VAN1_YEAST
ID VAN1_YEAST Reviewed; 535 AA.
AC P23642; D6W0G9;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Mannan polymerase I complex VAN1 subunit;
DE Short=M-pol I subunit VAN1;
DE AltName: Full=Vanadate resistance protein;
GN Name=VAN1; Synonyms=VRG7; OrderedLocusNames=YML115C; ORFNames=YM8339.04C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2137555; DOI=10.1128/mcb.10.3.898-909.1990;
RA Kanik-Ennulat C., Neff N.;
RT "Vanadate-resistant mutants of Saccharomyces cerevisiae show alterations in
RT protein phosphorylation and growth control.";
RL Mol. Cell. Biol. 10:898-909(1990).
RN [2]
RP SEQUENCE REVISION.
RA Kanik-Ennulat C., Neff N.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9434768; DOI=10.1006/bbrc.1997.7888;
RA Hashimoto H., Yoda K.;
RT "Novel membrane protein complexes for protein glycosylation in the yeast
RT Golgi apparatus.";
RL Biochem. Biophys. Res. Commun. 241:682-686(1997).
RN [6]
RP ACTIVITY OF M-POL I COMPLEX, GLYCOSYLATION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9430634; DOI=10.1093/emboj/17.2.423;
RA Jungmann J., Munro S.;
RT "Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with
RT alpha-1,6-mannosyltransferase activity.";
RL EMBO J. 17:423-434(1998).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11095735; DOI=10.1073/pnas.250472397;
RA Todorow Z., Spang A., Carmack E., Yates J., Schekman R.;
RT "Active recycling of yeast Golgi mannosyltransferase complexes through the
RT endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13643-13648(2000).
RN [8]
RP COMPOSITION OF THE M-POL I COMPLEX, AND MUTAGENESIS OF ASP-361.
RX PubMed=12235155; DOI=10.1074/jbc.m208023200;
RA Stolz J., Munro S.;
RT "The components of the Saccharomyces cerevisiae mannosyltransferase complex
RT M-Pol I have distinct functions in mannan synthesis.";
RL J. Biol. Chem. 277:44801-44808(2002).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in regulation of the phosphorylation of a number of
CC proteins, some of which appear to be important in cell growth control.
CC -!- FUNCTION: The M-Pol I complex possesses alpha-1,6-mannosyltransferase
CC activity and is probably involved in the elongation of the mannan
CC backbone of N-linked glycans on cell wall and periplasmic proteins.
CC -!- SUBUNIT: Component of the M-Pol I complex which contains MNN9 and VAN1.
CC {ECO:0000269|PubMed:9430634, ECO:0000269|PubMed:9434768}.
CC -!- INTERACTION:
CC P23642; P39107: MNN9; NbExp=4; IntAct=EBI-20237, EBI-11082;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11095735}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9434768}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:9434768}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9434768}. Note=Cis-Golgi (PubMed:9430634). Recycles
CC between endoplasmic reticulum and Golgi (PubMed:11095735).
CC {ECO:0000269|PubMed:11095735, ECO:0000269|PubMed:9430634}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9430634}.
CC -!- MISCELLANEOUS: Present with 4750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family. {ECO:0000305}.
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DR EMBL; M33957; AAA35204.1; -; Genomic_DNA.
DR EMBL; Z49210; CAA89103.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09783.1; -; Genomic_DNA.
DR PIR; S53957; S53957.
DR RefSeq; NP_013592.1; NM_001182477.1.
DR AlphaFoldDB; P23642; -.
DR SMR; P23642; -.
DR BioGRID; 35089; 298.
DR ComplexPortal; CPX-1672; alpha-1,6-mannosyltransferase complex, M-Pol I variant.
DR DIP; DIP-886N; -.
DR IntAct; P23642; 19.
DR STRING; 4932.YML115C; -.
DR CAZy; GT62; Glycosyltransferase Family 62.
DR iPTMnet; P23642; -.
DR MaxQB; P23642; -.
DR PaxDb; P23642; -.
DR PRIDE; P23642; -.
DR EnsemblFungi; YML115C_mRNA; YML115C; YML115C.
DR GeneID; 854925; -.
DR KEGG; sce:YML115C; -.
DR SGD; S000004583; VAN1.
DR VEuPathDB; FungiDB:YML115C; -.
DR eggNOG; ENOG502QRNF; Eukaryota.
DR GeneTree; ENSGT00940000176370; -.
DR HOGENOM; CLU_017872_1_1_1; -.
DR InParanoid; P23642; -.
DR OMA; AEYPTWR; -.
DR BioCyc; MetaCyc:YML115C-MON; -.
DR BioCyc; YEAST:YML115C-MON; -.
DR PRO; PR:P23642; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P23642; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000136; C:mannan polymerase complex; IDA:UniProtKB.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR GO; GO:0097502; P:mannosylation; IDA:ComplexPortal.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:SGD.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 2.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Growth regulation;
KW Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Sporulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..535
FT /note="Mannan polymerase I complex VAN1 subunit"
FT /id="PRO_0000193672"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..81
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 82..535
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 22..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 361
FT /note="D->A: Reduced activity of the M-Pol I complex."
FT /evidence="ECO:0000269|PubMed:12235155"
FT CONFLICT 87
FT /note="M -> L (in Ref. 1; AAA35204)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Q -> L (in Ref. 1; AAA35204)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="D -> E (in Ref. 1; AAA35204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61092 MW; 92767D0E4C3ECCED CRC64;
MGMFFNLRSN IKKKAMDNGL SLPISRNGSS NNIKDKRSEH NSNSLKGKYR YQPRSTPSKF
QLTVSITSLI IIAVLSLYLF ISFLSGMGIG VSTQNGRSLL GSSKSSENYK TIDLEDEEYY
DYDFEDIDPE VISKFDDGVQ HYLISQFGSE VLTPKDDEKY QRELNMLFDS TVEEYDLSNF
EGAPNGLETR DHILLCIPLR NAADVLPLMF KHLMNLTYPH ELIDLAFLVS DCSEGDTTLD
ALIAYSRHLQ NGTLSQIFQE IDAVIDSQTK GTDKLYLKYM DEGYINRVHQ AFSPPFHENY
DKPFRSVQIF QKDFGQVIGQ GFSDRHAVKV QGIRRKLMGR ARNWLTANAL KPYHSWVYWR
DADVELCPGS VIQDLMSKNY DVIVPNVWRP LPTFLGTEQP YDLNSWMESQ EALALAKTLD
EDDVIVEGYA EYPTWRVHLA YIRDAEGDPN EAVDLDGVGG VSILAKAKIF RNGVQFPAFT
FENHAETEAF GKMAKKMGYR VGGLPHYTIW HIYEPSDDDL KEIASREREK RRQSE
