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Protein

Dehydrodolichyl diphosphate syntase complex subunit SPAC4D7.04c

Gene

SPAC4D7.04c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

With nus1, forms the dehydrodolichyl diphosphate syntase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).1 Publication

Catalytic activityi

(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiR-SPO-446199. Synthesis of Dolichyl-phosphate.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrodolichyl diphosphate syntase complex subunit SPAC4D7.04cCurated (EC:2.5.1.871 Publication)
Alternative name(s):
Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)Curated
Gene namesi
ORF Names:SPAC4D7.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4D7.04c.
PomBaseiSPAC4D7.04c.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Dehydrodolichyl diphosphate syntase complex subunit SPAC4D7.04cPRO_0000123761Add
BLAST

Proteomic databases

MaxQBiO14171.

Interactioni

Subunit structurei

Forms an active dehydrodolichyl diphosphate syntase complex with nus1.1 Publication

Protein-protein interaction databases

BioGridi280034. 1 interaction.
MINTiMINT-4671094.

Structurei

3D structure databases

ProteinModelPortaliO14171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Phylogenomic databases

HOGENOMiHOG000006053.
InParanoidiO14171.
KOiK11778.
OMAiLMELCTH.
OrthoDBiEOG73BVQX.
PhylomeDBiO14171.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNLSGWFIH CPPLQWTLDQ LETMMINTIK RGKVPQHIAF VMDGNRRWAR
60 70 80 90 100
QRRMETIEGH SSGFEALKSL LKVCLKLGVK EVSAFTFSIE NFKRSKYEVD
110 120 130 140 150
MLMEIAKNSL TQITAHGDLV DQYGIRIRIV GDLSRLQPDV LETALKAVEI
160 170 180 190 200
TKHNTKATLN VCFPYTSRHE IATSVQSIVK MAEDGTITPE DIDEDIFEKN
210 220 230 240 250
LLIKDSLPLD LLIRTSGVER LSDFMLWQCH KNTEIKFIDF YWPDFSIWKF
260
FPMLIQYQLQ NQPA
Length:264
Mass (Da):30,543
Last modified:May 30, 2000 - v2
Checksum:i7DCC6094B114D29D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11276.1.
PIRiT38795.
RefSeqiNP_594957.1. NM_001020388.2.

Genome annotation databases

EnsemblFungiiSPAC4D7.04c.1; SPAC4D7.04c.1:pep; SPAC4D7.04c.
GeneIDi2543620.
KEGGispo:SPAC4D7.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11276.1.
PIRiT38795.
RefSeqiNP_594957.1. NM_001020388.2.

3D structure databases

ProteinModelPortaliO14171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280034. 1 interaction.
MINTiMINT-4671094.

Proteomic databases

MaxQBiO14171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4D7.04c.1; SPAC4D7.04c.1:pep; SPAC4D7.04c.
GeneIDi2543620.
KEGGispo:SPAC4D7.04c.

Organism-specific databases

EuPathDBiFungiDB:SPAC4D7.04c.
PomBaseiSPAC4D7.04c.

Phylogenomic databases

HOGENOMiHOG000006053.
InParanoidiO14171.
KOiK11778.
OMAiLMELCTH.
OrthoDBiEOG73BVQX.
PhylomeDBiO14171.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-SPO-446199. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

NextBioi20804626.
PROiO14171.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation."
    Park E.J., Grabinska K.A., Guan Z., Stranecky V., Hartmannova H., Hodanova K., Baresova V., Sovova J., Jozsef L., Ondruskova N., Hansikova H., Honzik T., Zeman J., Hulkova H., Wen R., Kmoch S., Sessa W.C.
    Cell Metab. 20:448-457(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiYE54_SCHPO
AccessioniPrimary (citable) accession number: O14171
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: November 11, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.