ID PTSS2_HUMAN Reviewed; 487 AA. AC Q9BVG9; DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=Phosphatidylserine synthase 2; DE Short=PSS-2; DE Short=PtdSer synthase 2; DE EC=2.7.8.29 {ECO:0000269|PubMed:19014349}; DE AltName: Full=Serine-exchange enzyme II; GN Name=PTDSS2; Synonyms=PSS2; 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]. RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-485, AND RP IDENTIFICATION BY 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 [7] 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 [8] 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 [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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-16, AND IDENTIFICATION BY RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP 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-16, AND IDENTIFICATION BY RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-24, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(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). Catalyzes the conversion of CC phosphatatidylethanolamine and does not act on phosphatidylcholine CC (PubMed:19014349). Can utilize both phosphatidylethanolamine (PE) CC plasmalogen and diacyl PE as substrate and the latter is six times CC better utilized, indicating the importance of an ester linkage at the CC sn-1 position (By similarity). Although it shows no sn-1 fatty acyl CC preference, exhibits significant preference towards docosahexaenoic CC acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By CC similarity). {ECO:0000250|UniProtKB:Q9Z1X2, CC ECO:0000269|PubMed:19014349}. 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}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607; CC Evidence={ECO:0000305|PubMed:19014349}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoethanolamine + L-serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)- CC sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:41484, CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:73007, CC ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41485; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- CC glycero-3-phosphoethanolamine + L-serine = 1-hexadecanoyl-2- CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine + CC ethanolamine; Xref=Rhea:RHEA:41488, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78261, ChEBI:CHEBI:78262; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41489; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero- CC 3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)- CC eicosatetraenoyl-sn-glycero-3-phosphoserine + ethanolamine; CC Xref=Rhea:RHEA:41500, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, CC ChEBI:CHEBI:78268, ChEBI:CHEBI:78269; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41501; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- CC glycero-3-phosphoethanolamine + L-serine = 1-octadecanoyl-2- CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine + CC ethanolamine; Xref=Rhea:RHEA:41492, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78265, ChEBI:CHEBI:78266; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41493; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-octadecenyl)-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)- CC sn-glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2- CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-L-serine CC + ethanolamine; Xref=Rhea:RHEA:41496, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78263, ChEBI:CHEBI:78264; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41497; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoethanolamine + L-serine = 1-octadecanoyl-2-(9Z-octadecenoyl)- CC sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:40795, CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:75038, CC ChEBI:CHEBI:78260; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40796; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-octadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-(9Z- CC octadecenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine; CC Xref=Rhea:RHEA:41600, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, CC ChEBI:CHEBI:78340, ChEBI:CHEBI:78341; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41601; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-octadecenyl)-2-(5Z,8Z,11Z,14Z- eicosatetraenoyl)-sn- CC glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2- CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CC ethanolamine; Xref=Rhea:RHEA:41604, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78342, ChEBI:CHEBI:78343; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41605; CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CC -!- ACTIVITY REGULATION: Requires calcium ions (PubMed:19014349). Inhibited CC by exogenous phosphatidylserine (PubMed:19014349). CC {ECO:0000269|PubMed:19014349}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=120 uM for serine (in the presence of 1 mM PE) CC {ECO:0000269|PubMed:19014349}; CC Vmax=0.57 mmol/h/mg enzyme {ECO:0000269|PubMed:19014349}; CC pH dependence: CC Optimum pH is around 7.5. {ECO:0000269|PubMed:19014349}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein CC {ECO:0000255}. Note=Highly enriched in the mitochondria-associated CC membrane (MAM). {ECO:0000250|UniProtKB:Q9Z1X2}. CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL834357; CAD39022.1; -; mRNA. DR EMBL; AC137894; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138230; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001210; AAH01210.1; -; mRNA. DR CCDS; CCDS7696.1; -. DR RefSeq; NP_110410.1; NM_030783.2. DR AlphaFoldDB; Q9BVG9; -. DR BioGRID; 123499; 144. DR IntAct; Q9BVG9; 8. DR MINT; Q9BVG9; -. DR STRING; 9606.ENSP00000308258; -. DR DrugBank; DB00144; Phosphatidyl serine. DR SwissLipids; SLP:000001061; -. DR GlyConnect; 1602; 1 N-Linked glycan (1 site). DR GlyCosmos; Q9BVG9; 1 site, 1 glycan. DR GlyGen; Q9BVG9; 1 site, 1 N-linked glycan (1 site). DR iPTMnet; Q9BVG9; -. DR PhosphoSitePlus; Q9BVG9; -. DR SwissPalm; Q9BVG9; -. DR BioMuta; PTDSS2; -. DR DMDM; 49036457; -. DR EPD; Q9BVG9; -. DR jPOST; Q9BVG9; -. DR MassIVE; Q9BVG9; -. DR MaxQB; Q9BVG9; -. DR PaxDb; 9606-ENSP00000308258; -. DR PeptideAtlas; Q9BVG9; -. DR ProteomicsDB; 79205; -. DR Pumba; Q9BVG9; -. DR Antibodypedia; 41975; 120 antibodies from 16 providers. DR DNASU; 81490; -. DR Ensembl; ENST00000308020.6; ENSP00000308258.5; ENSG00000174915.12. DR GeneID; 81490; -. DR KEGG; hsa:81490; -. DR MANE-Select; ENST00000308020.6; ENSP00000308258.5; NM_030783.3; NP_110410.1. DR UCSC; uc001lpj.3; human. DR AGR; HGNC:15463; -. DR CTD; 81490; -. DR GeneCards; PTDSS2; -. DR HGNC; HGNC:15463; PTDSS2. DR HPA; ENSG00000174915; Low tissue specificity. DR MIM; 612793; gene. DR neXtProt; NX_Q9BVG9; -. DR OpenTargets; ENSG00000174915; -. DR PharmGKB; PA33940; -. DR VEuPathDB; HostDB:ENSG00000174915; -. DR eggNOG; KOG2735; Eukaryota. DR GeneTree; ENSGT00530000063576; -. DR HOGENOM; CLU_037661_4_1_1; -. DR InParanoid; Q9BVG9; -. DR OMA; QHVLPNF; -. DR OrthoDB; 3933684at2759; -. DR PhylomeDB; Q9BVG9; -. DR TreeFam; TF300012; -. DR BioCyc; MetaCyc:HS10846-MONOMER; -. DR BRENDA; 2.7.8.29; 2681. DR PathwayCommons; Q9BVG9; -. DR Reactome; R-HSA-1483101; Synthesis of PS. DR SignaLink; Q9BVG9; -. DR UniPathway; UPA00948; -. DR BioGRID-ORCS; 81490; 12 hits in 1159 CRISPR screens. DR GenomeRNAi; 81490; -. DR Pharos; Q9BVG9; Tbio. DR PRO; PR:Q9BVG9; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9BVG9; Protein. DR Bgee; ENSG00000174915; Expressed in left testis and 97 other cell types or tissues. DR ExpressionAtlas; Q9BVG9; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:Ensembl. 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:SF7; PHOSPHATIDYLSERINE SYNTHASE 2; 1. DR Pfam; PF03034; PSS; 1. DR Genevisible; Q9BVG9; HS. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism; KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; KW Phosphoprotein; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..487 FT /note="Phosphatidylserine synthase 2" FT /id="PRO_0000056832" FT TOPO_DOM 1..62 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 63..83 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 84..96 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 97..117 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 118..126 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 127..147 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 148..313 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 314..334 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 335 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 336..356 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 357..376 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 377..397 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 398..403 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 404..424 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 425..487 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 451..487 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 485 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" SQ SEQUENCE 487 AA; 56253 MW; E02508F894841A4F CRC64; MRRGERRDAG GPRPESPVPA GRASLEEPPD GPSAGQATGP GEGRRSTESE VYDDGTNTFF WRAHTLTVLF ILTCTLGYVT LLEETPQDTA YNTKRGIVAS ILVFLCFGVT QAKDGPFSRP HPAYWRFWLC VSVVYELFLI FILFQTVQDG RQFLKYVDPK LGVPLPERDY GGNCLIYDPD NETDPFHNIW DKLDGFVPAH FLGWYLKTLM IRDWWMCMII SVMFEFLEYS LEHQLPNFSE CWWDHWIMDV LVCNGLGIYC GMKTLEWLSL KTYKWQGLWN IPTYKGKMKR IAFQFTPYSW VRFEWKPASS LRRWLAVCGI ILVFLLAELN TFYLKFVLWM PPEHYLVLLR LVFFVNVGGV AMREIYDFMD DPKPHKKLGP QAWLVAAITA TELLIVVKYD PHTLTLSLPF YISQCWTLGS VLALTWTVWR FFLRDITLRY KETRWQKWQN KDDQGSTVGN GDQHPLGLDE DLLGPGVAEG EGAPTPN //