PTSS2_RAT
ID PTSS2_RAT Reviewed; 471 AA.
AC B2GV22;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Phosphatidylserine synthase 2;
DE Short=PSS-2;
DE Short=PtdSer synthase 2;
DE EC=2.7.8.29 {ECO:0000250|UniProtKB:Q9Z1X2};
DE AltName: Full=Serine-exchange enzyme II;
GN Name=Ptdss2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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-12 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Catalyzes the conversion of
CC phosphatatidylethanolamine and does not act on phosphatidylcholine (By
CC similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen
CC and diacyl PE as substrate and the latter is six times better utilized,
CC indicating the importance of an ester linkage at the sn-1 position (By
CC similarity). Although it shows no sn-1 fatty acyl preference, exhibits
CC significant preference towards docosahexaenoic acid (22:6n-3) compared
CC with 18:1 or 20:4 at the sn-2 position (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z1X2}.
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:0000250|UniProtKB:Q9Z1X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
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 -!- 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}.
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DR EMBL; AC118351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473953; EDM11981.1; -; Genomic_DNA.
DR EMBL; BC166496; AAI66496.1; -; mRNA.
DR RefSeq; NP_001099786.1; NM_001106316.1.
DR AlphaFoldDB; B2GV22; -.
DR SMR; B2GV22; -.
DR STRING; 10116.ENSRNOP00000021925; -.
DR GlyGen; B2GV22; 1 site.
DR iPTMnet; B2GV22; -.
DR PhosphoSitePlus; B2GV22; -.
DR PaxDb; B2GV22; -.
DR PeptideAtlas; B2GV22; -.
DR PRIDE; B2GV22; -.
DR Ensembl; ENSRNOT00000021925; ENSRNOP00000021925; ENSRNOG00000015912.
DR GeneID; 293620; -.
DR KEGG; rno:293620; -.
DR UCSC; RGD:1307914; rat.
DR CTD; 81490; -.
DR RGD; 1307914; Ptdss2.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR HOGENOM; CLU_037661_4_1_1; -.
DR InParanoid; B2GV22; -.
DR OMA; MKYIDPN; -.
DR OrthoDB; 818196at2759; -.
DR PhylomeDB; B2GV22; -.
DR TreeFam; TF300012; -.
DR Reactome; R-RNO-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR PRO; PR:B2GV22; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000015912; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; B2GV22; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; ISO:RGD.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; ISO:RGD.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; ISO:RGD.
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..471
FT /note="Phosphatidylserine synthase 2"
FT /id="PRO_0000416034"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..74
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..291
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..471
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1X2"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 471 AA; 54722 MW; 0C196AB61180DB87 CRC64;
MRRGERRVAG GSGSESPLLE GRRSTESEVY DDGTNTFFWR AHTLTVLFIL TCALGYVTLL
EETPQDTAYN TKRGIVASIL VFLCFGVTQA KDGPFSRPHP AYWRFWLCVS VVYELFLIFI
LFQTVHDGRQ FLKYVDPRLG VPLPERDYGG NCLIYDADNK TDPFHNIWDK LDGFVPAHFI
GWYLKTLMIR DWWMCMIISV MFEFLEYSLE HQLPNFSECW WDHWIMDVLL CNGLGIYCGM
KTLEWLSLKT YKWQGLWNIP TYKGKMKRIA FQFTPYSWVR FEWKPASSLH RWLAVCGIIL
VFLLAELNTF YLKFVLWMPP EHYLVLLRLV FFVNVGGVAM REIYDFMDEL KPHRKLGQQA
WLVAAITVTE LLIVVKYDPH TLTLSLPFYI SQCWTLGSIL VLTWTVWRFF LRDITMRYKE
TRRQKQQSHQ AINNGDGHPG PEDDLPGTGT AEEEGTTNDG VPAEEGPSAA S
