PTSS2_CHICK
ID PTSS2_CHICK Reviewed; 442 AA.
AC E1BYA3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=PTDSS1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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}.
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; AADN02040056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BYA3; -.
DR STRING; 9031.ENSGALP00000006841; -.
DR PaxDb; E1BYA3; -.
DR VEuPathDB; HostDB:geneid_422997; -.
DR eggNOG; KOG2735; Eukaryota.
DR PhylomeDB; E1BYA3; -.
DR TreeFam; TF300012; -.
DR UniPathway; UPA00948; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..442
FT /note="Phosphatidylserine synthase 2"
FT /id="PRO_0000416035"
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..442
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 442 AA; 52146 MW; 9BD2CF6439A2ED94 CRC64;
MRRGERRGPA GPLGDGPALG LRRSTESEVY DDGTNTFFWR AHTLTVLFIL TCALGYVTLL
EETPQDTAYN TKRGIVASIL VFLCFGVTQA KDGPFSRPHP AYWRFWLCVS VVYELFLIFI
LFQTVQDGRQ FMKYIDPHLG VPLPERDYGG NCLIYDPGNE SDPFHNIWDK LDGFVPAHFF
GWYLKTLMIR DWWMCMIISV MFEFLEYSLE HQLPNFSECW WDHWIMDVIL CNGLGIYCGM
KTLSWLSLKT YKWQGLWNIP TYKGKMKRIV FQFTPYSWVK FEWKPASSLR RWLAVCGIIF
VFLLAELNTF YLKFVLWMPP EHYLVLLRLV FFVNVGGVAM REIYDFMDDP KFHKKLGQQA
WLVAAITATE FLIVVKYDPY TLTLSLPFYI TQCWILGIIL VLTWTAWRFF IRDITLRYKE
IRRQKQEHKY EKDKCLSNGD GH
