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Vesicle-associated membrane protein-associated protein SCS2 (VAMP-associated protein SCS2) (Choline sensitivity suppressor protein 2) (VAP homolog 1)

 SCS2_YEAST              Reviewed;         244 AA.
P40075; D3DM26;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 156.
RecName: Full=Vesicle-associated membrane protein-associated protein SCS2;
Short=VAMP-associated protein SCS2;
AltName: Full=Choline sensitivity suppressor protein 2;
AltName: Full=VAP homolog 1;
Name=SCS2; OrderedLocusNames=YER120W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8537323;
Nikawa J., Murakami A., Esumi E., Hosaka K.;
"Cloning and sequence of the SCS2 gene, which can suppress the defect
of INO1 expression in an inositol auxotrophic mutant of Saccharomyces
cerevisiae.";
J. Biochem. 118:39-45(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 2-14; 85-113; 144-156 AND 166-180, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (JUN-2005) to UniProtKB.
[6]
TOPOLOGY, AND SUBCELLULAR LOCATION.
PubMed=9537365;
Kagiwada S., Hosaka K., Murata M., Nikawa J., Takatsuki A.;
"The Saccharomyces cerevisiae SCS2 gene product, a homolog of a
synaptobrevin-associated protein, is an integral membrane protein of
the endoplasmic reticulum and is required for inositol metabolism.";
J. Bacteriol. 180:1700-1708(1998).
[7]
FUNCTION, INTERACTION WITH OPI1, AND SUBCELLULAR LOCATION.
PubMed=12727870; DOI=10.1093/emboj/cdg201;
Loewen C.J.R., Roy A., Levine T.P.;
"A conserved ER targeting motif in three families of lipid binding
proteins and in Opi1p binds VAP.";
EMBO J. 22:2025-2035(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
INTERACTION WITH OPI1, AND SUBCELLULAR LOCATION.
PubMed=15455074; DOI=10.1371/journal.pbio.0020342;
Brickner J.H., Walter P.;
"Gene recruitment of the activated INO1 locus to the nuclear
membrane.";
PLoS Biol. 2:1843-1852(2004).
[11]
FUNCTION, AND MUTAGENESIS OF LYS-40; 41-THR-THR-42 AND LYS-120.
PubMed=15668246; DOI=10.1074/jbc.M500147200;
Loewen C.J.R., Levine T.P.;
"A highly conserved binding site in vesicle-associated membrane
protein-associated protein (VAP) for the FFAT motif of lipid-binding
proteins.";
J. Biol. Chem. 280:14097-14104(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[13]
FFAT MOTIF-BINDING, AND MUTAGENESIS OF LYS-84 AND LEU-86.
PubMed=16004875; DOI=10.1016/j.str.2005.04.010;
Kaiser S.E., Brickner J.H., Reilein A.R., Fenn T.D., Walter P.,
Brunger A.T.;
"Structural basis of FFAT motif-mediated ER targeting.";
Structure 13:1035-1045(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Targets proteins containing a FFAT motif to endoplasmic
reticulum membranes. Regulates phospholipid biosynthesis by
modulating the subcellular localization of the transcriptional
repressor OPI1. {ECO:0000269|PubMed:12727870,
ECO:0000269|PubMed:15668246}.
-!- SUBUNIT: Interacts with OPI1. {ECO:0000269|PubMed:12727870,
ECO:0000269|PubMed:15455074}.
-!- INTERACTION:
Q00402:NUM1; NbExp=4; IntAct=EBI-16735, EBI-12386;
P21957:OPI1; NbExp=3; IntAct=EBI-16735, EBI-12555;
P38713:OSH3; NbExp=2; IntAct=EBI-16735, EBI-12630;
Q07657:SHS1; NbExp=4; IntAct=EBI-16735, EBI-22083;
P39523:YMR124W; NbExp=4; IntAct=EBI-16735, EBI-27256;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type IV membrane protein. Nucleus membrane; Single-pass type IV
membrane protein.
-!- DOMAIN: The MSP domain is required for binding to the FFAT motif
of target proteins.
-!- MISCELLANEOUS: Present with 3497 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC
9.B.17) family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; D44493; BAA07936.1; -; Genomic_DNA.
EMBL; U18916; AAC03218.1; -; Genomic_DNA.
EMBL; AY693125; AAT93144.1; -; Genomic_DNA.
EMBL; BK006939; DAA07780.1; -; Genomic_DNA.
PIR; S50623; S50623.
RefSeq; NP_011046.3; NM_001179010.3.
ProteinModelPortal; P40075; -.
SMR; P40075; -.
BioGrid; 36865; 317.
DIP; DIP-2272N; -.
IntAct; P40075; 57.
MINT; MINT-619890; -.
STRING; 4932.YER120W; -.
iPTMnet; P40075; -.
MaxQB; P40075; -.
PRIDE; P40075; -.
EnsemblFungi; YER120W; YER120W; YER120W.
GeneID; 856856; -.
KEGG; sce:YER120W; -.
EuPathDB; FungiDB:YER120W; -.
SGD; S000000922; SCS2.
GeneTree; ENSGT00390000006947; -.
HOGENOM; HOG000066102; -.
InParanoid; P40075; -.
OrthoDB; EOG092C5DHN; -.
BioCyc; YEAST:G3O-30284-MONOMER; -.
Reactome; R-SCE-6798695; Neutrophil degranulation.
PRO; PR:P40075; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0005635; C:nuclear envelope; IDA:SGD.
GO; GO:0031965; C:nuclear membrane; IDA:SGD.
GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0033149; F:FFAT motif binding; IMP:SGD.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0048309; P:endoplasmic reticulum inheritance; IMP:SGD.
GO; GO:0090158; P:endoplasmic reticulum membrane organization; IGI:SGD.
GO; GO:0061163; P:endoplasmic reticulum polarization; IDA:SGD.
GO; GO:0042992; P:negative regulation of transcription factor import into nucleus; IMP:SGD.
GO; GO:0008654; P:phospholipid biosynthetic process; IMP:SGD.
GO; GO:0032377; P:regulation of intracellular lipid transport; IMP:SGD.
GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IGI:SGD.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR000535; MSP_dom.
InterPro; IPR008962; PapD-like_sf.
InterPro; IPR016763; VAP.
PANTHER; PTHR10809; PTHR10809; 1.
Pfam; PF00635; Motile_Sperm; 1.
PIRSF; PIRSF019693; VAMP-associated; 1.
SUPFAM; SSF49354; SSF49354; 1.
PROSITE; PS50202; MSP; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.5}.
CHAIN 2 244 Vesicle-associated membrane protein-
associated protein SCS2.
/FTId=PRO_0000213467.
TOPO_DOM 2 222 Cytoplasmic. {ECO:0000255}.
TRANSMEM 223 243 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 244 244 Lumenal. {ECO:0000255}.
DOMAIN 3 126 MSP. {ECO:0000255|PROSITE-
ProRule:PRU00132}.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.5}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:19779198}.
MUTAGEN 40 40 K->N: Disrupts binding to FFAT motif and
causes OPI1 mislocalization.
{ECO:0000269|PubMed:15668246}.
MUTAGEN 41 42 TT->AA: Disrupts binding to FFAT motif
and causes OPI1 mislocalization.
{ECO:0000269|PubMed:15668246}.
MUTAGEN 84 84 K->D: Disrupts binding to FFAT motif;
when associated with D-86.
{ECO:0000269|PubMed:16004875}.
MUTAGEN 86 86 L->D: Disrupts binding to FFAT motif;
when associated with D-84.
{ECO:0000269|PubMed:16004875}.
MUTAGEN 120 120 K->N: Reduces binding to FFAT motif and
impairs OPI1 function.
{ECO:0000269|PubMed:15668246}.
SEQUENCE 244 AA; 26926 MW; 45390E24E31D392E CRC64;
MSAVEISPDV LVYKSPLTEQ STEYASISNN SDQTIAFKVK TTAPKFYCVR PNAAVVAPGE
TIQVQVIFLG LTEEPAADFK CRDKFLVITL PSPYDLNGKA VADVWSDLEA EFKQQAISKK
IKVKYLISPD VHPAQNQNIQ ENKETVEPVV QDSEPKEVPA VVNEKEVPAE PETQPPVQVK
KEEVPPVVQK TVPHENEKQT SNSTPAPQNQ IKEAATVPAE NESSSMGIFI LVALLILVLG
WFYR


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