Reviewed, UniProtKB/Swiss-Prot Q6C8M8 (ATG26_YARLI)

Names and origin

Protein names

Recommended name:
    Sterol 3-beta-glucosyltransferase
    EC=2.4.1.173
Alternative name(s):
    Autophagy-related protein 26

Gene names

Name:	ATG26
Ordered Locus Names:	YALI0D18403g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	1456 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside By similarity. Ref.2
Catalytic activity	UDP-glucose + a sterol = UDP + a sterol 3-beta-D-glucoside.
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 28 family. Contains 3 GRAM domains. Contains 1 PH domain.

Ontologies

Keywords
Biological process	Autophagy Lipid synthesis Protein transport Steroid biosynthesis Sterol biosynthesis Transport
Cellular component	Cytoplasm Membrane
Domain	Repeat
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lipid glycosylation Inferred from electronic annotation. Source: InterPro protein transport Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	sterol 3-beta-glucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1456	1456	Sterol 3-beta-glucosyltransferase		PRO_0000215615
Regions
	Domain	200 – 247	48	GRAM 1
	Domain	251 – 351	101	PH
	Domain	827 – 893	67	GRAM 2
	Compositional bias	438 – 466	29	His-rich
	Compositional bias	582 – 697	116	Gly-rich
	Compositional bias	724 – 734	11	Poly-Ala

Sequences

	Sequence		Length	Mass (Da)
	Q6C8M8-1 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: 6C585F5A9266FDA5	FASTA	1,456	159,607
	10 20 30 40 50 60 MLSASQFLKH RVSCLPMLNK VESDSTDGDP DDACQHPHDC NIFSVLVNGA TDRLEGFFDE 70 80 90 100 110 120 SDEEDGDEVE TPSTTTTAVS PSATMSAPSP TATAPTPHSG THTPKSPLHS ISHCPSFNSV 130 140 150 160 170 180 AQALPHSLSP HSLCHTSSHE ASRRGSAEQP SRTQSELARR IKTENILNSF HDSLEAAYEK 190 200 210 220 230 240 CHGGANPEEH QSNKTEYFQQ KLKGFAALDV DEQLIADYPV WLLKNVLIQG HLYITAKHMC 250 260 270 280 290 300 FLSYLPRRQN ANIRSGTLVK ARKRSLREGT RYWCVLKNDS FSYYPDSTDV YFPAGTIDLS 310 320 330 340 350 360 EALAAELCDD EGDVTEPESF RIVMPKKSVL FKADSHSAAH EWVKALQKEI FRAHNQGDTV 370 380 390 400 410 420 RIVIPLQNIV DLEKTKIFEF ATTIKTSVVE SNETYAIDEY IFTFFKFGDD VLRTLTENGV 430 440 450 460 470 480 EISGGNFSPR QSQLAVGHKH VTESVRDSTL LHASGHHHHF FHSAHHESDG KSNSKSHTSS 490 500 510 520 530 540 RSHTPRNLTP QVTGEQPHER DEKRDSKLPR LPKFLRRFKD KVDDKCDDKP TLVPSFLKSR 550 560 570 580 590 600 ASSRRNSAEG SDRPNLASQR TSSSTLFPSA PPTPGSQPTT PGVHAPGSST PGGSYGTTTP 610 620 630 640 650 660 GTPASADSVS LAGTPGVAAP VGDIEGLNGN PMPAGIAAEL KEKRKSGGAT SSGAATGATT 670 680 690 700 710 720 PGGAAAPGST GNSSPGTPGG LGGPGAVGAG GPGVMGGAES APAGTVPQQS HHAGISVVAP 730 740 750 760 770 780 HDPAAAAAAA DAAAPFTRGP GSGIPEIQDD SDSSDDDHWG HIGTAEVDED PEQDTFKKKN 790 800 810 820 830 840 KRFSTLSKVS DLWSGSTKHY GKHHTERLGD DDDKHLASAE EITESNERFQ KRFALGTEER 850 860 870 880 890 900 LIASYHCHLH RGGIPTYGKM YVSTNYVTFR SFLRTKTLMI VPLKVVENAT KDSGFKFGYS 910 920 930 940 950 960 GLVLTIQGYE EIFFEFASAS HRDDAEVMLL RQLDIIRPHI NDDIKSDDQY MLQSARLCTY 970 980 990 1000 1010 1020 EDALKAEANV EMPPVIIDGN LASVLPGLVT PQSKMLFTLL TIGSRGDVQP YISLGKALIE 1030 1040 1050 1060 1070 1080 EGHRVRIATH SEFKDWIEGY GIEFKEVAGD PSELMKIMVD HGVFSVSFLR DAASKFRGWI 1090 1100 1110 1120 1130 1140 NELLASSWEA CQGSDVLIES PSAMAGIHIA EALQIPYFRA FTMPWSRTRA YPHAFIVPDQ 1150 1160 1170 1180 1190 1200 KMGGSYNYLT YVMFDNVFWK GISGQVNRWR KKTLHLPRTN LDHMEQNKVP FLYNVSPAVL 1210 1220 1230 1240 1250 1260 PPPVDFPDWI KITGYWFLDE GSKDYTPDDK LCRFMEKARN DGKKLVYIGF GSIVVSDPTA 1270 1280 1290 1300 1310 1320 LTKSVVESVL KADVRCILNK GWSDRLGKKD AKEPEIPLPE EVLQITNCPH DWLFPQIDAC 1330 1340 1350 1360 1370 1380 VHHGGSGTTG AGLRAGLPTI IKPFFGDQFF YANRVEDLGA GIHLRKLNVS QFSKALWEAT 1390 1400 1410 1420 1430 1440 HNERIIAKAA AVGRQIRSEN GVISAIQAIY RDLDYARSLV QKKRGYTPTS DKEEETWTLV 1450 DDIERQMQDE VEKHNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.
[2]	"Sterol glucosyltransferases have different functional roles in Pichia pastoris and Yarrowia lipolytica." Stasyk O.V., Nazarko T.Y., Stasyk O.G., Krasovska O.S., Warnecke D.C., Nicaud J.-M., Cregg J.M., Sibirny A.A. Cell Biol. Int. 27:947-952(2003) [PubMed: 14585290] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382130 Genomic DNA. Translation: CAG81176.2.
RefSeq	XP_502984.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2911115.
GenomeReviews	Gene locus YALI0D18403g in contig CR382130_GR.
KEGG	yli:YALI0D18403g.
Phylogenomic databases
OrthoDB	EOG9908S8.
Enzyme and pathway databases
BRENDA	2.4.1.173. 3602.
Family and domain databases
InterPro	IPR004276. Glyco_trans_28. IPR004182. GRAM. IPR011993. PH_type. IPR001849. Pleckstrin_homology. IPR002213. UDP_glucos_trans. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
PANTHER	PTHR11926. UDP_glucos_trans. 1 hit.
Pfam	PF03033. Glyco_transf_28. 1 hit. PF02893. GRAM. 2 hits. PF00169. PH. 1 hit. PF00201. UDPGT. 1 hit. [Graphical view]
SMART	SM00568. GRAM. 2 hits. SM00233. PH. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATG26_YARLI

Accession

Primary (citable) accession number: Q6C8M8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	February 10, 2009
Last modified:	January 19, 2010
This is version 45 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)