PTSS1_HUMAN
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 03-AUG-2022, entry version 170.
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; 198.
DR IntAct; P48651; 27.
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; P48651; -.
DR PeptideAtlas; P48651; -.
DR PRIDE; P48651; -.
DR ProteomicsDB; 3928; -.
DR ProteomicsDB; 55920; -. [P48651-1]
DR ProteomicsDB; 79120; -.
DR Antibodypedia; 12969; 150 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 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; 818196at2759; -.
DR PhylomeDB; P48651; -.
DR TreeFam; TF300012; -.
DR BioCyc; MetaCyc:HS08129-MON; -.
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; 145 hits in 1082 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 205 other tissues.
DR ExpressionAtlas; P48651; baseline and differential.
DR Genevisible; P48651; HS.
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; 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 Pfam; PF03034; PSS; 1.
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
