Reviewed, UniProtKB/Swiss-Prot Q9Y751 (ATG26_PICPG)

Names and origin

Protein names

Recommended name:
    Sterol 3-beta-glucosyltransferase
    EC=2.4.1.173
Alternative name(s):
    Autophagy-related protein 26
    UDP-glycosyltransferase 51
    Pexophagy zeocin-resistant mutant protein 4
    Peroxisome degradation protein 3

Gene names

Name:	ATG26
Synonyms:	PAZ4, PDG3, UGT51, UGT51B1
ORF Names:	PAS_chr4_0167

Organism

Pichia pastoris (strain GS115) (Yeast)

Taxonomic identifier

644223 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

Protein attributes

Sequence length	1211 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in the biosynthesis of sterol glucoside. Involved in the invagination of peroxisomes into the vacuole for their degradation in both glucose-induced micropexophagy and ethanol-induced macropexophagy. Ref.1 Ref.3 Ref.4 Ref.5
Catalytic activity	UDP-glucose + a sterol = UDP + a sterol 3-beta-D-glucoside.
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Note: Found in perivacuolar punctate structures and micropexophagic apparatus (MIPA). Ref.5
Domain	The first GRAM domain is required for association with the micropexophagic apparatus.
Sequence similarities	Belongs to the glycosyltransferase 28 family. Contains 2 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
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 – 1211	1211	Sterol 3-beta-glucosyltransferase		PRO_0000215614
Regions
	Domain	196 – 235	40	GRAM 1
	Domain	248 – 347	100	PH
	Domain	586 – 652	67	GRAM 2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y751-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7C3CF0FC7A7C3822	FASTA	1,211	136,364
	10 20 30 40 50 60 MSQLRPRDSS AGKSSSPRRT DRNPESIDVN SKGGSEGMTS GLVPGTAPHK EDETEAEDDI 70 80 90 100 110 120 DCGRLITSKS LATMLTTASM YAGVSQLDDD AIESSALDEP IPYVPYEEDA ESVMSESTVG 130 140 150 160 170 180 VDTVRDTDSS EQINPEIDGL VALRKKQQHT LSKFELSVVR KRCSQLSLAG SSSGSTRRNS 190 200 210 220 230 240 FTLDNNETTR AVKLCEKLKT TFDLSDDDEF VNDYPCWLLH EVFLQGHIYI TSRYLLYFAF 250 260 270 280 290 300 LPKRDSTVTM SGALSIRSST TMRFSVRRWA VLKGNYFRLY ANSTERYFPS LNIDLRFLLK 310 320 330 340 350 360 VELSNPNLEE NKPTVFKLIT EARTHYFQAD SLDNARSWVT DLRKHIFTAK NSGGHVTIKV 370 380 390 400 410 420 PLENILDLSI ETLFEASQTL KLKVLESEES YAIDDYYFMF FNNGDQVLDS IRQSMKALGI 430 440 450 460 470 480 ELTDSDSSES DSDVSGSETN GRSTHRKSKL SRSLSVLTPI PRGIGSIYKP IKSSASGIIG 490 500 510 520 530 540 AIKKPQKSAT RPFSSVVETV VPNDNDSELK QDHAGDAPKD SEEPSTKPSN WSAKSLVQGF 550 560 570 580 590 600 LSTTSSISQS MLFASPMHYN NQLFIERGEE DPYFVTNKEE REVAQSRFRK HFSLPDSEEL 610 620 630 640 650 660 LASYFCHFQK NIPVYGKVYL GTTCICYRSL FPGTNTTMIL PYSDIENVYN LKGFRFGYSG 670 680 690 700 710 720 LVIVIRAHEE LFFEFGSNES RDDCDLFLLK QLDFTKSHKN AHSEQKRKRN DSIKLAESVQ 730 740 750 760 770 780 LADARLRYFE TRIESDIGRE VPIILEENQY STSEIRSKRR YKFVLLTIGS RGDVQPYISL 790 800 810 820 830 840 AKGLLAENHK VKIVTHEEFK PWVESYGIEF ATIAGNPAEL MSLMVTHKSL SVGFLKEAKE 850 860 870 880 890 900 KFTGWIGELL QSSWDACQDA DVLIESPSAM AGIHIAEKLQ IPYFRAFTMP WTRTRAYPHA 910 920 930 940 950 960 FVVPEQKRGG SYNYLTHIIF ENVFWKGISG EVNKWREQVL MLPKTNLERL EQNKVPFLYN 970 980 990 1000 1010 1020 VSPTVFPPSM DFPHWVKVVG YWFLDEGEAD SYDPPKPLLE FMEKAKTDGK KLVYIGFGSI 1030 1040 1050 1060 1070 1080 VVSDPKQLTE AVIDAVLSAD VRCILNKGWS DRLGKQTGVE VELPEEIYNS GNVPHDWLFG 1090 1100 1110 1120 1130 1140 KIDASVHHGG SGTTGATLRA GIPTIIKPFF GDQFFYANRV EDIGVGIGLR KLNSKSLSKA 1150 1160 1170 1180 1190 1200 IKEVTTNTRI IEKAKEIGKQ IQSENGVSAA IRCLYQEMEY AKKLSKSKQK YWDNQSEDIS 1210 DDSVSGSWFE V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional expression of UGT genes encoding sterol glucosyltransferases from Saccharomyces cerevisiae, Candida albicans, Pichia pastoris, and Dictyostelium discoideum." Warnecke D.C., Erdmann R., Fahl A., Hube B., Mueller F., Zank T., Zaehringer U., Heinz E. J. Biol. Chem. 274:13048-13059(1999) [PubMed: 10224056] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Genome sequence of the recombinant protein production host Pichia pastoris." De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S., Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N. Nat. Biotechnol. 27:561-566(2009) [PubMed: 19465926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of peroxisomes during micropexophagy." Mukaiyama H., Oku M., Baba M., Samizo T., Hammond A.T., Glick B.S., Kato N., Sakai Y. Genes Cells 7:75-90(2002) [PubMed: 11856375] [Abstract] Cited for: FUNCTION.
[4]	"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.
[5]	"Peroxisome degradation requires catalytically active sterol glucosyltransferase with a GRAM domain." Oku M., Warnecke D.C., Noda T., Mueller F., Heinz E., Mukaiyama H., Kato N., Sakai Y. EMBO J. 22:3231-3241(2003) [PubMed: 12839986] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF091397 Genomic DNA. Translation: AAD29570.1. FN392322 Genomic DNA. Translation: CAY71393.1.
RefSeq	XP_002493572.1.
3D structure databases
HSSP	HSSP built from PDB template 1IIR based on UniProtKB P96559.
ModBase	Search...
Protein family/group databases
CAZy	GT1. Glycosyltransferase Family 1.
Genome annotation databases
GeneID	8201077.
Enzyme and pathway databases
BRENDA	2.4.1.173. 390.
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_PICPG

Accession

Primary (citable) accession number: Q9Y751
Secondary accession number(s): C4R718

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	November 1, 1999
Last modified:	October 13, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)