位置:首页 > 蛋白库 > PTSS2_HUMAN
PTSS2_HUMAN
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   03-AUG-2022, entry version 151.
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; 127.
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   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; Q9BVG9; -.
DR   PeptideAtlas; Q9BVG9; -.
DR   PRIDE; Q9BVG9; -.
DR   ProteomicsDB; 79205; -.
DR   Antibodypedia; 41975; 103 antibodies from 15 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   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; MKYIDPN; -.
DR   OrthoDB; 818196at2759; -.
DR   PhylomeDB; Q9BVG9; -.
DR   TreeFam; TF300012; -.
DR   BioCyc; MetaCyc:HS10846-MON; -.
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 1083 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 95 other tissues.
DR   ExpressionAtlas; Q9BVG9; baseline and differential.
DR   Genevisible; Q9BVG9; 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; 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   Pfam; PF03034; PSS; 1.
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024