Reviewed, UniProtKB/Swiss-Prot A2QNQ5 (ATG26_ASPNC)

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
ORF Names:	An07g06610

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	1371 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.
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 2 GRAM domains. Contains 1 PH domain.
Sequence caution	The sequence CAK39507.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAK39507.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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 – 1371	1371	Sterol 3-beta-glucosyltransferase		PRO_0000318041
Regions
	Domain	241 – 301	61	GRAM 1
	Domain	292 – 391	100	PH
	Domain	717 – 783	67	GRAM 2

Sequences

	Sequence		Length	Mass (Da)
	A2QNQ5-1 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 1E8C4CF3CEFA773F	FASTA	1,371	153,536
	10 20 30 40 50 60 MRPFIDDAKR RVDRRLSASR QSISNSRMFA SVLPERLRND NDDDDDSQVD FSAPPGGMGP 70 80 90 100 110 120 REGHMQYMHQ SIFGMIAAVG SRSGFHARYD ESSDSDGEDE SRARKDAENL SATAGALPKR 130 140 150 160 170 180 SGNESPRLSP KPQSPTPERG RRHRRTISDH KLLRPFKLNS KQNKGQEPAV QSEPQTGDEM 190 200 210 220 230 240 SRASTPKRPR SVTPRAAPVL SRMVEARALL DTEDSTKGAP STTEEIRDEG PTQKSASALS 250 260 270 280 290 300 LRLKEMFGFE APEKVLVEYA CSFLQSMLLQ GYMYVTEGHV CFYAYLPRKS TVAIKSGYVY 310 320 330 340 350 360 KRGRKNPKYN RYWFSLKGDV LSYYADPSKL YFPSGHVDLR YGISASLAEP KDKGREVKDF 370 380 390 400 410 420 QVTTDQRTYY FRADSSSSAK EWVKALQKVI FRTHNDKGSV KISFPIENII DIEESPMVDF 430 440 450 460 470 480 AETFKIRVVE SEETYAIDEY YFTSFNYGQD AFNFLKGLVA DTPMKRSQQT LSPQPEQTSR 490 500 510 520 530 540 SRRTRGSQNR WSITSATSQS RGIGKSGNRR RSASTGQFSF GHDALSMSPP MRQQDSSLSF 550 560 570 580 590 600 GNSFEQATEA SGILQSMTDT TESASQILNR SDVFQSPTIR TMRRGPSGAE KTVRRHSDET 610 620 630 640 650 660 ARSVHTTRNG PEIQYAVSES DRDTQTPSGL HPSTPALNEL VRAGVYPLQR AAGFAEYLKT 670 680 690 700 710 720 RSKQMSNLLA SESMGYLEKV SGMWAGGGKH YGESENILPD DQAVDPEDLE AGCKDGDRFR 730 740 750 760 770 780 EHFALPPSEK LQASYFAWLH RMIPLYGKIY ISQKKLCFRS LMPGTRTKMI LPLKDVENVD 790 800 810 820 830 840 KEKGFNFGRH GLVVVIRGHE ELFFEFGTAD TRDDCAVTLH KGLESTKFLM ASGLLAECEE 850 860 870 880 890 900 KDESESATAE HRLLQEARLD ITGMHSSRSA MAASNELHPI FDDPRASIIN FKPTESLRIT 910 920 930 940 950 960 CLTIGSRGDV QPYIALCKGL LAEGHRPKIA THAEFEPWVR KHGIDFALVD GDPAELMRIC 970 980 990 1000 1010 1020 VENGMFTYSF FKEATAKFRG WIDDLLSSAW KACQDTDLLI ESPSAMAGIH IAEALRIPYF 1030 1040 1050 1060 1070 1080 RAFTMPWSRT RAYPHAFAVP EHKMGGAYNY ITYVMFDNVF WKSVAGQVNR WRKKELGLKA 1090 1100 1110 1120 1130 1140 TGLDKMQPNK VPFLYNYSPT VVPPPLDYPD WIRITGYWFL SEGSDWTPPA ELVDFIQRAR 1150 1160 1170 1180 1190 1200 KDEKKVVYIG FGSIVVSDPS ALTRTVIESV QKADVRCILS KGWSDRLGDP ASAKSEVPLP 1210 1220 1230 1240 1250 1260 PEIYQIQSAP HDWLFSHIDA AAHHGGAGTT GASLRAGVPT IVKPFFGDQF FFGTRVEDLG 1270 1280 1290 1300 1310 1320 VGICLKKLNV TMFSRALWEA THDERMIVKA HKLGAQIRSE DGVDTAIQAI YRDLEYAKTL 1330 1340 1350 1360 1370 AQARSNVSST PFSPTPSAKT VAEQEADEDV PEEEWTIVED DTELEMRPTV A

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed: 17259976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270135 Genomic DNA. Translation: CAK39507.1. Sequence problems.
RefSeq	XP_001391739.1.
3D structure databases
SMR	A2QNQ5. Positions 294-390.
ModBase	Search...
Genome annotation databases
GeneID	4981929.
KEGG	ang:An07g06610.
Phylogenomic databases
HOGENOM	HBG332791.
OrthoDB	EOG9908S8.
Enzyme and pathway databases
BRENDA	2.4.1.173. 277.
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. [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_ASPNC

Accession

Primary (citable) accession number: A2QNQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	February 9, 2010
This is version 26 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)