arikketh D., Nelson R., Vance J.E.;
RT "Defining the importance of phosphatidylserine synthase-1 (PSS1):
RT unexpected viability of PSS1-deficient mice.";
RL J. Biol. Chem. 283:12888-12897(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-425, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:10432300, PubMed:9516423, PubMed:18343815,
CC PubMed:10938271). Catalyzes mainly the conversion of
CC phosphatidylcholine (PubMed:9516423, PubMed:18343815, PubMed:10432300,
CC PubMed:10938271). Also converts, in vitro and to a lesser extent,
CC phosphatidylethanolamine (PubMed:10432300, PubMed:9516423,
CC PubMed:18343815, PubMed:10938271). {ECO:0000269|PubMed:10432300,
CC ECO:0000269|PubMed:10938271, ECO:0000269|PubMed:18343815,
CC ECO:0000269|PubMed:9516423}.
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:10432300, ECO:0000269|PubMed:10938271,
CC ECO:0000269|PubMed:18343815, ECO:0000269|PubMed:9516423};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000305|PubMed:10432300};
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:10432300,
CC ECO:0000269|PubMed:10938271, ECO:0000269|PubMed:18343815,
CC ECO:0000269|PubMed:9516423};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45089;
CC Evidence={ECO:0000305|PubMed:9516423};
CC -!- ACTIVITY REGULATION: Potently inhibited by choline in the mitochondria-
CC associated membrane (MAM). Very little inhibition by choline in the
CC endoplasmic reticulum (ER) per se. {ECO:0000269|PubMed:10938271}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10938271}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10938271}. Note=Highly enriched in the
CC mitochondria-associated membrane (MAM).
CC -!- TISSUE SPECIFICITY: Expressed in kidney, testis, lung, skeletal muscle,
CC liver brain, heart and spleen with highest expression in testis, liver,
CC heart and brain. {ECO:0000269|PubMed:10432300}.
CC -!- DISRUPTION PHENOTYPE: Null mice are viable, fertile and have a normal
CC life span. Toal serine exchange is reduced up to 85%, but apart from in
CC liver, the phosphatatidylserine content was unaltered. Elimination of
CC either Pss1 or Pss2, but not both, is compatible with mouse viability.
CC Mice can tolerate as little as 10% serine-exchange activity and are
CC viable with small amounts of phosphatidylserine and
CC phosphatidylethanolamine content. to phosphatidylethanolamine.
CC {ECO:0000269|PubMed:18343815}.
CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC {ECO:0000305}.
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DR EMBL; AF042731; AAB97845.1; -; mRNA.
DR EMBL; AK036990; BAC29660.1; -; mRNA.
DR EMBL; AK054101; BAC35656.1; -; mRNA.
DR EMBL; AK085857; BAC39555.1; -; mRNA.
DR EMBL; AK088048; BAC40117.1; -; mRNA.
DR EMBL; AK137681; BAE23459.1; -; mRNA.
DR EMBL; BC003260; AAH03260.1; -; mRNA.
DR CCDS; CCDS26612.1; -.
DR RefSeq; NP_032985.2; NM_008959.3.
DR AlphaFoldDB; Q99LH2; -.
DR STRING; 10090.ENSMUSP00000021990; -.
DR iPTMnet; Q99LH2; -.
DR PhosphoSitePlus; Q99LH2; -.
DR SwissPalm; Q99LH2; -.
DR EPD; Q99LH2; -.
DR jPOST; Q99LH2; -.
DR MaxQB; Q99LH2; -.
DR PaxDb; Q99LH2; -.
DR PRIDE; Q99LH2; -.
DR ProteomicsDB; 301980; -.
DR Antibodypedia; 12969; 150 antibodies from 23 providers.
DR DNASU; 19210; -.
DR Ensembl; ENSMUST00000021990; ENSMUSP00000021990; ENSMUSG00000021518.
DR GeneID; 19210; -.
DR KEGG; mmu:19210; -.
DR UCSC; uc007qzz.1; mouse.
DR CTD; 9791; -.
DR MGI; MGI:1276575; Ptdss1.
DR VEuPathDB; HostDB:ENSMUSG00000021518; -.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR HOGENOM; CLU_037661_3_0_1; -.
DR InParanoid; Q99LH2; -.
DR OMA; QYYMYVT; -.
DR OrthoDB; 818196at2759; -.
DR PhylomeDB; Q99LH2; -.
DR TreeFam; TF300012; -.
DR BRENDA; 2.7.8.29; 3474.
DR Reactome; R-MMU-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR BioGRID-ORCS; 19210; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Ptdss1; mouse.
DR PRO; PR:Q99LH2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q99LH2; protein.
DR Bgee; ENSMUSG00000021518; Expressed in external carotid artery and 270 other tissues.
DR ExpressionAtlas; Q99LH2; baseline and differential.
DR Genevisible; Q99LH2; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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; ISO:MGI.
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; 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_0000056830"
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 428..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..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:0007744|PubMed:21183079"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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"
FT CONFLICT 166
FT /note="D -> E (in Ref. 1; AAB97845)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..171
FT /note="AFG -> SFA (in Ref. 1; AAB97845)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="C -> H (in Ref. 1; AAB97845)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="F -> L (in Ref. 2; BAC40117)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> G (in Ref. 1; AAB97845)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="F -> S (in Ref. 1; AAB97845)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="G -> C (in Ref. 1; AAB97845 and 2; BAC40117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 55604 MW; F185CA20FFADB84A CRC64;
MASCVGSRTL SKDDVNYRMH FRMINEQQVE DITIDFFYRP HTITLLSFTI ISLMYFAFTR
DDSVPEDNIW 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 WGRILFIGCI TAPTVRQYYA YLTDTQCKRV GTQCWVFGVI
GFLEAIVCIK FGQDLFSKTQ ILYVMLWLLC VAFTTFLCLY GMVWYAEHYG HREKTYSECE
DGTYSPEISW HHGKGSKGSE DSPPKHSSNH ESHSSRRRNR HSKSKVTNGV GKK
