Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ceramide glucosyltransferase

Gene

PAS_chr3_0357

Organism
Komagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final step in the biosynthesis of the membrane lipid glucosylceramide (GluCer), the transfer of glucose to ceramide. Glucosylceramides play important roles in growth, differentiation and pathogenicity.1 Publication

Catalytic activityi

UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.1 Publication

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei321 – 3211Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00222.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceramide glucosyltransferaseBy similarity (EC:2.4.1.801 Publication)
Alternative name(s):
GLCT-1
Glucosylceramide synthase1 Publication
Short name:
GCS
UDP-glucose ceramide glucosyltransferase1 Publication
UDP-glucose:N-acylsphingosine D-glucosyltransferase
Gene namesi
Ordered Locus Names:PAS_chr3_0357
OrganismiKomagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Taxonomic identifieri644223 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeKomagataella
ProteomesiUP000000314 Componenti: Chromosome 3

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4242LumenalCuratedAdd
BLAST
Transmembranei43 – 6321HelicalSequence analysisAdd
BLAST
Topological domaini64 – 384321CytoplasmicBy similarityAdd
BLAST
Transmembranei385 – 40521HelicalSequence analysisAdd
BLAST
Topological domaini406 – 4083LumenalCurated
Transmembranei409 – 42921HelicalSequence analysisAdd
BLAST
Topological domaini430 – 46637CytoplasmicCuratedAdd
BLAST
Transmembranei467 – 48721HelicalSequence analysisAdd
BLAST
Topological domaini488 – 50922LumenalCuratedAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Results in complete loss of glucosylceramides (GluCers) in mutant cells (PubMed:11443131). Shows increased resistance to plant defensins MsDef1 and RsAFP2, and to heliomicin, a defensin-like peptide from the insect Heliothis virescens (PubMed:14604982, PubMed:19028992).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509Ceramide glucosyltransferasePRO_5002942221Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi644223.XP_002492578.1.

Structurei

3D structure databases

ProteinModelPortaliC4R4B3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi123 – 1231D1Curated
Motifi179 – 1791D2Curated
Motifi321 – 3211D3Curated
Motifi361 – 3655(Q/R)XXRWCurated

Domaini

The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS active site, involved in catalysis and UDP-sugar binding.By similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1215.
HOGENOMiHOG000246631.
InParanoidiC4R4B3.
KOiK00720.
OrthoDBiEOG7SXWCQ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 3 hits.

Sequencei

Sequence statusi: Complete.

C4R4B3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIMQLGLTSL AFLALKCDAY NIAPKIDTPN VEPFAPSGGL KLLAIVAIIW
60 70 80 90 100
YVVVLLVAYY GFFEIMQKFS KRKTLPVPPQ VEGVTILRPI KGIDPEMELC
110 120 130 140 150
LQSAFDQDYP KFEIIICVES ENDPGIGVAE ALIRKYPHVD ARILKGDSHN
160 170 180 190 200
PDHFGPNPKV NNLAKGYSAG KYDIMWILDS NVWVCSGALS RSVDALNRSL
210 220 230 240 250
DNGRSTFDFQ TGKGRKVNLV HHVPMAISIN PQTGTNLDEM FLFTSHSKFY
260 270 280 290 300
ISINKAALAP CVNGKSNLYR RSELDLAVKR LGKGSEPSLD GTTGILAKDA
310 320 330 340 350
AYYGSKPGQG LRFFARYIGE DNMIATALWF QNGGRTGLTG DAAIQPLGGV
360 370 380 390 400
NSTSLKNYLL RRIRWLRVRK HMVLEATLLE PTTECLLCGT FGTFAISTLF
410 420 430 440 450
LQSYFNWKFF IFHLLVWMVT DYTQFHILLT NASQDTATCN VPYFAEPNFN
460 470 480 490 500
AYGSPFESSN LRTFHRWVLY WLLREVLALP IWISAMLGTR IIWRNRPFRI

NVDLSAEEL
Length:509
Mass (Da):57,164
Last modified:July 7, 2009 - v1
Checksum:i08F80CB3F1B77821
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF364403 Genomic DNA. Translation: AAK73020.1.
FN392321 Genomic DNA. Translation: CAY70399.1.
RefSeqiXP_002492578.1. XM_002492533.1.

Genome annotation databases

EnsemblFungiiCAY70399; CAY70399; PAS_chr3_0357.
GeneIDi8199490.
KEGGippa:PAS_chr3_0357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF364403 Genomic DNA. Translation: AAK73020.1.
FN392321 Genomic DNA. Translation: CAY70399.1.
RefSeqiXP_002492578.1. XM_002492533.1.

3D structure databases

ProteinModelPortaliC4R4B3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi644223.XP_002492578.1.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAY70399; CAY70399; PAS_chr3_0357.
GeneIDi8199490.
KEGGippa:PAS_chr3_0357.

Phylogenomic databases

eggNOGiCOG1215.
HOGENOMiHOG000246631.
InParanoidiC4R4B3.
KOiK00720.
OrthoDBiEOG7SXWCQ.

Enzyme and pathway databases

UniPathwayiUPA00222.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glucosylceramide synthases, a gene family responsible for the biosynthesis of glucosphingolipids in animals, plants, and fungi."
    Leipelt M., Warnecke D., Zahringer U., Ott C., Muller F., Hube B., Heinz E.
    J. Biol. Chem. 276:33621-33629(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE.
    Strain: GS115 / ATCC 20864.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GS115 / ATCC 20864.
  3. Cited for: DISRUPTION PHENOTYPE.
  4. "Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum."
    Ramamoorthy V., Cahoon E.B., Thokala M., Kaur J., Li J., Shah D.M.
    Eukaryot. Cell 8:217-229(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCEGT_PICPG
AccessioniPrimary (citable) accession number: C4R4B3
Secondary accession number(s): Q96V37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 9, 2015
Last sequence update: July 7, 2009
Last modified: January 20, 2016
This is version 42 of the entry and version 1 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. 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.