VPS4_YEAST
ID VPS4_YEAST Reviewed; 437 AA.
AC P52917; D6W4H4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Vacuolar protein sorting-associated protein 4;
DE AltName: Full=DOA4-independent degradation protein 6;
DE AltName: Full=Protein END13;
DE AltName: Full=Vacuolar protein-targeting protein 10;
GN Name=VPS4; Synonyms=CSC1, DID6, END13, GRD13, VPL4, VPT10;
GN OrderedLocusNames=YPR173C; ORFNames=P9705.10;
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], AND FUNCTION.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=11329380; DOI=10.1242/jcs.114.10.1935;
RA Zahn R., Stevenson B.J., Schroeder-Koehne S., Zanolari B., Riezman H.,
RA Munn A.L.;
RT "End13p/Vps4p is required for efficient transport from early to late
RT endosomes in Saccharomyces cerevisiae.";
RL J. Cell Sci. 114:1935-1947(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF LYS-179 AND
RP GLU-233.
RX PubMed=9155008; DOI=10.1093/emboj/16.8.1820;
RA Babst M., Sato T.K., Banta L.M., Emr S.D.;
RT "Endosomal transport function in yeast requires a novel AAA-type ATPase,
RT Vps4p.";
RL EMBO J. 16:1820-1831(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9606181; DOI=10.1093/emboj/17.11.2982;
RA Babst M., Wendland B., Estepa E.J., Emr S.D.;
RT "The Vps4p AAA ATPase regulates membrane association of a Vps protein
RT complex required for normal endosome function.";
RL EMBO J. 17:2982-2993(1998).
RN [6]
RP INTERACTION WITH VPS20 AND VTA1.
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 [7]
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 [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 INTERACTION WITH VTA1, AND OLIGOMERIZATION.
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 INTERACTION WITH DID2.
RX PubMed=17130288; DOI=10.1083/jcb.200606113;
RA Nickerson D.P., West M., Odorizzi G.;
RT "Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes.";
RL J. Cell Biol. 175:715-720(2006).
RN [11]
RP ERRATUM OF PUBMED:17130288.
RA Nickerson D.P., West M., Odorizzi G.;
RL J. Cell Biol. 175:1043-1043(2006).
RN [12]
RP INTERACTION WITH 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 [13]
RP IDENTIFICATION BY 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 [14]
RP MUTAGENESIS OF LEU-64.
RX PubMed=17928862; DOI=10.1038/nature06172;
RA Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A.,
RA Ghaffarian S., Sundquist W.I.;
RT "ESCRT-III recognition by VPS4 ATPases.";
RL Nature 449:740-744(2007).
RN [15]
RP INTERACTION WITH VTA1, AND SUBUNIT.
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 [16]
RP INTERACTION WITH IST1.
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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 83-437, OLIGOMERIZATION, AND
RP INTERACTION WITH VPS20 AND DID4.
RX PubMed=17949747; DOI=10.1016/j.jmb.2007.09.067;
RA Xiao J., Xia H., Yoshino-Koh K., Zhou J., Xu Z.;
RT "Structural characterization of the ATPase reaction cycle of endosomal AAA
RT protein Vps4.";
RL J. Mol. Biol. 374:655-670(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1-82 IN COMPLEX WITH DID4, AND
RP INTERACTION WITH DID2.
RX PubMed=17928861; DOI=10.1038/nature06171;
RA Obita T., Saksena S., Ghazi-Tabatabai S., Gill D.J., Perisic O., Emr S.D.,
RA Williams R.L.;
RT "Structural basis for selective recognition of ESCRT-III by the AAA ATPase
RT Vps4.";
RL Nature 449:735-739(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 116-437, OLIGOMERIZATION, AND
RP MUTAGENESIS OF GLN-216.
RX PubMed=18272179; DOI=10.1016/j.jmb.2008.01.010;
RA Hartmann C., Chami M., Zachariae U., de Groot B.L., Engel A., Grutter M.G.;
RT "Vacuolar protein sorting: two different functional states of the AAA-
RT ATPase Vps4p.";
RL J. Mol. Biol. 377:352-363(2008).
CC -!- FUNCTION: Involved in the transport of biosynthetic membrane proteins
CC from the prevacuolar/endosomal compartment to the vacuole. Required for
CC multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent
CC dissociation of class E VPS proteins from endosomal membranes, such as
CC the disassembly of the ESCRT-III complex. {ECO:0000269|PubMed:11329380,
CC ECO:0000269|PubMed:9155008, ECO:0000269|PubMed:9606181}.
CC -!- SUBUNIT: Monomer or homodimer (in nucleotide-free form). Decamer,
CC dodecamer or tetradecamer of two stacked respective homooligomeric
CC rings (when bound to ATP); the dodecameric form seems to be
CC predominant. Interacts with VPS20. Interacts with VTA1; the interaction
CC requires the dimeric structure of VTA1; 6 homodimers of VTA1 appear to
CC associate with the dodecameric VSP4 complex. Interacts with DID2.
CC Interacts with DID4. Interacts with IST1; IST1 competes with VTA1 for
CC binding with VPS4. {ECO:0000269|PubMed:12953057,
CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:16505166,
CC ECO:0000269|PubMed:16601096, ECO:0000269|PubMed:17130288,
CC ECO:0000269|PubMed:17928861, ECO:0000269|PubMed:17949747,
CC ECO:0000269|PubMed:18032584, ECO:0000269|PubMed:18280501,
CC ECO:0000269|PubMed:9606181}.
CC -!- INTERACTION:
CC P52917; P69771: DID2; NbExp=3; IntAct=EBI-20475, EBI-2053489;
CC P52917; P36108: DID4; NbExp=4; IntAct=EBI-20475, EBI-26574;
CC P52917; Q04272: VPS20; NbExp=6; IntAct=EBI-20475, EBI-28157;
CC P52917; P52917: VPS4; NbExp=3; IntAct=EBI-20475, EBI-20475;
CC P52917; Q06263: VTA1; NbExp=12; IntAct=EBI-20475, EBI-37098;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 5350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; X92680; CAA63364.1; -; Genomic_DNA.
DR EMBL; U25842; AAB68107.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11590.1; -; Genomic_DNA.
DR PIR; S59831; S59831.
DR RefSeq; NP_015499.1; NM_001184270.1.
DR PDB; 2QP9; X-ray; 2.90 A; X=83-437.
DR PDB; 2QPA; X-ray; 3.20 A; A/B/C=83-437.
DR PDB; 2RKO; X-ray; 3.35 A; A=124-437.
DR PDB; 2V6X; X-ray; 1.98 A; A=1-82.
DR PDB; 3EIE; X-ray; 2.70 A; A=122-437.
DR PDB; 3EIH; X-ray; 3.25 A; A/B/C=104-437.
DR PDB; 3MHV; X-ray; 3.10 A; C=299-413.
DR PDB; 4NIQ; X-ray; 2.30 A; A/B=1-82.
DR PDB; 5FVK; X-ray; 1.66 A; A/B=1-82.
DR PDB; 5FVL; X-ray; 1.97 A; A/B=1-82.
DR PDB; 5UIE; EM; 5.70 A; A/B/C/D/E/F=1-437.
DR PDB; 5XMI; EM; 3.90 A; A/B/C/D/E/F=1-437.
DR PDB; 5XMK; EM; 4.18 A; A/B/C/D/E/F=1-437.
DR PDB; 6AP1; EM; 3.20 A; A/B/C/D/E/F=101-437.
DR PDB; 6BMF; EM; 3.20 A; A/B/C/D/E=101-437.
DR PDB; 6NDY; EM; 3.60 A; A/B/C/D/E=101-437.
DR PDB; 6OO2; EM; 4.40 A; A/B/C/D/E/F=101-437.
DR PDBsum; 2QP9; -.
DR PDBsum; 2QPA; -.
DR PDBsum; 2RKO; -.
DR PDBsum; 2V6X; -.
DR PDBsum; 3EIE; -.
DR PDBsum; 3EIH; -.
DR PDBsum; 3MHV; -.
DR PDBsum; 4NIQ; -.
DR PDBsum; 5FVK; -.
DR PDBsum; 5FVL; -.
DR PDBsum; 5UIE; -.
DR PDBsum; 5XMI; -.
DR PDBsum; 5XMK; -.
DR PDBsum; 6AP1; -.
DR PDBsum; 6BMF; -.
DR PDBsum; 6NDY; -.
DR PDBsum; 6OO2; -.
DR AlphaFoldDB; P52917; -.
DR SMR; P52917; -.
DR BioGRID; 36346; 672.
DR ComplexPortal; CPX-334; VPS4 complex.
DR DIP; DIP-1746N; -.
DR IntAct; P52917; 19.
DR MINT; P52917; -.
DR STRING; 4932.YPR173C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P52917; -.
DR MaxQB; P52917; -.
DR PaxDb; P52917; -.
DR PRIDE; P52917; -.
DR DNASU; 856303; -.
DR EnsemblFungi; YPR173C_mRNA; YPR173C; YPR173C.
DR GeneID; 856303; -.
DR KEGG; sce:YPR173C; -.
DR SGD; S000006377; VPS4.
DR VEuPathDB; FungiDB:YPR173C; -.
DR eggNOG; KOG0739; Eukaryota.
DR GeneTree; ENSGT00940000154973; -.
DR HOGENOM; CLU_000688_21_2_1; -.
DR InParanoid; P52917; -.
DR OMA; MFELNVG; -.
DR BioCyc; YEAST:G3O-34300-MON; -.
DR BRENDA; 3.6.4.6; 984.
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 EvolutionaryTrace; P52917; -.
DR PRO; PR:P52917; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P52917; protein.
DR GO; GO:1904949; C:ATPase complex; IMP:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:1990621; C:ESCRT IV complex; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0030496; C:midbody; IC:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0070676; P:intralumenal vesicle formation; IMP:SGD.
DR GO; GO:0061764; P:late endosome to lysosome transport via multivesicular body sorting pathway; IMP:ComplexPortal.
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; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0090148; P:membrane fission; IMP:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; IC:ComplexPortal.
DR GO; GO:0036258; P:multivesicular body assembly; IMP:ComplexPortal.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:ComplexPortal.
DR GO; GO:0031468; P:nuclear membrane reassembly; IC:ComplexPortal.
DR GO; GO:0006997; P:nucleus organization; IC:ComplexPortal.
DR GO; GO:0001778; P:plasma membrane repair; IC:ComplexPortal.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IDA:SGD.
DR GO; GO:0016125; P:sterol metabolic process; IMP:SGD.
DR GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR CDD; cd02678; MIT_VPS4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR InterPro; IPR045253; VPS4_MIT.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endosome; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..437
FT /note="Vacuolar protein sorting-associated protein 4"
FT /id="PRO_0000084760"
FT DOMAIN 3..80
FT /note="MIT"
FT REGION 74..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 64
FT /note="L->D: Inhibits membrane protein sorting to the
FT vacuole."
FT /evidence="ECO:0000269|PubMed:17928862"
FT MUTAGEN 179
FT /note="K->A: No ATP hydrolysis. Missorting of vacuolar
FT proteins."
FT /evidence="ECO:0000269|PubMed:9155008"
FT MUTAGEN 216
FT /note="Q->A: Abolishes oligomerization."
FT /evidence="ECO:0000269|PubMed:18272179"
FT MUTAGEN 233
FT /note="E->Q: Defective in ATP hydrolysis. Missorting of
FT vacuolar proteins."
FT /evidence="ECO:0000269|PubMed:9155008"
FT CONFLICT 32
FT /note="A -> S (in Ref. 1; CAA63364)"
FT /evidence="ECO:0000305"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:5FVK"
FT HELIX 26..46
FT /evidence="ECO:0007829|PDB:5FVK"
FT HELIX 50..81
FT /evidence="ECO:0007829|PDB:5FVK"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:6AP1"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:3EIE"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6AP1"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6AP1"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2RKO"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:3EIE"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3MHV"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:2QP9"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:3EIE"
FT HELIX 421..432
FT /evidence="ECO:0007829|PDB:3EIE"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3EIH"
SQ SEQUENCE 437 AA; 48172 MW; E65BCDB19C9510DD CRC64;
MSTGDFLTKG IELVQKAIDL DTATQYEEAY TAYYNGLDYL MLALKYEKNP KSKDLIRAKF
TEYLNRAEQL KKHLESEEAN AAKKSPSAGS GSNGGNKKIS QEEGEDNGGE DNKKLRGALS
SAILSEKPNV KWEDVAGLEG AKEALKEAVI LPVKFPHLFK GNRKPTSGIL LYGPPGTGKS
YLAKAVATEA NSTFFSVSSS DLVSKWMGES EKLVKQLFAM ARENKPSIIF IDEVDALTGT
RGEGESEASR RIKTELLVQM NGVGNDSQGV LVLGATNIPW QLDSAIRRRF ERRIYIPLPD
LAARTTMFEI NVGDTPCVLT KEDYRTLGAM TEGYSGSDIA VVVKDALMQP IRKIQSATHF
KDVSTEDDET RKLTPCSPGD DGAIEMSWTD IEADELKEPD LTIKDFLKAI KSTRPTVNED
DLLKQEQFTR DFGQEGN
