Reviewed, UniProtKB/Swiss-Prot P23642 (VAN1_YEAST)

Names and origin

Protein names

Recommended name:
    Mannan polymerase I complex VAN1 subunit
      Short name=M-pol I subunit VAN1
Alternative name(s):
    Vanadate resistance protein

Gene names

Name:	VAN1
Synonyms:	VRG7
Ordered Locus Names:	YML115C
ORF Names:	YM8339.04C

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

General annotation (Comments)

Function	Involved in regulation of the phosphorylation of a number of proteins, some of which appear to be important in cell growth control. The M-Pol I complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.
Subunit structure	Component of the M-Pol I complex which contains MNN9 and VAN1.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Note= Cis-Golgi. Recycles between endoplasmic reticulum and Golgi.
Post-translational modification	Glycosylated.
Miscellaneous	Present with 4750 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ANP1/MMN9/VAN1 family.

Ontologies

Keywords
Biological process	Growth regulation Sporulation
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall mannoprotein biosynthetic process Ref.5 Traceable author statement. Source: UniProtKB protein amino acid N-linked glycosylation Ref.5 Inferred from direct assay. Source: SGD
Cellular component	alpha-1,6-mannosyltransferase complex Ref.4 Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	alpha-1,6-mannosyltransferase activity Ref.5 Ref.7 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MNN9	P39107	1	EBI-20237,EBI-11082

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 535	535	Mannan polymerase I complex VAN1 subunit
Regions
	Topological domain	1 – 64	64	Cytoplasmic Potential
	Transmembrane	65 – 81	17	Signal-anchor for type II membrane protein
	Topological domain	82 – 535	454	Lumenal Potential
Amino acid modifications
	Modified residue	25	1	Phosphoserine
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Glycosylation	251	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	361	1	D → A: Reduced activity of the M-Pol I complex
	Sequence conflict	87	1	M → L in AAA35204. Ref.1
	Sequence conflict	140	1	Q → L in AAA35204. Ref.1
	Sequence conflict	281	1	D → E in AAA35204. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23642-1 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: 92767D0E4C3ECCED	FASTA	535	61,092
	10 20 30 40 50 60 MGMFFNLRSN IKKKAMDNGL SLPISRNGSS NNIKDKRSEH NSNSLKGKYR YQPRSTPSKF 70 80 90 100 110 120 QLTVSITSLI IIAVLSLYLF ISFLSGMGIG VSTQNGRSLL GSSKSSENYK TIDLEDEEYY 130 140 150 160 170 180 DYDFEDIDPE VISKFDDGVQ HYLISQFGSE VLTPKDDEKY QRELNMLFDS TVEEYDLSNF 190 200 210 220 230 240 EGAPNGLETR DHILLCIPLR NAADVLPLMF KHLMNLTYPH ELIDLAFLVS DCSEGDTTLD 250 260 270 280 290 300 ALIAYSRHLQ NGTLSQIFQE IDAVIDSQTK GTDKLYLKYM DEGYINRVHQ AFSPPFHENY 310 320 330 340 350 360 DKPFRSVQIF QKDFGQVIGQ GFSDRHAVKV QGIRRKLMGR ARNWLTANAL KPYHSWVYWR 370 380 390 400 410 420 DADVELCPGS VIQDLMSKNY DVIVPNVWRP LPTFLGTEQP YDLNSWMESQ EALALAKTLD 430 440 450 460 470 480 EDDVIVEGYA EYPTWRVHLA YIRDAEGDPN EAVDLDGVGG VSILAKAKIF RNGVQFPAFT 490 500 510 520 530 FENHAETEAF GKMAKKMGYR VGGLPHYTIW HIYEPSDDDL KEIASREREK RRQSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Vanadate-resistant mutants of Saccharomyces cerevisiae show alterations in protein phosphorylation and growth control." Kanik-Ennulat C., Neff N. Mol. Cell. Biol. 10:898-909(1990) [PubMed: 2137555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Kanik-Ennulat C., Neff N. Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Novel membrane protein complexes for protein glycosylation in the yeast Golgi apparatus." Hashimoto H., Yoda K. Biochem. Biophys. Res. Commun. 241:682-686(1997) [PubMed: 9434768] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[5]	"Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity." Jungmann J., Munro S. EMBO J. 17:423-434(1998) [PubMed: 9430634] [Abstract] Cited for: ACTIVITY OF M-POL I COMPLEX, GLYCOSYLATION, SUBUNIT, SUBCELLULAR LOCATION.
[6]	"Active recycling of yeast Golgi mannosyltransferase complexes through the endoplasmic reticulum." Todorow Z., Spang A., Carmack E., Yates J., Schekman R. Proc. Natl. Acad. Sci. U.S.A. 97:13643-13648(2000) [PubMed: 11095735] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"The components of the Saccharomyces cerevisiae mannosyltransferase complex M-Pol I have distinct functions in mannan synthesis." Stolz J., Munro S. J. Biol. Chem. 277:44801-44808(2002) [PubMed: 12235155] [Abstract] Cited for: COMPOSITION OF THE M-POL I COMPLEX, MUTAGENESIS OF ASP-361.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M33957 Genomic DNA. Translation: AAA35204.1. Z49210 Genomic DNA. Translation: CAA89103.1.
PIR	S53957.
RefSeq	NP_013592.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:886N.
IntAct	P23642.
Proteomic databases
PeptideAtlas	P23642.
Genome annotation databases
Ensembl	YML115C. Saccharomyces cerevisiae. [Contig view]
GeneID	854925.
GenomeReviews	Gene locus YML115C in contig Z71257_GR.
KEGG	sce:YML115C.
NMPDR	fig|4932.3.peg.4628.
Organism-specific databases
CYGD	YML115c.
SGD	S000004583. VAN1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P23642.
Gene expression databases
GermOnline	YML115C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005109. Anp1. [Graphical view]
Pfam	PF03452. Anp1. 1 hit. [Graphical view]
ProDom	P23642. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P23642.
ProtoNet	Search...

Entry information

Entry name

VAN1_YEAST

Accession

Primary (citable) accession number: P23642

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	October 1, 1996
Last modified:	September 2, 2008
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)