SNF7_YEAST
ID SNF7_YEAST Reviewed; 240 AA.
AC P39929; D6VY27; E9P8V6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Vacuolar-sorting protein SNF7 {ECO:0000305};
DE AltName: Full=DOA4-independent degradation protein 1 {ECO:0000303|PubMed:11029042};
DE AltName: Full=Sucrose nonfermenting protein 7 {ECO:0000303|PubMed:1752413};
DE AltName: Full=Vacuolar protein-sorting-associated protein 32 {ECO:0000303|PubMed:3062374};
GN Name=SNF7 {ECO:0000303|PubMed:1752413};
GN Synonyms=DID1 {ECO:0000303|PubMed:11029042},
GN VPS32 {ECO:0000303|PubMed:3062374};
GN OrderedLocusNames=YLR025W {ECO:0000312|SGD:S000004015};
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8224817; DOI=10.1093/genetics/135.1.17;
RA Tu J., Vallier L.G., Carlson M.;
RT "Molecular and genetic analysis of the SNF7 gene in Saccharomyces
RT cerevisiae.";
RL Genetics 135:17-23(1993).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=3062374; DOI=10.1128/mcb.8.11.4936-4948.1988;
RA Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.;
RT "Protein sorting in Saccharomyces cerevisiae: isolation of mutants
RT defective in the delivery and processing of multiple vacuolar hydrolases.";
RL Mol. Cell. Biol. 8:4936-4948(1988).
RN [6]
RP IDENTIFICATION.
RX PubMed=1752413; DOI=10.1093/genetics/129.3.675;
RA Vallier L.G., Carlson M.;
RT "New SNF genes, GAL11 and GRR1 affect SUC2 expression in Saccharomyces
RT cerevisiae.";
RL Genetics 129:675-684(1991).
RN [7]
RP FUNCTION.
RX PubMed=11029042; DOI=10.1091/mbc.11.10.3365;
RA Amerik A.Y., Nowak J., Swaminathan S., Hochstrasser M.;
RT "The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar
RT protein-sorting and endocytic pathways.";
RL Mol. Biol. Cell 11:3365-3380(2000).
RN [8]
RP FUNCTION.
RX PubMed=11559748; DOI=10.1242/jcs.114.13.2395;
RA Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
RT "CHMP1 functions as a member of a newly defined family of vesicle
RT trafficking proteins.";
RL J. Cell Sci. 114:2395-2404(2001).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS20,
RP AND SUBCELLULAR LOCATION.
RX PubMed=12194857; DOI=10.1016/s1534-5807(02)00220-4;
RA Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D.;
RT "Escrt-III: an endosome-associated heterooligomeric protein complex
RT required for mvb sorting.";
RL Dev. Cell 3:271-282(2002).
RN [10]
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 [11]
RP INTERACTION WITH BRO1.
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 [12]
RP INTERACTION WITH BRO1, AND FUNCTION.
RX PubMed=15935782; DOI=10.1016/j.devcel.2005.04.001;
RA Kim J., Sitaraman S., Hierro A., Beach B.M., Odorizzi G., Hurley J.H.;
RT "Structural basis for endosomal targeting by the Bro1 domain.";
RL Dev. Cell 8:937-947(2005).
RN [13]
RP INTERACTION WITH VTA1.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP ASSEMBLY OF THE ESCRT-III COMPLEX.
RX PubMed=18854142; DOI=10.1016/j.devcel.2008.08.013;
RA Teis D., Saksena S., Emr S.D.;
RT "Ordered assembly of the ESCRT-III complex on endosomes is required to
RT sequester cargo during MVB formation.";
RL Dev. Cell 15:578-589(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-193, AND
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 [18]
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 [19]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [20]
RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-2; PHE-6 AND
RP TRP-8.
RX PubMed=24139821; DOI=10.1016/j.devcel.2013.09.009;
RA Buchkovich N.J., Henne W.M., Tang S., Emr S.D.;
RT "Essential N-terminal insertion motif anchors the ESCRT-III filament during
RT MVB vesicle formation.";
RL Dev. Cell 27:201-214(2013).
RN [21]
RP INTERACTION WITH BRO1; RIM20; VPS20; VPS24; VPS4; VTA1 AND YGR122W.
RX PubMed=24058170; DOI=10.1128/ec.00241-13;
RA Sciskala B., Koelling R.;
RT "Interaction maps of the Saccharomyces cerevisiae ESCRT-III protein Snf7.";
RL Eukaryot. Cell 12:1538-1546(2013).
RN [22]
RP INTERACTION WITH VPS4, AND FUNCTION OF THE ESCRT-III COMPLEX.
RX PubMed=24711499; DOI=10.1083/jcb.201310114;
RA Adell M.A., Vogel G.F., Pakdel M., Mueller M., Lindner H., Hess M.W.,
RA Teis D.;
RT "Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction
RT during MVB vesicle formation.";
RL J. Cell Biol. 205:33-49(2014).
RN [23]
RP FUNCTION, INTERACTION WITH HEH1 AND HEH2, AND SUBCELLULAR LOCATION.
RX PubMed=25303532; DOI=10.1016/j.cell.2014.09.012;
RA Webster B.M., Colombi P., Jaeger J., Lusk C.P.;
RT "Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4.";
RL Cell 159:388-401(2014).
RN [24]
RP INTERACTION WITH DOA4.
RX PubMed=26427873; DOI=10.1016/j.bbrc.2015.09.136;
RA Wolters N., Amerik A.;
RT "The N-terminal domains determine cellular localization and functions of
RT the Doa4 and Ubp5 deubiquitinating enzymes.";
RL Biochem. Biophys. Res. Commun. 467:570-576(2015).
RN [25]
RP FUNCTION, SUBUNIT, AND ELECTRON MICROSCOPY.
RX PubMed=26522593; DOI=10.1016/j.cell.2015.10.017;
RA Chiaruttini N., Redondo-Morata L., Colom A., Humbert F., Lenz M.,
RA Scheuring S., Roux A.;
RT "Relaxation of loaded ESCRT-III spiral springs drives membrane
RT deformation.";
RL Cell 163:866-879(2015).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 12-150, MUTAGENESIS OF ARG-25;
RP HIS-29; LYS-36; ARG-52; THR-83; MET-87; GLN-90; ILE-94; GLU-95; ALA-97;
RP LEU-99; LEU-101; GLU-102; THR-103; MET-104; MET-107; GLU-109; MET-114;
RP ILE-117 AND LEU-121, AND FUNCTION.
RX PubMed=26670543; DOI=10.7554/elife.12548;
RA Tang S., Henne W.M., Borbat P.P., Buchkovich N.J., Freed J.H., Mao Y.,
RA Fromme J.C., Emr S.D.;
RT "Structural basis for activation, assembly and membrane binding of ESCRT-
RT III Snf7 filaments.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Acts a component of the ESCRT-III complex required for the
CC sorting and concentration of proteins resulting in the entry of these
CC proteins into the invaginating vesicles of the multivesicular body
CC (MVB) (PubMed:11559748, PubMed:12194857). The sequential action of
CC ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III
CC links membrane invagination to cargo sorting (PubMed:12194857).
CC Membrane scission in the neck of the growing vesicle releases mature,
CC cargo-laden ILVs into the lumen (PubMed:24139821, PubMed:24711499).
CC ESCRT-III is critical for late steps in MVB sorting, such as membrane
CC invagination and final cargo sorting and recruitment of late-acting
CC components of the sorting machinery (PubMed:24139821, PubMed:24711499).
CC SNF7 is the most abundant ESCRT-III subunit which forms membrane-
CC sculpting filaments with 30 Angstrom periodicity and a exposed cationic
CC membrane-binding surface (PubMed:26670543). Its activation requires a
CC prominent conformational rearrangement to expose protein-membrane and
CC protein-protein interfaces (PubMed:26670543). SNF7 filaments then form
CC spirals that could function as spiral springs (PubMed:26522593). The
CC elastic expansion of compressed SNF7 spirals generates an area
CC difference between the two sides of the membrane and thus curvature
CC which could be the origin of membrane deformation leading eventually to
CC fission (PubMed:26522593). SNF7 recruits BRO1, which in turn recruits
CC DOA4, which deubiquitinates cargos before their enclosure within MVB
CC vesicles (PubMed:11029042, PubMed:15935782). ESCRT-III is also
CC recruited to the nuclear envelope (NE) by integral INM proteins to
CC surveil and clear defective nuclear pore complex (NPC) assembly
CC intermediates to ensure the fidelity of NPC assembly (PubMed:25303532).
CC {ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:12194857,
CC ECO:0000269|PubMed:15935782, ECO:0000269|PubMed:24139821,
CC ECO:0000269|PubMed:24711499, ECO:0000269|PubMed:25303532,
CC ECO:0000269|PubMed:26522593, ECO:0000269|PubMed:3062374}.
CC -!- SUBUNIT: Core component of the ESCRT-III complex (endosomal sorting
CC required for transport complex III) (PubMed:12194857, PubMed:18854142).
CC ESCRT-III appears to be sequentially assembled as a flat lattice on the
CC endosome membrane and forms a transient 450 kDa complex that contains
CC DID4, oligomerized SNF7, VPS20 and VPS24 (PubMed:18854142). SNF7
CC polymerizes into spirals at the surface of lipid bilayers
CC (PubMed:26522593). SNF7 polymerization is nucleated by association of
CC SNF7 with VPS20; the process is terminated through association of
CC VPS24, possibly by capping the SNF7 filament (PubMed:24058170,
CC PubMed:24711499). Interacts with VTA1; the interaction requires DID2
CC (PubMed:16601096, PubMed:24058170). Interacts with BRO1
CC (PubMed:15086794, PubMed:15935782, PubMed:24058170). Interacts with
CC DOA4 (PubMed:26427873). Interacts with HEH1 and HEH2 (PubMed:25303532).
CC Interacts with RIM20 and YGR122W (PubMed:24058170).
CC {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:15086794,
CC ECO:0000269|PubMed:15935782, ECO:0000269|PubMed:16601096,
CC ECO:0000269|PubMed:18854142, ECO:0000269|PubMed:24058170,
CC ECO:0000269|PubMed:24711499, ECO:0000269|PubMed:25303532,
CC ECO:0000269|PubMed:26427873, ECO:0000269|PubMed:26522593}.
CC -!- INTERACTION:
CC P39929; P48582: BRO1; NbExp=3; IntAct=EBI-17554, EBI-3768;
CC P39929; P36108: DID4; NbExp=4; IntAct=EBI-17554, EBI-26574;
CC P39929; Q03281: HEH2; NbExp=3; IntAct=EBI-17554, EBI-22131;
CC P39929; P39929: SNF7; NbExp=9; IntAct=EBI-17554, EBI-17554;
CC P39929; Q04272: VPS20; NbExp=5; IntAct=EBI-17554, EBI-28157;
CC P39929; Q06263: VTA1; NbExp=2; IntAct=EBI-17554, EBI-37098;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12194857}. Endosome
CC membrane {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821};
CC Peripheral membrane protein {ECO:0000269|PubMed:12194857,
CC ECO:0000269|PubMed:24139821}. Nucleus envelope
CC {ECO:0000269|PubMed:25303532}.
CC -!- DOMAIN: The N-terminus (residues 1 to 11) forms an amphipathic helix
CC which is required for the association to membrane.
CC {ECO:0000269|PubMed:24139821}.
CC -!- DISRUPTION PHENOTYPE: Exhibits defects in the sorting and processing of
CC native vacuolar proteins (PubMed:3062374).
CC {ECO:0000269|PubMed:3062374}.
CC -!- MISCELLANEOUS: Present with 3270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a nuclear protein and mutations
CC were shown to prevent full derepression of the SUC2 (invertase) gene.
CC {ECO:0000305|PubMed:8224817}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On releasing tension - Issue
CC 180 of June 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/180/";
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DR EMBL; L09751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z73197; CAA97548.1; -; Genomic_DNA.
DR EMBL; AY558202; AAS56528.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09343.1; -; Genomic_DNA.
DR PIR; S52590; S52590.
DR RefSeq; NP_013125.1; NM_001181912.1.
DR PDB; 5FD7; X-ray; 2.40 A; A=12-150.
DR PDB; 5FD9; X-ray; 1.60 A; A=12-150.
DR PDB; 5T8L; X-ray; 2.20 A; A=12-150.
DR PDB; 5T8N; X-ray; 2.20 A; A=12-150.
DR PDBsum; 5FD7; -.
DR PDBsum; 5FD9; -.
DR PDBsum; 5T8L; -.
DR PDBsum; 5T8N; -.
DR AlphaFoldDB; P39929; -.
DR SMR; P39929; -.
DR BioGRID; 31299; 159.
DR ComplexPortal; CPX-1624; ESCRT-III complex.
DR DIP; DIP-1747N; -.
DR IntAct; P39929; 26.
DR MINT; P39929; -.
DR STRING; 4932.YLR025W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P39929; -.
DR MaxQB; P39929; -.
DR PaxDb; P39929; -.
DR PRIDE; P39929; -.
DR EnsemblFungi; YLR025W_mRNA; YLR025W; YLR025W.
DR GeneID; 850712; -.
DR KEGG; sce:YLR025W; -.
DR SGD; S000004015; SNF7.
DR VEuPathDB; FungiDB:YLR025W; -.
DR eggNOG; KOG1656; Eukaryota.
DR HOGENOM; CLU_071097_1_0_1; -.
DR InParanoid; P39929; -.
DR OMA; WSWFGGA; -.
DR BioCyc; YEAST:G3O-32186-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:P39929; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P39929; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0000815; C:ESCRT III complex; IDA:SGD.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0071454; P:cellular response to anoxia; IMP:SGD.
DR GO; GO:1904902; P:ESCRT III complex assembly; IDA:SGD.
DR GO; GO:0070676; P:intralumenal vesicle formation; IMP: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; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IDA:SGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..240
FT /note="Vacuolar-sorting protein SNF7"
FT /id="PRO_0000211446"
FT REGION 193..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 2
FT /note="W->E: Impairs binding to membrane."
FT /evidence="ECO:0000269|PubMed:24139821"
FT MUTAGEN 6
FT /note="F->E: Impairs binding to membrane."
FT /evidence="ECO:0000269|PubMed:24139821"
FT MUTAGEN 8
FT /note="W->E: Impairs binding to membrane."
FT /evidence="ECO:0000269|PubMed:24139821"
FT MUTAGEN 25
FT /note="R->E: Leads to severe sorting defects; when
FT associated with E-29 and E-36."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 29
FT /note="H->E: Leads to severe sorting defects; when
FT associated with E-25 and E-36."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 36
FT /note="K->E: Leads to severe sorting defects; when
FT associated with E-25 and E-29."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 52
FT /note="R->E: Impairs the formation of protofilaments; when
FT associated with K-90. Also impairs the formation of
FT protofilaments; when associated with E-94. Also impairs the
FT formation of protofilaments; when associated with E-107.
FT Also impairs the formation of protofilaments; when
FT associated with E-114."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 83
FT /note="T->E: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 87
FT /note="M->E: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 90
FT /note="Q->K: Leads to severe sorting defects. Impairs the
FT formation of protofilaments; when associated with E-52."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 94
FT /note="I->E: Leads to severe sorting defects. Impairs the
FT formation of protofilaments; when associated with E-52."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 95
FT /note="E->K: Leads to severe sorting defects; when
FT associated with K-102 and K-109."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 97
FT /note="A->K: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 99
FT /note="L->K: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 101
FT /note="L->E: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 102
FT /note="E->K: Leads to severe sorting defects; when
FT associated with K-95 and K-109."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 103
FT /note="T->E: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 104
FT /note="M->E: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 107
FT /note="M->E: Leads to severe sorting defects. Impairs the
FT formation of protofilaments; when associated with E-52."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 109
FT /note="E->K: Leads to severe sorting defects; when
FT associated with K-95 and K-102."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 114
FT /note="M->E: Leads to severe sorting defects. Impairs the
FT formation of protofilaments; when associated with E-52."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 117
FT /note="I->E: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT MUTAGEN 121
FT /note="L->D: Leads to severe sorting defects."
FT /evidence="ECO:0000269|PubMed:26670543"
FT CONFLICT 173
FT /note="E -> G (in Ref. 4; AAS56528)"
FT /evidence="ECO:0000305"
FT HELIX 19..56
FT /evidence="ECO:0007829|PDB:5FD9"
FT HELIX 60..118
FT /evidence="ECO:0007829|PDB:5FD9"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5FD7"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:5FD9"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:5FD9"
SQ SEQUENCE 240 AA; 26987 MW; 5241A18BB181F0C1 CRC64;
MWSSLFGWTS SNAKNKESPT KAIVRLREHI NLLSKKQSHL RTQITNQENE ARIFLTKGNK
VMAKNALKKK KTIEQLLSKV EGTMESMEQQ LFSIESANLN LETMRAMQEG AKAMKTIHSG
LDIDKVDETM DEIREQVELG DEISDAISRP LITGANEVDE DELDEELDML AQENANQETS
KIVNNNVNAA PISENKVSLP SVPSNKIKQS ENSVKDGEEE EDEEDEDEKA LRELQAEMGL
