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Vacuolar-sorting protein SNF7 (DOA4-independent degradation protein 1) (Sucrose nonfermenting protein 7) (Vacuolar protein-sorting-associated protein 32)

 SNF7_YEAST              Reviewed;         240 AA.
P39929; D6VY27; E9P8V6;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 163.
RecName: Full=Vacuolar-sorting protein SNF7 {ECO:0000305};
AltName: Full=DOA4-independent degradation protein 1 {ECO:0000303|PubMed:11029042};
AltName: Full=Sucrose nonfermenting protein 7 {ECO:0000303|PubMed:1752413};
AltName: Full=Vacuolar protein-sorting-associated protein 32 {ECO:0000303|PubMed:3062374};
Name=SNF7 {ECO:0000303|PubMed:1752413};
Synonyms=DID1 {ECO:0000303|PubMed:11029042},
VPS32 {ECO:0000303|PubMed:3062374};
OrderedLocusNames=YLR025W {ECO:0000312|SGD:S000004015};
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].
STRAIN=ATCC 204508 / S288c;
PubMed=8224817;
Tu J., Vallier L.G., Carlson M.;
"Molecular and genetic analysis of the SNF7 gene in Saccharomyces
cerevisiae.";
Genetics 135:17-23(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(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]
DISRUPTION PHENOTYPE.
PubMed=3062374; DOI=10.1128/MCB.8.11.4936;
Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.;
"Protein sorting in Saccharomyces cerevisiae: isolation of mutants
defective in the delivery and processing of multiple vacuolar
hydrolases.";
Mol. Cell. Biol. 8:4936-4948(1988).
[6]
IDENTIFICATION.
PubMed=1752413;
Vallier L.G., Carlson M.;
"New SNF genes, GAL11 and GRR1 affect SUC2 expression in Saccharomyces
cerevisiae.";
Genetics 129:675-684(1991).
[7]
FUNCTION.
PubMed=11029042; DOI=10.1091/mbc.11.10.3365;
Amerik A.Y., Nowak J., Swaminathan S., Hochstrasser M.;
"The Doa4 deubiquitinating enzyme is functionally linked to the
vacuolar protein-sorting and endocytic pathways.";
Mol. Biol. Cell 11:3365-3380(2000).
[8]
FUNCTION.
PubMed=11559748;
Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
"CHMP1 functions as a member of a newly defined family of vesicle
trafficking proteins.";
J. Cell Sci. 114:2395-2404(2001).
[9]
FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH
VPS20, AND SUBCELLULAR LOCATION.
PubMed=12194857; DOI=10.1016/S1534-5807(02)00220-4;
Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D.;
"Escrt-III: an endosome-associated heterooligomeric protein complex
required for mvb sorting.";
Dev. Cell 3:271-282(2002).
[10]
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).
[11]
INTERACTION WITH BRO1.
PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x;
Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P.,
Stevens T.H.;
"Protein-protein interactions of ESCRT complexes in the yeast
Saccharomyces cerevisiae.";
Traffic 5:194-210(2004).
[12]
INTERACTION WITH BRO1, AND FUNCTION.
PubMed=15935782; DOI=10.1016/j.devcel.2005.04.001;
Kim J., Sitaraman S., Hierro A., Beach B.M., Odorizzi G., Hurley J.H.;
"Structural basis for endosomal targeting by the Bro1 domain.";
Dev. Cell 8:937-947(2005).
[13]
INTERACTION WITH VTA1.
PubMed=16601096; DOI=10.1073/pnas.0601712103;
Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H.;
"Vta1p and Vps46p regulate the membrane association and ATPase
activity of Vps4p at the yeast multivesicular body.";
Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[16]
ASSEMBLY OF THE ESCRT-III COMPLEX.
PubMed=18854142; DOI=10.1016/j.devcel.2008.08.013;
Teis D., Saksena S., Emr S.D.;
"Ordered assembly of the ESCRT-III complex on endosomes is required to
sequester cargo during MVB formation.";
Dev. Cell 15:578-589(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-193, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
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).
[19]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-229, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[20]
FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-2;
PHE-6 AND TRP-8.
PubMed=24139821; DOI=10.1016/j.devcel.2013.09.009;
Buchkovich N.J., Henne W.M., Tang S., Emr S.D.;
"Essential N-terminal insertion motif anchors the ESCRT-III filament
during MVB vesicle formation.";
Dev. Cell 27:201-214(2013).
[21]
INTERACTION WITH BRO1; RIM20; VPS20; VPS24; VPS4; VTA1 AND YGR122W.
PubMed=24058170; DOI=10.1128/EC.00241-13;
Sciskala B., Koelling R.;
"Interaction maps of the Saccharomyces cerevisiae ESCRT-III protein
Snf7.";
Eukaryot. Cell 12:1538-1546(2013).
[22]
INTERACTION WITH VPS4, AND FUNCTION OF THE ESCRT-III COMPLEX.
PubMed=24711499; DOI=10.1083/jcb.201310114;
Adell M.A., Vogel G.F., Pakdel M., Mueller M., Lindner H., Hess M.W.,
Teis D.;
"Coordinated binding of Vps4 to ESCRT-III drives membrane neck
constriction during MVB vesicle formation.";
J. Cell Biol. 205:33-49(2014).
[23]
FUNCTION, INTERACTION WITH HEH1 AND HEH2, AND SUBCELLULAR LOCATION.
PubMed=25303532; DOI=10.1016/j.cell.2014.09.012;
Webster B.M., Colombi P., Jaeger J., Lusk C.P.;
"Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4.";
Cell 159:388-401(2014).
[24]
INTERACTION WITH DOA4.
PubMed=26427873; DOI=10.1016/j.bbrc.2015.09.136;
Wolters N., Amerik A.;
"The N-terminal domains determine cellular localization and functions
of the Doa4 and Ubp5 deubiquitinating enzymes.";
Biochem. Biophys. Res. Commun. 467:570-576(2015).
[25]
FUNCTION, SUBUNIT, AND ELECTRON MICROSCOPY.
PubMed=26522593; DOI=10.1016/j.cell.2015.10.017;
Chiaruttini N., Redondo-Morata L., Colom A., Humbert F., Lenz M.,
Scheuring S., Roux A.;
"Relaxation of loaded ESCRT-III spiral springs drives membrane
deformation.";
Cell 163:866-879(2015).
[26]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 12-150, MUTAGENESIS OF
ARG-25; HIS-29; LYS-36; ARG-52; THR-83; MET-87; GLN-90; ILE-94;
GLU-95; ALA-97; LEU-99; LEU-101; GLU-102; THR-103; MET-104; MET-107;
GLU-109; MET-114; ILE-117 AND LEU-121, AND FUNCTION.
PubMed=26670543; DOI=10.7554/eLife.12548;
Tang S., Henne W.M., Borbat P.P., Buchkovich N.J., Freed J.H., Mao Y.,
Fromme J.C., Emr S.D.;
"Structural basis for activation, assembly and membrane binding of
ESCRT-III Snf7 filaments.";
Elife 4:0-0(2015).
-!- FUNCTION: Acts a component of the ESCRT-III complex required for
the sorting and concentration of proteins resulting in the entry
of these proteins into the invaginating vesicles of the
multivesicular body (MVB) (PubMed:11559748, PubMed:12194857). The
sequential action of ESCRT-0, -I, and -II together with the
ordered assembly of ESCRT-III links membrane invagination to cargo
sorting (PubMed:12194857). Membrane scission in the neck of the
growing vesicle releases mature, cargo-laden ILVs into the lumen
(PubMed:24139821, PubMed:24711499). ESCRT-III is critical for late
steps in MVB sorting, such as membrane invagination and final
cargo sorting and recruitment of late-acting components of the
sorting machinery (PubMed:24139821, PubMed:24711499). SNF7 is the
most abundant ESCRT-III subunit which forms membrane-sculpting
filaments with 30 Angstrom periodicity and a exposed cationic
membrane-binding surface (PubMed:26670543). Its activation
requires a prominent conformational rearrangement to expose
protein-membrane and protein-protein interfaces (PubMed:26670543).
SNF7 filaments then form spirals that could function as spiral
springs (PubMed:26522593). The elastic expansion of compressed
SNF7 spirals generates an area difference between the two sides of
the membrane and thus curvature which could be the origin of
membrane deformation leading eventually to fission
(PubMed:26522593). SNF7 recruits BRO1, which in turn recruits
DOA4, which deubiquitinates cargos before their enclosure within
MVB vesicles (PubMed:11029042, PubMed:15935782). ESCRT-III is also
recruited to the nuclear envelope (NE) by integral INM proteins to
surveil and clear defective nuclear pore complex (NPC) assembly
intermediates to ensure the fidelity of NPC assembly
(PubMed:25303532). {ECO:0000269|PubMed:11559748,
ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:15935782,
ECO:0000269|PubMed:24139821, ECO:0000269|PubMed:24711499,
ECO:0000269|PubMed:25303532, ECO:0000269|PubMed:26522593,
ECO:0000269|PubMed:3062374}.
-!- SUBUNIT: Core component of the ESCRT-III complex (endosomal
sorting required for transport complex III) (PubMed:12194857,
PubMed:18854142). ESCRT-III appears to be sequentially assembled
as a flat lattice on the endosome membrane and forms a transient
450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and
VPS24 (PubMed:18854142). SNF7 polymerizes into spirals at the
surface of lipid bilayers (PubMed:26522593). SNF7 polymerization
is nucleated by association of SNF7 with VPS20; the process is
terminated through association of VPS24, possibly by capping the
SNF7 filament (PubMed:24058170, PubMed:24711499). Interacts with
VTA1; the interaction requires DID2 (PubMed:16601096,
PubMed:24058170). Interacts with BRO1 (PubMed:15086794,
PubMed:15935782, PubMed:24058170). Interacts with DOA4
(PubMed:26427873). Interacts with HEH1 and HEH2 (PubMed:25303532).
Interacts with RIM20 and YGR122W (PubMed:24058170).
{ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:15086794,
ECO:0000269|PubMed:15935782, ECO:0000269|PubMed:16601096,
ECO:0000269|PubMed:18854142, ECO:0000269|PubMed:24058170,
ECO:0000269|PubMed:24711499, ECO:0000269|PubMed:25303532,
ECO:0000269|PubMed:26427873, ECO:0000269|PubMed:26522593}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-17554, EBI-17554;
P48582:BRO1; NbExp=3; IntAct=EBI-17554, EBI-3768;
P36108:DID4; NbExp=4; IntAct=EBI-17554, EBI-26574;
Q03281:HEH2; NbExp=3; IntAct=EBI-17554, EBI-22131;
Q04272:VPS20; NbExp=5; IntAct=EBI-17554, EBI-28157;
Q06263:VTA1; NbExp=2; IntAct=EBI-17554, EBI-37098;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12194857}.
Endosome membrane {ECO:0000269|PubMed:12194857,
ECO:0000269|PubMed:24139821}; Peripheral membrane protein
{ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821}.
Nucleus envelope {ECO:0000269|PubMed:25303532}.
-!- DOMAIN: The N-terminus (residues 1 to 11) forms an amphipatic
helix which is required for the association to membrane.
{ECO:0000269|PubMed:24139821}.
-!- DISRUPTION PHENOTYPE: Exhibits defects in the sorting and
processing of native vacuolar proteins (PubMed:3062374).
{ECO:0000269|PubMed:3062374}.
-!- MISCELLANEOUS: Present with 3270 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be a nuclear protein and
mutations were shown to prevent full derepression of the SUC2
(invertase) gene. {ECO:0000305|PubMed:8224817}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=On releasing tension
- Issue 180 of June 2016;
URL="http://web.expasy.org/spotlight/back_issues/180/";
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EMBL; L09751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z73197; CAA97548.1; -; Genomic_DNA.
EMBL; AY558202; AAS56528.1; -; Genomic_DNA.
EMBL; BK006945; DAA09343.1; -; Genomic_DNA.
PIR; S52590; S52590.
RefSeq; NP_013125.1; NM_001181912.1.
PDB; 5FD7; X-ray; 2.40 A; A=12-150.
PDB; 5FD9; X-ray; 1.60 A; A=12-150.
PDB; 5T8L; X-ray; 2.20 A; A=12-150.
PDB; 5T8N; X-ray; 2.20 A; A=12-150.
PDBsum; 5FD7; -.
PDBsum; 5FD9; -.
PDBsum; 5T8L; -.
PDBsum; 5T8N; -.
ProteinModelPortal; P39929; -.
SMR; P39929; -.
BioGrid; 31299; 139.
DIP; DIP-1747N; -.
IntAct; P39929; 26.
MINT; MINT-389266; -.
STRING; 4932.YLR025W; -.
iPTMnet; P39929; -.
MaxQB; P39929; -.
PRIDE; P39929; -.
EnsemblFungi; YLR025W; YLR025W; YLR025W.
GeneID; 850712; -.
KEGG; sce:YLR025W; -.
EuPathDB; FungiDB:YLR025W; -.
SGD; S000004015; SNF7.
GeneTree; ENSGT00390000005006; -.
HOGENOM; HOG000209960; -.
InParanoid; P39929; -.
KO; K12194; -.
OMA; MQVNTLE; -.
OrthoDB; EOG092C50TH; -.
BioCyc; YEAST:G3O-32186-MONOMER; -.
Reactome; R-SCE-1632852; Macroautophagy.
PRO; PR:P39929; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0000815; C:ESCRT III complex; IDA:SGD.
GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:1904669; P:ATP export; IMP:SGD.
GO; GO:0071454; P:cellular response to anoxia; IMP:SGD.
GO; GO:0070676; P:intralumenal vesicle formation; IMP:SGD.
GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:SGD.
InterPro; IPR005024; Snf7_fam.
Pfam; PF03357; Snf7; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Endosome; Isopeptide bond;
Membrane; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Transport; Ubl conjugation.
CHAIN 1 240 Vacuolar-sorting protein SNF7.
/FTId=PRO_0000211446.
COMPBIAS 68 71 Poly-Lys.
COMPBIAS 216 228 Asp/Glu-rich (acidic).
MOD_RES 72 72 Phosphothreonine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CROSSLNK 229 229 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 2 2 W->E: Impairs binding to membrane.
{ECO:0000269|PubMed:24139821}.
MUTAGEN 6 6 F->E: Impairs binding to membrane.
{ECO:0000269|PubMed:24139821}.
MUTAGEN 8 8 W->E: Impairs binding to membrane.
{ECO:0000269|PubMed:24139821}.
MUTAGEN 25 25 R->E: Leads to severe sorting defects;
when associated with E-29 and E-36.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 29 29 H->E: Leads to severe sorting defects;
when associated with E-25 and E-36.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 36 36 K->E: Leads to severe sorting defects;
when associated with E-25 and E-29.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 52 52 R->E: Impairs the formation of
protofilaments; when associated with K-
90. Also impairs the formation of
protofilaments; when associated with E-
94. Also impairs the formation of
protofilaments; when associated with E-
107. Also impairs the formation of
protofilaments; when associated with E-
114. {ECO:0000269|PubMed:26670543}.
MUTAGEN 83 83 T->E: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 87 87 M->E: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 90 90 Q->K: Leads to severe sorting defects.
Impairs the formation of protofilaments;
when associated with E-52.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 94 94 I->E: Leads to severe sorting defects.
Impairs the formation of protofilaments;
when associated with E-52.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 95 95 E->K: Leads to severe sorting defects;
when associated with K-102 and K-109.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 97 97 A->K: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 99 99 L->K: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 101 101 L->E: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 102 102 E->K: Leads to severe sorting defects;
when associated with K-95 and K-109.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 103 103 T->E: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 104 104 M->E: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 107 107 M->E: Leads to severe sorting defects.
Impairs the formation of protofilaments;
when associated with E-52.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 109 109 E->K: Leads to severe sorting defects;
when associated with K-95 and K-102.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 114 114 M->E: Leads to severe sorting defects.
Impairs the formation of protofilaments;
when associated with E-52.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 117 117 I->E: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
MUTAGEN 121 121 L->D: Leads to severe sorting defects.
{ECO:0000269|PubMed:26670543}.
CONFLICT 173 173 E -> G (in Ref. 4; AAS56528).
{ECO:0000305}.
HELIX 19 56 {ECO:0000244|PDB:5FD9}.
HELIX 60 118 {ECO:0000244|PDB:5FD9}.
TURN 120 122 {ECO:0000244|PDB:5FD7}.
HELIX 127 138 {ECO:0000244|PDB:5FD9}.
TURN 139 141 {ECO:0000244|PDB:5FD9}.
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


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