Reviewed, UniProtKB/Swiss-Prot P38179 (ALG3_YEAST)

Names and origin

Protein names

Recommended name:
    Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
    EC=2.4.1.130
Alternative name(s):
    Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
    Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase
    Asparagine-linked glycosylation protein 3
    HM-1 killer toxin resistance protein

Gene names

Name:	ALG3
Synonyms:	RHK1
Ordered Locus Names:	YBL082C
ORF Names:	YBL0720

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-PP-Dol. Sensitive to H.mrakii HM-1 killer toxin. Ref.4
Catalytic activity	Transfers an alpha-D-mannosyl residue from dolichyl-phosphate D-mannose into membrane lipid-linked oligosaccharide.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.
Sequence similarities	Belongs to the glycosyltransferase 58 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oligosaccharide-lipid intermediate assembly Ref.5 Inferred from direct assay. Source: SGD
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-1,3-mannosyltransferase activity Inferred from direct assay. Source: SGD dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase 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 – 458	458	Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase		PRO_0000080565
Regions
	Topological domain	1 – 41	41	Lumenal Potential
	Transmembrane	42 – 62	21	Potential
	Topological domain	63 – 95	33	Cytoplasmic Potential
	Transmembrane	96 – 116	21	Potential
	Topological domain	117 – 137	21	Lumenal Potential
	Transmembrane	138 – 158	21	Potential
	Topological domain	159 – 171	13	Cytoplasmic Potential
	Transmembrane	172 – 192	21	Potential
	Topological domain	193 – 216	24	Lumenal Potential
	Transmembrane	217 – 237	21	Potential
	Topological domain	238 – 242	5	Cytoplasmic Potential
	Transmembrane	243 – 263	21	Potential
	Topological domain	264 – 302	39	Lumenal Potential
	Transmembrane	303 – 323	21	Potential
	Topological domain	324 – 345	22	Cytoplasmic Potential
	Transmembrane	346 – 366	21	Potential
	Topological domain	367 – 381	15	Lumenal Potential
	Transmembrane	382 – 402	21	Potential
	Topological domain	403 – 415	13	Cytoplasmic Potential
	Transmembrane	416 – 436	21	Potential
	Topological domain	437 – 458	22	Lumenal Potential
Experimental info
	Mutagenesis	275	1	A → V in ALG3-1; leads to an underglycosylation of secretory proteins.
	Sequence conflict	86	1	G → R in AAA75352. Ref.3
	Sequence conflict	187 – 198	12	LGAIV…RCHQR → FRGYRGQQVPSA in AAA75352. Ref.3
	Sequence conflict	266	1	S → Q in AAA75352. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P38179-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 1C2FEAD6D459C249	FASTA	458	52,861
	10 20 30 40 50 60 MEGEQSPQGE KSLQRKQFVR PPLDLWQDLK DGVRYVIFDC RANLIVMPLL ILFESMLCKI 70 80 90 100 110 120 IIKKVAYTEI DYKAYMEQIE MIQLDGMLDY SQVSGGTGPL VYPAGHVLIY KMMYWLTEGM 130 140 150 160 170 180 DHVERGQVFF RYLYLLTLAL QMACYYLLHL PPWCVVLACL SKRLHSIYVL RLFNDCFTTL 190 200 210 220 230 240 FMVVTVLGAI VASRCHQRPK LKKSLALVIS ATYSMAVSIK MNALLYFPAM MISLFILNDA 250 260 270 280 290 300 NVILTLLDLV AMIAWQVAVA VPFLRSFPQQ YLHCAFNFGR KFMYQWSINW QMMDEEAFND 310 320 330 340 350 360 KRFHLALLIS HLIALTTLFV TRYPRILPDL WSSLCHPLRK NAVLNANPAK TIPFVLIASN 370 380 390 400 410 420 FIGVLFSRSL HYQFLSWYHW TLPILIFWSG MPFFVGPIWY VLHEWCWNSY PPNSQASTLL 430 440 450 LALNTVLLLL LALTQLSGSV ALAKSHLRTT SSMEKKLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Sequence of a segment of yeast chromosome II shows two novel genes, one almost entirely hydrophobic and the other extremely asparagine-serine rich." Cusick M.E. Yeast 10:1251-1256(1994) [PubMed: 7754714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-406.
[4]	"A novel yeast gene, RHK1, is involved in the synthesis of the cell wall receptor for the HM-1 killer toxin that inhibits beta-1,3-glucan synthesis." Kimura T., Kitamoto N., Kito Y., Iimura Y., Shirai T., Komiyama T., Furuichi Y., Sakka K., Ohmiya K. Mol. Gen. Genet. 254:139-147(1997) [PubMed: 9108275] [Abstract] Cited for: FUNCTION.
[5]	"Cloning and characterization of the ALG3 gene of Saccharomyces cerevisiae." Aebi M., Gassenhuber J., Domdey H., Te Heesen S. Glycobiology 6:439-444(1996) [PubMed: 8842708] [Abstract] Cited for: CHARACTERIZATION, VARIANT ALG3-1.
[6]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X79489 Genomic DNA. Translation: CAA56024.1. Z35844 Genomic DNA. Translation: CAA84904.1. M89908 Genomic DNA. Translation: AAA75352.1.
PIR	S45424.
RefSeq	NP_009471.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4854N.
IntAct	P38179. 1 interaction.
Protein family/group databases
CAZy	GT58. Glycosyltransferase Family 58.
Proteomic databases
PeptideAtlas	P38179.
Genome annotation databases
Ensembl	YBL082C. Saccharomyces cerevisiae. [Contig view]
GeneID	852196.
GenomeReviews	Gene locus YBL082C in contig Y13134_GR.
KEGG	sce:YBL082C.
NMPDR	fig|4932.3.peg.157.
Organism-specific databases
CYGD	YBL082c.
SGD	S000000178. ALG3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38179.
OMA	P38179. LRLFNDC.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-7188.
BRENDA	2.4.1.130. 250.
Gene expression databases
ArrayExpress	P38179.
GermOnline	YBL082C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007873. Glycosyltransferase_ALG3. [Graphical view]
PANTHER	PTHR12646. ALG3. 1 hit.
Pfam	PF05208. ALG3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	970682.

Entry information

Entry name

ALG3_YEAST

Accession

Primary (citable) accession number: P38179

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)