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 27-MAR-2024, entry version 200. 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}, VPS32 GN {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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 170. 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; 4932-YLR025W; -. DR PeptideAtlas; P39929; -. DR EnsemblFungi; YLR025W_mRNA; YLR025W; YLR025W. DR GeneID; 850712; -. DR KEGG; sce:YLR025W; -. DR AGR; SGD:S000004015; -. DR SGD; S000004015; SNF7. DR VEuPathDB; FungiDB:YLR025W; -. DR eggNOG; KOG1656; Eukaryota. DR HOGENOM; CLU_071097_1_0_1; -. DR InParanoid; P39929; -. DR OMA; FMSYFGG; -. DR OrthoDB; 1537206at2759; -. DR BioCyc; YEAST:G3O-32186-MONOMER; -. 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 BioGRID-ORCS; 850712; 6 hits in 10 CRISPR screens. 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: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 Gene3D; 6.10.250.1710; -; 1. DR Gene3D; 1.10.287.1060; ESAT-6-like; 1. DR InterPro; IPR005024; Snf7_fam. DR PANTHER; PTHR22761; CHARGED MULTIVESICULAR BODY PROTEIN; 1. DR PANTHER; PTHR22761:SF10; GH13992P; 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 //