VTA1_YEAST
ID VTA1_YEAST Reviewed; 330 AA.
AC Q06263; D6VYI5; Q07057;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Vacuolar protein sorting-associated protein VTA1;
DE AltName: Full=VPS20-associated protein 1;
GN Name=VTA1; OrderedLocusNames=YLR181C;
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=3316224; DOI=10.1016/s0021-9258(18)49312-x;
RA Thomas D., Surdin-Kerjan Y.;
RT "SAM1, the structural gene for one of the S-adenosylmethionine synthetases
RT in Saccharomyces cerevisiae. Sequence and expression.";
RL J. Biol. Chem. 262:16704-16709(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH VPS4.
RX PubMed=12953057; DOI=10.1242/jcs.00751;
RA Yeo S.C.L., Xu L., Ren J., Boulton V.J., Wagle M.D., Liu C., Ren G.,
RA Wong P., Zahn R., Sasajala P., Yang H., Piper R.C., Munn A.L.;
RT "Vps20p and Vta1p interact with Vps4p and function in multivesicular body
RT sorting and endosomal transport in Saccharomyces cerevisiae.";
RL J. Cell Sci. 116:3957-3970(2003).
RN [5]
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 [6]
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 [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH VPS60, AND SUBCELLULAR LOCATION.
RX PubMed=14701806; DOI=10.1074/jbc.m312669200;
RA Shiflett S.L., Ward D.M., Huynh D., Vaughn M.B., Simmons J.C., Kaplan J.;
RT "Characterization of Vta1p, a class E Vps protein in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 279:10982-10990(2004).
RN [8]
RP INTERACTION WITH DID2.
RX PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x;
RA Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P.,
RA Stevens T.H.;
RT "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces
RT cerevisiae.";
RL Traffic 5:194-210(2004).
RN [9]
RP FUNCTION, INTERACTION WITH VSP4 AND VSP60, AND MUTAGENESIS OF LYS-299;
RP LYS-302; SER-306 AND LYS-322.
RX PubMed=16505166; DOI=10.1083/jcb.200508166;
RA Azmi I., Davies B., Dimaano C., Payne J., Eckert D., Babst M.,
RA Katzmann D.J.;
RT "Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL
RT region in Vta1.";
RL J. Cell Biol. 172:705-717(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH SNF7 AND DID2.
RX PubMed=16601096; DOI=10.1073/pnas.0601712103;
RA Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H.;
RT "Vta1p and Vps46p regulate the membrane association and ATPase activity of
RT Vps4p at the yeast multivesicular body.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006).
RN [11]
RP INTERACTION WITH DID2.
RX PubMed=18194652; DOI=10.1016/j.devcel.2007.10.021;
RA Azmi I.F., Davies B.A., Xiao J., Babst M., Xu Z., Katzmann D.J.;
RT "ESCRT-III family members stimulate Vps4 ATPase activity directly or via
RT Vta1.";
RL Dev. Cell 14:50-61(2008).
RN [12]
RP INTERACTION WITH VSP4.
RX PubMed=18280501; DOI=10.1016/j.jmb.2008.01.009;
RA Yu Z., Gonciarz M.D., Sundquist W.I., Hill C.P., Jensen G.J.;
RT "Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p.";
RL J. Mol. Biol. 377:364-377(2008).
RN [13]
RP INTERACTION WITH VPS60.
RX PubMed=18032584; DOI=10.1091/mbc.e07-07-0694;
RA Rue S.M., Mattei S., Saksena S., Emr S.D.;
RT "Novel Ist1-Did2 complex functions at a late step in multivesicular body
RT sorting.";
RL Mol. Biol. Cell 19:475-484(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; THR-195 AND SER-233, AND
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).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-167, X-RAY CRYSTALLOGRAPHY (1.5
RP ANGSTROMS) OF 280-330, INTERACTION WITH VPS60 AND DID2, AND MUTAGENESIS OF
RP TRP-122; LYS-152; TYR-303; TYR-310; GLU-311; ASP-312; LEU-320 AND LEU-327.
RX PubMed=18194651; DOI=10.1016/j.devcel.2007.10.013;
RA Xiao J., Xia H., Zhou J., Azmi I.F., Davies B.A., Katzmann D.J., Xu Z.;
RT "Structural basis of Vta1 function in the multivesicular body sorting
RT pathway.";
RL Dev. Cell 14:37-49(2008).
CC -!- FUNCTION: Has a role in the formation of the multivesicular body (MVB).
CC Required for the sorting of lipids to form intralumenal vesicles and
CC for fluid-phase transport to the vacuole. Required for sorting the
CC plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of
CC VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase
CC activity by 6- to 8-fold. {ECO:0000269|PubMed:12953057,
CC ECO:0000269|PubMed:14701806, ECO:0000269|PubMed:16505166,
CC ECO:0000269|PubMed:16601096}.
CC -!- SUBUNIT: Homodimer (in cytoplasm). Interacts with VPS4; the interaction
CC requires the dimeric structure of VTA1; 6 homodimers of VTA1 appear to
CC associate with the dodecameric VSP4 complex; the interaction is ADP-
CC dependent. Interacts with SNF7; the interaction requires DID2.
CC Interacts with DID2. Interacts with VPS60; the interaction occurs at he
CC endosomal membrane. {ECO:0000269|PubMed:12953057,
CC ECO:0000269|PubMed:14701806, ECO:0000269|PubMed:15086794,
CC ECO:0000269|PubMed:16505166, ECO:0000269|PubMed:16601096,
CC ECO:0000269|PubMed:18032584, ECO:0000269|PubMed:18194651,
CC ECO:0000269|PubMed:18194652, ECO:0000269|PubMed:18280501}.
CC -!- INTERACTION:
CC Q06263; P69771: DID2; NbExp=3; IntAct=EBI-37098, EBI-2053489;
CC Q06263; P39929: SNF7; NbExp=2; IntAct=EBI-37098, EBI-17554;
CC Q06263; P52917: VPS4; NbExp=12; IntAct=EBI-37098, EBI-20475;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14701806}. Endosome
CC membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14701806}.
CC -!- MISCELLANEOUS: Present with 4400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VTA1 family. {ECO:0000305}.
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DR EMBL; J03477; AAA66933.1; -; Genomic_DNA.
DR EMBL; U17246; AAB67473.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09501.1; -; Genomic_DNA.
DR PIR; S51426; S51426.
DR RefSeq; NP_013282.1; NM_001182068.1.
DR PDB; 2LUH; NMR; -; A=1-167.
DR PDB; 2RKK; X-ray; 2.90 A; A/B=1-167.
DR PDB; 2RKL; X-ray; 1.50 A; A/B/C/D/E/F=280-330.
DR PDB; 3MHV; X-ray; 3.10 A; A=289-330.
DR PDB; 5H7P; NMR; -; A=1-167.
DR PDB; 5UIE; EM; 5.70 A; H/I/J/K/L/M/N/O/P/Q/R/S=1-330.
DR PDB; 5XMK; EM; 4.18 A; G/H/I/J/K/L/M/N=1-330.
DR PDB; 6AP1; EM; 3.20 A; H/I/J/K/L/M/N/O/P/Q/R/S=1-330.
DR PDB; 6OO2; EM; 4.40 A; H/I/J/K/L/M/N/O/P/Q/R/S=280-330.
DR PDBsum; 2LUH; -.
DR PDBsum; 2RKK; -.
DR PDBsum; 2RKL; -.
DR PDBsum; 3MHV; -.
DR PDBsum; 5H7P; -.
DR PDBsum; 5UIE; -.
DR PDBsum; 5XMK; -.
DR PDBsum; 6AP1; -.
DR PDBsum; 6OO2; -.
DR AlphaFoldDB; Q06263; -.
DR BMRB; Q06263; -.
DR SMR; Q06263; -.
DR BioGRID; 31452; 106.
DR DIP; DIP-4802N; -.
DR IntAct; Q06263; 8.
DR MINT; Q06263; -.
DR STRING; 4932.YLR181C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; Q06263; -.
DR MaxQB; Q06263; -.
DR PaxDb; Q06263; -.
DR PRIDE; Q06263; -.
DR DNASU; 850878; -.
DR EnsemblFungi; YLR181C_mRNA; YLR181C; YLR181C.
DR GeneID; 850878; -.
DR KEGG; sce:YLR181C; -.
DR SGD; S000004171; VTA1.
DR VEuPathDB; FungiDB:YLR181C; -.
DR eggNOG; ENOG502RXP8; Eukaryota.
DR HOGENOM; CLU_063501_0_0_1; -.
DR InParanoid; Q06263; -.
DR OMA; YCKIYVL; -.
DR BioCyc; YEAST:G3O-32305-MON; -.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR EvolutionaryTrace; Q06263; -.
DR PRO; PR:Q06263; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06263; protein.
DR GO; GO:0005768; C:endosome; HDA:SGD.
DR GO; GO:1990621; C:ESCRT IV complex; IDA:FlyBase.
DR GO; GO:0005771; C:multivesicular body; IDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IGI:SGD.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.270; -; 1.
DR InterPro; IPR044538; Vta1-like.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR InterPro; IPR041212; Vta1_C.
DR PANTHER; PTHR46009; PTHR46009; 2.
DR Pfam; PF04652; Vta1; 1.
DR Pfam; PF18097; Vta1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Lipid transport; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..330
FT /note="Vacuolar protein sorting-associated protein VTA1"
FT /id="PRO_0000065933"
FT REGION 1..167
FT /note="Interaction with DID2"
FT REGION 37..68
FT /note="Interaction with VSP60"
FT /evidence="ECO:0000269|PubMed:16505166"
FT REGION 187..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..330
FT /note="Dimerization"
FT REGION 290..330
FT /note="Interaction with VSP4"
FT COMPBIAS 237..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 122
FT /note="W->A: Abolishes interaction with VSP60 and DID2."
FT /evidence="ECO:0000269|PubMed:18194651"
FT MUTAGEN 152
FT /note="K->A: Abolishes interaction with VSP60 and DID2."
FT /evidence="ECO:0000269|PubMed:18194651"
FT MUTAGEN 299
FT /note="K->A: Abolishes interaction with VSP4."
FT /evidence="ECO:0000269|PubMed:16505166"
FT MUTAGEN 302
FT /note="K->A: Abolishes interaction with VSP4."
FT /evidence="ECO:0000269|PubMed:16505166"
FT MUTAGEN 303
FT /note="Y->A: Abolishes interaction with VSP4, no effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:18194651"
FT MUTAGEN 306
FT /note="S->A: Diminishes interaction with VSP4."
FT /evidence="ECO:0000269|PubMed:16505166"
FT MUTAGEN 310
FT /note="Y->A: Abolishes interaction with VSP4, no effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:18194651"
FT MUTAGEN 311
FT /note="E->A: Abolishes interaction with VSP4 and
FT dimerization."
FT /evidence="ECO:0000269|PubMed:18194651"
FT MUTAGEN 312
FT /note="D->A: Abolishes interaction with VSP4 and
FT dimerization."
FT /evidence="ECO:0000269|PubMed:18194651"
FT MUTAGEN 320
FT /note="L->E: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:18194651"
FT MUTAGEN 322
FT /note="K->A: No effect on interaction with VSP4."
FT /evidence="ECO:0000269|PubMed:16505166"
FT MUTAGEN 327
FT /note="L->E: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:18194651"
FT CONFLICT 12
FT /note="A -> G (in Ref. 1; AAA66933)"
FT /evidence="ECO:0000305"
FT HELIX 1..17
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 43..61
FT /evidence="ECO:0007829|PDB:2RKK"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:5H7P"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2LUH"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 86..109
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 141..162
FT /evidence="ECO:0007829|PDB:2RKK"
FT HELIX 280..308
FT /evidence="ECO:0007829|PDB:2RKL"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2RKL"
FT HELIX 313..328
FT /evidence="ECO:0007829|PDB:2RKL"
SQ SEQUENCE 330 AA; 37316 MW; BB6E6975596C1674 CRC64;
MASNAARVVA TAKDFDKVGL GIIGYYLQLY AVELILSEED RSQEMTALAT ELLDTIEAFK
KEIGGESEAE DSDKSLHVMN TLIHDQEKAK IYMLNFTMSL YNEKLKQLKD GPWDVMLKRS
LWCCIDLFSC ILHLWKENIS ETSTNSLQKR IKYCKIYLSK LAKGEIGSSD EKTLDYADFA
DDSEEIKDED VDHQTSDLEN NNNDKVEGLA PKDQTTSYEP VDEVPEFIDD ADSVNEEEQT
VDKNEDAITK DEQQVVKKEV DLTRPSAPSE PAAAEHKSYT KDELTKIMDR ASKIEQIQKL
AKYAISALNY EDLPTAKDEL TKALDLLNSI
