Mannan polymerase I complex VAN1 subunit - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P23642 (VAN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
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. Ref.5 Ref.6
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. Ref.5 Ref.6 Ref.7
Post-translational modification	Glycosylated. Ref.6
Miscellaneous	Present with 4750 molecules/cell in log phase SD medium. Ref.9
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 Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell wall mannoprotein biosynthetic process Traceable author statement Ref.6. Source: UniProtKB protein N-linked glycosylation Inferred from mutant phenotype Ref.6. Source: SGD regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell alpha-1,6-mannosyltransferase complex Inferred from direct assay Ref.5. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-1,6-mannosyltransferase activity Inferred from direct assay Ref.6. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MNN9	P39107	5	EBI-20237,EBI-11082

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 535

535

Mannan polymerase I complex VAN1 subunit

PRO_0000193672

Regions

Topological domain

1 – 64

Cytoplasmic Potential

Transmembrane

65 – 81

Helical; Signal-anchor for type II membrane protein

Topological domain

82 – 535

454

Lumenal Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.10

Glycosylation

215

N-linked (GlcNAc...) Potential

Glycosylation

251

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

361

D → A: Reduced activity of the M-Pol I complex. Ref.8

Sequence conflict

M → L in AAA35204. Ref.1

Sequence conflict

140

Q → L in AAA35204. Ref.1

Sequence conflict

281

D → E in AAA35204. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P23642 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 92767D0E4C3ECCED
Show »

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

« Hide

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. 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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].
[10]	"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
EMBL GenBank DDBJ	M33957 Genomic DNA. Translation: AAA35204.1. Z49210 Genomic DNA. Translation: CAA89103.1. BK006946 Genomic DNA. Translation: DAA09783.1.
PIR	S53957.
RefSeq	NP_013592.1. NM_001182477.1.
3D structure databases
ProteinModelPortal	P23642.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-886N.
IntAct	P23642. 4 interactions.
MINT	MINT-522083.
STRING	P23642.
Protein family/group databases
CAZy	GT62. Glycosyltransferase Family 62.
Proteomic databases
PeptideAtlas	P23642.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML115C; YML115C; YML115C.
GeneID	854925.
KEGG	sce:YML115C.
NMPDR	fig\|4932.3.peg.4628.
Organism-specific databases
CYGD	YML115c.
SGD	S000004583. VAN1.
Phylogenomic databases
eggNOG	fuNOG07910.
GeneTree	EFGT00050000002721.
HOGENOM	HBG323986.
OMA	FSDRHAV.
OrthoDB	EOG4HB1V3.
Gene expression databases
ArrayExpress	P23642.
Genevestigator	P23642.
GermOnline	YML115C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005109. Anp1. [Graphical view]
KO	K05530.
Pfam	PF03452. Anp1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977944.

Entry information

Entry name

VAN1_YEAST

Accession

Primary (citable) accession number: P23642
Secondary accession number(s): D6W0G9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents