ID   PTSS1_HUMAN             Reviewed;         473 AA.
AC   P48651; B4DE85; E5RFC5; Q9BUQ5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Phosphatidylserine synthase 1;
DE            Short=PSS-1;
DE            Short=PtdSer synthase 1;
DE            EC=2.7.8.29 {ECO:0000269|PubMed:19014349, ECO:0000269|PubMed:24241535};
DE   AltName: Full=Serine-exchange enzyme I;
GN   Name=PTDSS1; Synonyms=KIAA0024, PSSA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA   Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA   Nagase T., Seki N., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. I. The
RT   coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT   randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL   DNA Res. 1:27-35(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, Lymph, and Muscle;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-425, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19014349; DOI=10.1042/bj20081597;
RA   Tomohiro S., Kawaguti A., Kawabe Y., Kitada S., Kuge O.;
RT   "Purification and characterization of human phosphatidylserine synthases 1
RT   and 2.";
RL   Biochem. J. 418:421-429(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442 AND SER-454, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-425, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   VARIANTS LMHD PRO-265; SER-269 AND ARG-353, CHARACTERIZATION OF VARIANTS
RP   LMHD PRO-265; SER-269 AND ARG-353, FUNCTION, CATALYTIC ACTIVITY, AND
RP   ACTIVITY REGULATION.
RX   PubMed=24241535; DOI=10.1038/ng.2829;
RA   Sousa S.B., Jenkins D., Chanudet E., Tasseva G., Ishida M., Anderson G.,
RA   Docker J., Ryten M., Sa J., Saraiva J.M., Barnicoat A., Scott R.,
RA   Calder A., Wattanasirichaigoon D., Chrzanowska K., Simandlova M.,
RA   Van Maldergem L., Stanier P., Beales P.L., Vance J.E., Moore G.E.;
RT   "Gain-of-function mutations in the phosphatidylserine synthase 1 (PTDSS1)
RT   gene cause Lenz-Majewski syndrome.";
RL   Nat. Genet. 46:70-76(2014).
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:19014349, PubMed:24241535). Catalyzes
CC       mainly the conversion of phosphatidylcholine (PubMed:19014349,
CC       PubMed:24241535). Also converts, in vitro and to a lesser extent,
CC       phosphatidylethanolamine (PubMed:19014349, PubMed:24241535).
CC       {ECO:0000269|PubMed:19014349, ECO:0000269|PubMed:24241535}.
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:19014349, ECO:0000269|PubMed:24241535};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC         Evidence={ECO:0000305|PubMed:19014349};
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:19014349,
CC         ECO:0000269|PubMed:24241535};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45089;
CC         Evidence={ECO:0000305|PubMed:19014349};
CC   -!- ACTIVITY REGULATION: Requires calcium ions (PubMed:19014349). Inhibited
CC       by exogenous phosphatidylserine (PubMed:24241535).
CC       {ECO:0000269|PubMed:19014349, ECO:0000269|PubMed:24241535}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=67 uM for serine (in the presence of 2 mM PC)
CC         {ECO:0000269|PubMed:19014349};
CC         KM=24 uM for serine (in the presence of 1 mM PE)
CC         {ECO:0000269|PubMed:19014349};
CC       pH dependence:
CC         Optimum pH for both PC and PE is between 7.0 and 7.5.
CC         {ECO:0000269|PubMed:19014349};
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P48651-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P48651-2; Sequence=VSP_055980;
CC       Name=3;
CC         IsoId=P48651-3; Sequence=VSP_057421, VSP_057422;
CC   -!- DISEASE: Lenz-Majewski hyperostotic dwarfism (LMHD) [MIM:151050]: A
CC       syndrome of intellectual disability and multiple congenital anomalies
CC       that features generalized craniotubular hyperostosis. LMHD is
CC       characterized by the combination of sclerosing bone dysplasia,
CC       intellectual disability and distinct craniofacial, dental, cutaneous
CC       and distal limb anomalies. The progressive generalized hyperostosis
CC       associated with this syndrome affects the cranium, the vertebrae and
CC       the diaphyses of tubular bones, leading to severe growth restriction.
CC       {ECO:0000269|PubMed:24241535}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; D14694; BAA03520.1; -; mRNA.
DR   EMBL; AK293513; BAG56996.1; -; mRNA.
DR   EMBL; AP003465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KC877275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004192; AAH04192.1; -; mRNA.
DR   EMBL; BC002376; AAH02376.2; -; mRNA.
DR   EMBL; BC004390; AAH04390.1; -; mRNA.
DR   CCDS; CCDS6271.1; -. [P48651-1]
DR   RefSeq; NP_001277154.1; NM_001290225.1. [P48651-2]
DR   RefSeq; NP_055569.1; NM_014754.2. [P48651-1]
DR   AlphaFoldDB; P48651; -.
DR   BioGRID; 115135; 220.
DR   IntAct; P48651; 28.
DR   MINT; P48651; -.
DR   STRING; 9606.ENSP00000430548; -.
DR   DrugBank; DB00144; Phosphatidyl serine.
DR   SwissLipids; SLP:000001060; -.
DR   GlyGen; P48651; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P48651; -.
DR   MetOSite; P48651; -.
DR   PhosphoSitePlus; P48651; -.
DR   SwissPalm; P48651; -.
DR   BioMuta; PTDSS1; -.
DR   DMDM; 1346881; -.
DR   EPD; P48651; -.
DR   jPOST; P48651; -.
DR   MassIVE; P48651; -.
DR   MaxQB; P48651; -.
DR   PaxDb; 9606-ENSP00000430548; -.
DR   PeptideAtlas; P48651; -.
DR   ProteomicsDB; 3928; -.
DR   ProteomicsDB; 55920; -. [P48651-1]
DR   ProteomicsDB; 79120; -.
DR   Pumba; P48651; -.
DR   Antibodypedia; 12969; 172 antibodies from 23 providers.
DR   DNASU; 9791; -.
DR   Ensembl; ENST00000517309.6; ENSP00000430548.1; ENSG00000156471.13. [P48651-1]
DR   Ensembl; ENST00000522072.1; ENSP00000430928.1; ENSG00000156471.13. [P48651-3]
DR   GeneID; 9791; -.
DR   KEGG; hsa:9791; -.
DR   MANE-Select; ENST00000517309.6; ENSP00000430548.1; NM_014754.3; NP_055569.1.
DR   UCSC; uc003yht.2; human. [P48651-1]
DR   UCSC; uc064ouh.1; human.
DR   AGR; HGNC:9587; -.
DR   CTD; 9791; -.
DR   DisGeNET; 9791; -.
DR   GeneCards; PTDSS1; -.
DR   HGNC; HGNC:9587; PTDSS1.
DR   HPA; ENSG00000156471; Low tissue specificity.
DR   MalaCards; PTDSS1; -.
DR   MIM; 151050; phenotype.
DR   MIM; 612792; gene.
DR   neXtProt; NX_P48651; -.
DR   OpenTargets; ENSG00000156471; -.
DR   Orphanet; 2658; Lenz-Majewski hyperostotic dwarfism.
DR   PharmGKB; PA33939; -.
DR   VEuPathDB; HostDB:ENSG00000156471; -.
DR   eggNOG; KOG2735; Eukaryota.
DR   GeneTree; ENSGT00530000063576; -.
DR   HOGENOM; CLU_037661_3_0_1; -.
DR   InParanoid; P48651; -.
DR   OMA; QYYMYVT; -.
DR   OrthoDB; 3933684at2759; -.
DR   PhylomeDB; P48651; -.
DR   TreeFam; TF300012; -.
DR   BioCyc; MetaCyc:HS08129-MONOMER; -.
DR   BRENDA; 2.7.8.29; 2681.
DR   PathwayCommons; P48651; -.
DR   Reactome; R-HSA-1483101; Synthesis of PS.
DR   SignaLink; P48651; -.
DR   UniPathway; UPA00948; -.
DR   BioGRID-ORCS; 9791; 161 hits in 1159 CRISPR screens.
DR   ChiTaRS; PTDSS1; human.
DR   GenomeRNAi; 9791; -.
DR   Pharos; P48651; Tbio.
DR   PRO; PR:P48651; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P48651; Protein.
DR   Bgee; ENSG00000156471; Expressed in cortical plate and 207 other cell types or tissues.
DR   ExpressionAtlas; P48651; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0106258; F:L-serine-phosphatidylcholine phosphatidyltransferase activity; IDA:FlyBase.
DR   GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IDA:FlyBase.
DR   GO; GO:0016740; F:transferase activity; TAS:Reactome.
DR   GO; GO:0006659; P:phosphatidylserine biosynthetic process; IDA:FlyBase.
DR   InterPro; IPR004277; PSS.
DR   PANTHER; PTHR15362; PHOSPHATIDYLINOSITOL SYNTHASE; 1.
DR   PANTHER; PTHR15362:SF15; PHOSPHATIDYLSERINE SYNTHASE 1; 1.
DR   Pfam; PF03034; PSS; 1.
DR   Genevisible; P48651; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Disease variant; Dwarfism;
KW   Endoplasmic reticulum; Intellectual disability; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   CHAIN           2..473
FT                   /note="Phosphatidylserine synthase 1"
FT                   /id="PRO_0000056829"
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        430..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:0007744|PubMed:25944712"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231"
FT   MOD_RES         454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VAR_SEQ         1..203
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057421"
FT   VAR_SEQ         1..146
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055980"
FT   VAR_SEQ         449..473
FT                   /note="NNESHSSRRRNRHSKSKVTNGVGKK -> EGTWGSLFEIVSLVSHRPGRVRQ
FT                   IIAWGAFANVGSLLTSALDMRSPVAARCVEGKR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057422"
FT   VARIANT         265
FT                   /note="L -> P (in LMHD; does not affect protein levels;
FT                   increases the rate of phosphatidylserine synthesis;
FT                   profoundly impairs negative feedback enzyme regulation by
FT                   phosphatidylserine; dbSNP:rs587777090)"
FT                   /evidence="ECO:0000269|PubMed:24241535"
FT                   /id="VAR_070987"
FT   VARIANT         269
FT                   /note="P -> S (in LMHD; does not affect protein levels;
FT                   increases the rate of phosphatidylserine synthesis;
FT                   profoundly impairs negative feedback enzyme regulation by
FT                   phosphatidylserine; dbSNP:rs587777089)"
FT                   /evidence="ECO:0000269|PubMed:24241535"
FT                   /id="VAR_070988"
FT   VARIANT         353
FT                   /note="Q -> R (in LMHD; does not affect protein levels;
FT                   increases the rate of phosphatidylserine synthesis;
FT                   profoundly impairs negative feedback enzyme regulation by
FT                   phosphatidylserine; dbSNP:rs587777088)"
FT                   /evidence="ECO:0000269|PubMed:24241535"
FT                   /id="VAR_070989"
FT   VARIANT         423
FT                   /note="T -> N (in dbSNP:rs7835798)"
FT                   /id="VAR_048735"
SQ   SEQUENCE   473 AA;  55528 MW;  CFC8F50A33CE038D CRC64;
     MASCVGSRTL SKDDVNYKMH FRMINEQQVE DITIDFFYRP HTITLLSFTI VSLMYFAFTR
     DDSVPEDNIW RGILSVIFFF LIISVLAFPN GPFTRPHPAL WRMVFGLSVL YFLFLVFLLF
     LNFEQVKSLM YWLDPNLRYA TREADVMEYA VNCHVITWER IISHFDIFAF GHFWGWAMKA
     LLIRSYGLCW TISITWELTE LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL
     EMRTYHWASF KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGV YLFMIIWQLT
     ELNTFFLKHI FVFQASHPLS WGRILFIGGI TAPTVRQYYA YLTDTQCKRV GTQCWVFGVI
     GFLEAIVCIK FGQDLFSKTQ ILYVVLWLLC VAFTTFLCLY GMIWYAEHYG HREKTYSECE
     DGTYSPEISW HHRKGTKGSE DSPPKHAGNN ESHSSRRRNR HSKSKVTNGV GKK
//