PSS1_ARATH
ID PSS1_ARATH Reviewed; 425 AA.
AC F4HXY7; Q9XI59;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase 1;
DE EC=2.7.8.8;
DE AltName: Full=Phosphatidylserine synthase 1;
GN Name=PSS1; OrderedLocusNames=At1g15110; ORFNames=F9L1.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21554450; DOI=10.1111/j.1365-313x.2011.04624.x;
RA Yamaoka Y., Yu Y., Mizoi J., Fujiki Y., Saito K., Nishijima M., Lee Y.,
RA Nishida I.;
RT "PHOSPHATIDYLSERINE SYNTHASE1 is required for microspore development in
RT Arabidopsis thaliana.";
RL Plant J. 67:648-661(2011).
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. Is essential for phosphatidylserine (PS)
CC biosynthesis and PE seems to be the most plausible substrate. Plays an
CC important role in microspore maturation. {ECO:0000269|PubMed:21554450}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC Evidence={ECO:0000269|PubMed:21554450};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 1/2.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21554450}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21554450}. Nucleus envelope
CC {ECO:0000269|PubMed:21554450}. Note=Mainly localized in nuclei and ER
CC membranes during pollen development.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4HXY7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in trichomes, leaf veins and root
CC vasculature. {ECO:0000269|PubMed:21554450}.
CC -!- DEVELOPMENTAL STAGE: Expressed in anthers and microspores at floral
CC stages 9 to 12, tapetum at floral stages 7 to 11, mature embryos at 5
CC days after flowering and dry seed embryos.
CC -!- DISRUPTION PHENOTYPE: Mostly embryonic lethality with low frequencies
CC of dwarf infertile plants. {ECO:0000269|PubMed:21554450}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39639.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007591; AAD39639.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29265.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60487.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60488.1; -; Genomic_DNA.
DR EMBL; BX813560; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; G86284; G86284.
DR RefSeq; NP_001322771.1; NM_001332150.1. [F4HXY7-1]
DR RefSeq; NP_001322772.1; NM_001332149.1. [F4HXY7-1]
DR RefSeq; NP_172963.3; NM_101379.5. [F4HXY7-1]
DR AlphaFoldDB; F4HXY7; -.
DR BioGRID; 23314; 3.
DR STRING; 3702.AT1G15110.2; -.
DR PaxDb; F4HXY7; -.
DR PRIDE; F4HXY7; -.
DR ProteomicsDB; 248815; -. [F4HXY7-1]
DR EnsemblPlants; AT1G15110.1; AT1G15110.1; AT1G15110. [F4HXY7-1]
DR EnsemblPlants; AT1G15110.3; AT1G15110.3; AT1G15110. [F4HXY7-1]
DR EnsemblPlants; AT1G15110.4; AT1G15110.4; AT1G15110. [F4HXY7-1]
DR GeneID; 838074; -.
DR Gramene; AT1G15110.1; AT1G15110.1; AT1G15110. [F4HXY7-1]
DR Gramene; AT1G15110.3; AT1G15110.3; AT1G15110. [F4HXY7-1]
DR Gramene; AT1G15110.4; AT1G15110.4; AT1G15110. [F4HXY7-1]
DR KEGG; ath:AT1G15110; -.
DR Araport; AT1G15110; -.
DR eggNOG; KOG2735; Eukaryota.
DR HOGENOM; CLU_037661_1_1_1; -.
DR OMA; FIKHIFA; -.
DR BRENDA; 2.7.8.8; 399.
DR UniPathway; UPA00558; UER00615.
DR PRO; PR:F4HXY7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HXY7; baseline and differential.
DR Genevisible; F4HXY7; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IEA:InterPro.
DR GO; GO:0009556; P:microsporogenesis; IMP:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleus; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..425
FT /note="CDP-diacylglycerol--serine O-phosphatidyltransferase
FT 1"
FT /id="PRO_0000429526"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 281
FT /note="H -> N (in Ref. 3; BX813560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 49518 MW; D115455EE19654FD CRC64;
MEPNGYRKER RKEQHLGRMN GGGGDVETDL DPWTAWAYKP RTISLLLIGA CFLIWASGAL
DPDSTTSDDL VTSVKRGVWA MIAVFLAYSL LQAPSTVLIR PHPAIWRLVH GMAVIYLVAL
TFLLFQRRDD ARQFMKFLHP DLGIELPEKS YGADCRIYVP DHPTNRFKNL YDTVFDEFFL
AHIFGWWGKA ILIRNQPLLW VLSIGFELLE VTFRHMLPNF NECWWDSIVL DILICNWFGI
WAGMYTVRYF DGKTYEWVGI SRQPNIIGKV KRTLGQFTPA HWDKDEWHPL QGPWRFIQVL
TLCIIFLTVE LNTFFLKFSL WIPPRNPVIL YRLILWWLIA IPTTREYNSY LQDRKPVKKV
GAFCWLSLGI CIVELLICIK FGSGLYPTEM PLWVVTLWGS VGLGLVAFLL SWTWKIQKIL
AQKRR
