VTS1_YEAST
ID VTS1_YEAST Reviewed; 523 AA.
AC Q08831; D6W354;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=RNA-binding protein VTS1 {ECO:0000303|PubMed:12858164};
DE AltName: Full=VTI1-2 suppressor protein 1;
GN Name=VTS1; OrderedLocusNames=YOR359W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11445562; DOI=10.1074/jbc.m101551200;
RA Dilcher M., Koehler B., von Mollard G.F.;
RT "Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions
RT for the R-SNARE YKT6.";
RL J. Biol. Chem. 276:34537-34544(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION, DOMAIN, RNA-BINDING, AND MUTAGENESIS OF LYS-467 AND ALA-498.
RX PubMed=12858164; DOI=10.1038/nsb956;
RA Aviv T., Lin Z., Lau S., Rendl L.M., Sicheri F., Smibert C.A.;
RT "The RNA-binding SAM domain of Smaug defines a new family of post-
RT transcriptional regulators.";
RL Nat. Struct. Biol. 10:614-621(2003).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY 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: RNA-binding protein involved in post-transcriptional
CC regulation through transcript degradation of SRE (SMG-recognition
CC elements) bearing mRNAs. {ECO:0000269|PubMed:12858164}.
CC -!- SUBUNIT: Monomer. Binds to RNA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11445562,
CC ECO:0000269|PubMed:14562095}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:J9VVN9}.
CC -!- DOMAIN: The SAM domain is essential for RNA-binding.
CC {ECO:0000269|PubMed:12858164}.
CC -!- MISCELLANEOUS: Present with 3200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VTS1 family. {ECO:0000305}.
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DR EMBL; Z75267; CAA99688.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11120.1; -; Genomic_DNA.
DR PIR; S67271; S67271.
DR RefSeq; NP_015004.3; NM_001183779.3.
DR PDB; 2B6G; NMR; -; A=407-523.
DR PDB; 2D3D; X-ray; 1.60 A; A=436-523.
DR PDB; 2ES6; NMR; -; A=373-523.
DR PDB; 2ESE; NMR; -; A=373-523.
DR PDB; 2F8K; X-ray; 2.00 A; A=436-523.
DR PDB; 2FE9; NMR; -; A=438-523.
DR PDBsum; 2B6G; -.
DR PDBsum; 2D3D; -.
DR PDBsum; 2ES6; -.
DR PDBsum; 2ESE; -.
DR PDBsum; 2F8K; -.
DR PDBsum; 2FE9; -.
DR AlphaFoldDB; Q08831; -.
DR BMRB; Q08831; -.
DR SMR; Q08831; -.
DR BioGRID; 34744; 498.
DR DIP; DIP-1279N; -.
DR IntAct; Q08831; 4.
DR MINT; Q08831; -.
DR STRING; 4932.YOR359W; -.
DR TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; Q08831; -.
DR MaxQB; Q08831; -.
DR PaxDb; Q08831; -.
DR PRIDE; Q08831; -.
DR EnsemblFungi; YOR359W_mRNA; YOR359W; YOR359W.
DR GeneID; 854541; -.
DR KEGG; sce:YOR359W; -.
DR SGD; S000005886; VTS1.
DR VEuPathDB; FungiDB:YOR359W; -.
DR eggNOG; KOG3791; Eukaryota.
DR GeneTree; ENSGT00940000169155; -.
DR HOGENOM; CLU_595905_0_0_1; -.
DR InParanoid; Q08831; -.
DR OMA; QQNTVMD; -.
DR BioCyc; YEAST:G3O-33830-MON; -.
DR EvolutionaryTrace; Q08831; -.
DR PRO; PR:Q08831; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08831; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0070336; F:flap-structured DNA binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:SGD.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd09556; SAM_VTS1_fungal; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037635; VTS1_SAM.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleotide-binding; Protein transport;
KW Reference proteome; RNA-binding; Transport.
FT CHAIN 1..523
FT /note="RNA-binding protein VTS1"
FT /id="PRO_0000081458"
FT DOMAIN 451..512
FT /note="SAM"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 467
FT /note="K->Q: Loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:12858164"
FT MUTAGEN 498
FT /note="A->Q: Loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:12858164"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 496..514
FT /evidence="ECO:0007829|PDB:2D3D"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:2D3D"
SQ SEQUENCE 523 AA; 57557 MW; 56F55D1A8B4C0EDD CRC64;
MKHPYEEFPT GSKSPYNMSR GAHPGAVLLS PQSSAINKNN PGSNSGNNQG NSSVTANVLS
PQSHSMSLND MLDQQSFMLD TAGTRAQPLQ QQQQQQQQQQ QASLPSLNIQ TVSSTAAGSA
IVSPMMQSPK ALQSTLSSTS MYLDSFQRSP NNILGIPSQS GSIPLPQSRQ SQQQSQSQKN
DPNMGTNFSQ DINQLCSWIS MLNSSQQNTV MDNILSILND DVLKYTKLKI ETLTNTPFIS
PPLPAIASPI PNRDDTQILN IDSVFSSSPI TNDPENTDNL LYQNWSPQPH SIPISQPIYD
NITDASQRSK SAEPHVNSSP NLIPVQKQFN NGNSTKYKKL PSENPNYLSH SLSSSHSFFQ
PKKRSNMGNE YNSHHHHSLH HPLHNTTSYF SNTSRPSGTD LNKSNQNVFN NTITHPNAGP
TSATSTSTSS NGNTPLSSNS SMNPKSLTDP KLLKNIPMWL KSLRLHKYSD ALSGTPWIEL
IYLDDETLEK KGVLALGARR KLLKAFGIVI DYKERDLIDR SAY
