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Reviewed, UniProtKB/Swiss-Prot P53037 (PSD2_YEAST)

Last modified November 3, 2009. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidylserine decarboxylase proenzyme 2
    EC=4.1.1.65
Cleaved into the following 2 chains:
    1- Recommended name:
            Phosphatidylserine decarboxylase 2 beta chain
    2- Recommended name:
            Phosphatidylserine decarboxylase 2 alpha chain
Gene names
Name: PSD2
Ordered Locus Names: YGR170W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1138 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May be involved in the regulation of phospholipid biosynthesis and interorganelle trafficking of phosphatidylserine.

Catalytic activity

Phosphatidyl-L-serine = phosphatidylethanolamine + CO2.

Cofactor

Pyruvoyl group.

Pathway

Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.

Subcellular location

Golgi apparatusGolgi stack. Vacuole.

Sequence similarities

Belongs to the phosphatidylserine decarboxylase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentGolgi apparatus
Vacuole
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   PTMPhosphoprotein
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphosphatidylcholine biosynthetic process

Inferred from direct assay. Source: SGD

   Cellular componentGolgi membrane

Traceable author statement. Source: SGD

Golgi stack

Inferred from electronic annotation. Source: UniProtKB-SubCell

fungal-type vacuole membrane

Traceable author statement. Source: SGD

   Molecular functionphosphatidylserine decarboxylase activity

Traceable author statement. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11381138Phosphatidylserine decarboxylase proenzyme 2
PRO_0000045200
Chain1 – 10421042Phosphatidylserine decarboxylase 2 beta chain By similarity
PRO_0000045201
Chain1043 – 113896Phosphatidylserine decarboxylase 2 alpha chain By similarity
PRO_0000045202

Regions

Compositional bias152 – 1598Poly-Ser
Compositional bias271 – 2744Poly-Ser
Compositional bias591 – 5944Poly-Gln
Compositional bias1045 – 10495Poly-Ile

Sites

Site1042 – 10432Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue10431Pyruvic acid (Ser) By similarity
Modified residue11081Phosphoserine Ref.4

Experimental info

Sequence conflict8011E → G in AAA69819. Ref.1
Sequence conflict9741Y → N in AAA69819. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P53037-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 934BA6579E121053

FASTA1,138130,065
        10         20         30         40         50         60 
MRIIKGRKRG KNKKPTLILK IHVIQAENIE ALKTFNCNPV CFVTTNTFYS QKTNKLKNSN 

        70         80         90        100        110        120 
THWNQTLRIK LPRNPTSEWL RIIVYDALPT GAPPTTPSRP RTTTANTSSS TLSNSGLSSH 

       130        140        150        160        170        180 
SHSSRNLNVT SKGNQTSTSI NSVSSSATPA PSHSSSSLST TGPGSTHKNR INSYLYLGEA 

       190        200        210        220        230        240 
KISLLDLFKR KDTTTSYKFS IEAQRYHLYD MKGGKDQDSL NCNFLVGDIL LGFKLECNVK 

       250        260        270        280        290        300 
RTPTFQAFNA WRNELNTYLG RIDRNKARMR SSSSLPPPLE DMLSNSSAVS GNEIRREKPY 

       310        320        330        340        350        360 
SDTDLAHDEE VNAEDEIDAE ESIEDMNSSG SICTERRYDI DNDTIFDSIS EVVSLNDEEL 

       370        380        390        400        410        420 
DILNDFEEAD HPNVPDINVH DIDEDTRISL SSMITALDEY DIVEPEDVAK LPAVSENDIT 

       430        440        450        460        470        480 
SVDDEESENQ QESDEEFDIY NEDEREDSDF QSKEYIGSRL LHLQRGKHNK SYANYLYRRA 

       490        500        510        520        530        540 
KSNFFISKKE HAMGVVFMHI GAIKNLPALR NRLSKTNYEM DPFIVISFGR RVFKTSWRKH 

       550        560        570        580        590        600 
TLNPEFNEYA AFEVFPHETN FAFSIKVVDK DSFSFNDDVA KCELAWFDML QQQQHENEWI 

       610        620        630        640        650        660 
PYEIPLDLTV EPAHAPKQPV LYSSFKYVSY PFLKKSFWKE AVDTSVNLER LDIIQVMLYL 

       670        680        690        700        710        720 
ERLGSFTMAD SFELFQHFNK SAWAGQSITR SQLVEGLQSW RKSTNFKRIW TCPRCMRSCK 

       730        740        750        760        770        780 
PTRNARRSKL VLENDLITHF AICTFSKEHK TLKPSYVSSA FASKRWFSKV LIKLTYGKYA 

       790        800        810        820        830        840 
LGSNNANILV QDRDTGIIIE EKISAHVKLG MRIIYNGKSP ESKKFRSLLK TLSIRQGKKF 

       850        860        870        880        890        900 
DSTASAKQIE PFIKFHSLDL SQCRDKDFKT FNEFFYRKLK PGSRLPESNN KEILFSPADS 

       910        920        930        940        950        960 
RCTVFPTIQE SKEIWVKGRK FSIKKLANNY NPETFNDNNC SIGIFRLAPQ DYHRFHSPCN 

       970        980        990       1000       1010       1020 
GTIGKPVYVD GEYYTVNPMA VRSELDVFGE NIRVIIPIDS PQFGKLLYIP IGAMMVGSIL 

      1030       1040       1050       1060       1070       1080 
LTCKENDVVE SGQELGYFKF GGSTIIIIIP HNNFMFDSDL VKNSSERIET LVKVGMSIGH 

      1090       1100       1110       1120       1130 
TSNVNELKRI RIKVDDPKKI ERIKRTISVS DENAKSTGNV TWEYHTLREM MNKDFAGL 

« Hide

References

« Hide 'large scale' references
[1]"Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele."
Trotter P.J., Pedretti J., Yates R., Voelker D.R.
J. Biol. Chem. 270:6071-6080(1995) [PubMed: 7890740] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PTY36.
[2]"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
Yeast 13:1077-1090(1997) [PubMed: 9290212] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1108, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U19910 Genomic DNA. Translation: AAA69819.1.
Z72955 Genomic DNA. Translation: CAA97196.1.
PIRS64484.
RefSeqNP_011686.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6756N.
IntActP53037. 9 interactions.
STRINGP53037.

Proteomic databases

PRIDEP53037.

Genome annotation databases

EnsemblYGR170W; YGR170W; YGR170W; Saccharomyces cerevisiae. [Genome view]
GeneID853080.
GenomeReviewsGene locus YGR170W in contig Y13135_GR.
KEGGsce:YGR170W.
NMPDRfig|4932.3.peg.2812.

Organism-specific databases

CYGDYGR170w.
SGDS000003402. PSD2.

Phylogenomic databases

HOGENOMP53037.
OMAMRIIYNG.

Enzyme and pathway databases

BRENDA4.1.1.65. 250.

Gene expression databases

ArrayExpressP53037.
GenevestigatorP53037.
GermOnlineYGR170W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR003817. PS_Dcarbxylase.
IPR005221. PS_decarb.
[Graphical view]
PANTHERPTHR10067. PS_decarb. 1 hit.
PfamPF00168. C2. 2 hits.
PF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
SMARTSM00239. C2. 2 hits.
[Graphical view]
TIGRFAMsTIGR00163. PS_decarb. 1 hit.
ProtoNetSearch...

Other Resources

NextBio973047.

Entry information

Entry namePSD2_YEAST
AccessionPrimary (citable) accession number: P53037
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 3, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents