Q5B0M8 (ALG10_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
EC=2.4.1.256

Alternative name(s):
Alpha-1,2-glucosyltransferase alg10
Alpha-2-glucosyltransferase alg10
Asparagine-linked glycosylation protein 10
Dolichyl-phosphoglucose-dependent glucosyltransferase alg10

Gene names

Name:	alg10
ORF Names:	AN5902

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc2Man9GlcNAc(2)-PP-Dol.
Catalytic activity	Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ALG10 glucosyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	transferase activity, transferring hexosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 608	608	Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase		PRO_0000215455
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Transmembrane	64 – 84	21	Helical; Potential
	Transmembrane	143 – 163	21	Helical; Potential
	Transmembrane	183 – 203	21	Helical; Potential
	Transmembrane	271 – 291	21	Helical; Potential
	Transmembrane	312 – 332	21	Helical; Potential
	Transmembrane	359 – 379	21	Helical; Potential
	Transmembrane	407 – 427	21	Helical; Potential
	Transmembrane	507 – 527	21	Helical; Potential
	Transmembrane	569 – 589	21	Helical; Potential
Amino acid modifications
	Glycosylation	292	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5B0M8 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: BB8DDD03839B08CE	FASTA	608	68,448
	10 20 30 40 50 60 MNAQPRSALA LAARYAVPFG LLLIPIWMTQ VNSVVPEPYL DEAFHIPQAQ AYWSHQWTQW 70 80 90 100 110 120 DPKITTPPGL YLFSYAVCAL ILLLRGSPEH LDPPALRATN AAAAAVLLPL RLQTALDTVR 130 140 150 160 170 180 KQRNTRPSGA WLSHTVLNIC LFPPLFFFSG LYYTDVLALL VVIEAYNWDL SRGRPNAVKL 190 200 210 220 230 240 ETAVFLVLGV LALLFRQTNI FWVSVFFGGL QVVRRLRRVT KNCESTNVAD ILAAGSRNEL 250 260 270 280 290 300 YDPLVLDASL VDYVKTAASL CSVALNNLGS VITSLVPYLI ILATFGGFVL WNGSVVMGHK 310 320 330 340 350 360 EFHTASLHIA QMLYIWPYFV FFSWPLLLVP MANIVLPKFM LPKFLNQGFP ASRRRLPSLL 370 380 390 400 410 420 TVLIILPIML AVVHFNTIVH PFTLADNRHY VFYVFRILLN SHPYTRYVAT LVYFLGAWMI 430 440 450 460 470 480 ISAMGYSPVT AAPGLASVVR TQAPPASATS AEERTEKTQK LERKQKGFKK SAQVASSAPA 490 500 510 520 530 540 PIDPKVLADL QEHIRRRQRL EHETSRVSFV LVWLAATALS LISAPLVEPR YLIIPWVMWR 550 560 570 580 590 600 LHLPPSPTPV IYRRASDEKD LEARIAVNFP LFLETVWFLL VNVITGTLFL RGGFEWPQEP GKVQRFLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACD01000101 Genomic DNA. Translation: EAA57765.1. BN001301 Genomic DNA. Translation: CBF70603.1.
RefSeq	XP_663506.1. XM_658414.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5B0M8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00007131; CADANIAP00007131; CADANIAG00007131.
GeneID	2870820.
KEGG	ani:AN5902.2.
Phylogenomic databases
OMA	QEPGKVQ.
OrthoDB	EOG47WRXP.
PhylomeDB	Q5B0M8.
Family and domain databases
InterPro	IPR007006. Glycosyltransferase_ALG10. [Graphical view]
KO	K03850.
PANTHER	PTHR12989. DIE2_ALG10. 1 hit.
Pfam	PF04922. DIE2_ALG10. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG10_EMENI

Accession

Primary (citable) accession number: Q5B0M8
Secondary accession number(s): C8UZU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program