MSP1_YEAST
ID MSP1_YEAST Reviewed; 362 AA.
AC P28737; D6VUG3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Outer mitochondrial transmembrane helix translocase {ECO:0000305};
DE EC=7.4.2.- {ECO:0000269|PubMed:28712723, ECO:0000269|PubMed:28906250, ECO:0000269|PubMed:32541053};
DE AltName: Full=Mitochondrial sorting of proteins {ECO:0000303|PubMed:8226973};
DE AltName: Full=Tat-binding homolog 4 {ECO:0000303|PubMed:7754704};
GN Name=MSP1 {ECO:0000303|PubMed:8226973, ECO:0000312|SGD:S000003260};
GN Synonyms=YTA4 {ECO:0000303|PubMed:7754704}; OrderedLocusNames=YGR028W;
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], SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=SF747-19D;
RX PubMed=8226973; DOI=10.1016/s0021-9258(20)80519-5;
RA Nakai M., Endo T., Hase T., Matsubara H.;
RT "Intramitochondrial protein sorting. Isolation and characterization of the
RT yeast MSP1 gene which belongs to a novel family of putative ATPases.";
RL J. Biol. Chem. 268:24262-24269(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754704; DOI=10.1002/yea.320100903;
RA Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., Schwarzlose C.,
RA Vetter I., Feldmann H.;
RT "Identification of a set of yeast genes coding for a novel family of
RT putative ATPases with high similarity to constituents of the 26S protease
RT complex.";
RL Yeast 10:1141-1155(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-362.
RC STRAIN=SC167;
RX PubMed=1552903; DOI=10.1007/bf00299137;
RA Lisowsky T.;
RT "Dual function of a new nuclear gene for oxidative phosphorylation and
RT vegetative growth in yeast.";
RL Mol. Gen. Genet. 232:58-64(1992).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24843043; DOI=10.15252/embj.201487943;
RA Chen Y.C., Umanah G.K., Dephoure N., Andrabi S.A., Gygi S.P., Dawson T.M.,
RA Dawson V.L., Rutter J.;
RT "Msp1/ATAD1 maintains mitochondrial function by facilitating the
RT degradation of mislocalized tail-anchored proteins.";
RL EMBO J. 33:1548-1564(2014).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24821790; DOI=10.1073/pnas.1405755111;
RA Okreglak V., Walter P.;
RT "The conserved AAA-ATPase Msp1 confers organelle specificity to tail-
RT anchored proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8019-8024(2014).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH PEX3,
RP AND ACTIVITY REGULATION.
RX PubMed=28906250; DOI=10.7554/elife.28507;
RA Weir N.R., Kamber R.A., Martenson J.S., Denic V.;
RT "The AAA protein Msp1 mediates clearance of excess tail-anchored proteins
RT from the peroxisomal membrane.";
RL Elife 6:0-0(2017).
RN [12]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-12; LEU-69; TYR-72; GLU-73;
RP LEU-77; VAL-81; ILE-86; ILE-93; GLY-94; GLY-95; LEU-96; 122-LEU-LEU-123 AND
RP GLU-193.
RX PubMed=30858337; DOI=10.15252/embr.201846989;
RA Li L., Zheng J., Wu X., Jiang H.;
RT "Mitochondrial AAA-ATPase Msp1 detects mislocalized tail-anchored proteins
RT through a dual-recognition mechanism.";
RL EMBO Rep. 20:0-0(2019).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 122-LEU-LEU-123; LYS-139
RP AND GLU-193.
RX PubMed=31445887; DOI=10.1016/j.molcel.2019.07.006;
RA Matsumoto S., Nakatsukasa K., Kakuta C., Tamura Y., Esaki M., Endo T.;
RT "Msp1 clears mistargeted proteins by facilitating their transfer from
RT mitochondria to the ER.";
RL Mol. Cell 76:191-205(2019).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION, INTERACTION
RP WITH PEX3, AND MUTAGENESIS OF 166-TRP-TYR-167 AND GLU-193.
RX PubMed=32541053; DOI=10.1073/pnas.1920109117;
RA Castanzo D.T., LaFrance B., Martin A.;
RT "The AAA+ ATPase Msp1 is a processive protein translocase with robust
RT unfoldase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:14970-14977(2020).
RN [15] {ECO:0007744|PDB:5W0T}
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 51-345, FUNCTION, TOPOLOGY,
RP CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF 122-LEU-LEU-123;
RP 166-TRP-TYR-167; GLU-193 AND 206-HIS-GLU-207.
RX PubMed=28712723; DOI=10.1016/j.molcel.2017.06.019;
RA Wohlever M.L., Mateja A., McGilvray P.T., Day K.J., Keenan R.J.;
RT "Msp1 is a membrane protein dislocase for tail-anchored proteins.";
RL Mol. Cell 67:194-202(2017).
CC -!- FUNCTION: Outer mitochondrial translocase required to remove
CC mislocalized tail-anchored transmembrane proteins on mitochondria
CC (PubMed:24843043, PubMed:24821790, PubMed:28906250, PubMed:30858337,
CC PubMed:31445887, PubMed:28712723). Specifically recognizes and binds
CC exposed hydrophobic surfaces of mistargeted tail-anchored transmembrane
CC proteins (PubMed:30858337). Acts as a dislocase that mediates the ATP-
CC dependent extraction of mistargeted tail-anchored transmembrane
CC proteins from the mitochondrion outer membrane (PubMed:24843043,
CC PubMed:24821790, PubMed:28906250, PubMed:30858337, PubMed:32541053,
CC PubMed:28712723). Able to unfold protein substrates by processive
CC threading through its central pore (PubMed:32541053). Once extracted
CC from the mitochondrion outer membrane, substrate proteins are then
CC transferred to the endoplasmic reticulum, where they are ubiquitinated
CC and degraded by the proteasome (PubMed:31445887). Also mediates
CC extraction of excess tail-anchored proteins from the peroxisomal
CC membrane (PubMed:28906250). In normal conditions, MSP1 translocase
CC activity is inhibited by PEX3 at peroxisomes; only catalyzes removal of
CC excess tail-anchored proteins (PubMed:28906250).
CC {ECO:0000269|PubMed:24821790, ECO:0000269|PubMed:24843043,
CC ECO:0000269|PubMed:28712723, ECO:0000269|PubMed:28906250,
CC ECO:0000269|PubMed:30858337, ECO:0000269|PubMed:31445887,
CC ECO:0000269|PubMed:32541053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O =
CC [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:28712723, ECO:0000269|PubMed:28906250,
CC ECO:0000269|PubMed:32541053};
CC -!- ACTIVITY REGULATION: Interaction with PEX3 inhibits the translocase
CC activity by preventing unfolding of target proteins.
CC {ECO:0000269|PubMed:32541053}.
CC -!- SUBUNIT: Homohexamer; in presence of ATP (PubMed:30858337,
CC PubMed:32541053, PubMed:28712723). Interacts with PEX3; leading to
CC inhibit the translocase activity (PubMed:28906250, PubMed:32541053).
CC {ECO:0000269|PubMed:28712723, ECO:0000269|PubMed:28906250,
CC ECO:0000269|PubMed:30858337, ECO:0000269|PubMed:32541053}.
CC -!- INTERACTION:
CC P28737; Q12421: ATG31; NbExp=3; IntAct=EBI-11435, EBI-34768;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:24843043, ECO:0000269|PubMed:28906250,
CC ECO:0000269|PubMed:31445887, ECO:0000269|PubMed:8226973,
CC ECO:0000305|PubMed:24821790}; Single-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24821790,
CC ECO:0000269|PubMed:24843043, ECO:0000269|PubMed:28906250}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impaired transmembrane tail-anchored protein
CC localization, characterized by mislocalization of PEX15 to the
CC mitochondrion outer membrane. {ECO:0000269|PubMed:24821790}.
CC -!- MISCELLANEOUS: Present with 3530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X68055; CAA48191.1; -; Genomic_DNA.
DR EMBL; X81069; CAA56956.1; -; Genomic_DNA.
DR EMBL; Z72813; CAA97015.1; -; Genomic_DNA.
DR EMBL; X60722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY557772; AAS56098.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08124.1; -; Genomic_DNA.
DR PIR; A49506; A49506.
DR RefSeq; NP_011542.3; NM_001181157.3.
DR PDB; 5W0T; X-ray; 2.63 A; A=51-345.
DR PDBsum; 5W0T; -.
DR AlphaFoldDB; P28737; -.
DR SMR; P28737; -.
DR BioGRID; 33272; 104.
DR DIP; DIP-8029N; -.
DR IntAct; P28737; 22.
DR MINT; P28737; -.
DR STRING; 4932.YGR028W; -.
DR iPTMnet; P28737; -.
DR MaxQB; P28737; -.
DR PaxDb; P28737; -.
DR PRIDE; P28737; -.
DR DNASU; 852915; -.
DR EnsemblFungi; YGR028W_mRNA; YGR028W; YGR028W.
DR GeneID; 852915; -.
DR KEGG; sce:YGR028W; -.
DR SGD; S000003260; MSP1.
DR VEuPathDB; FungiDB:YGR028W; -.
DR eggNOG; KOG0737; Eukaryota.
DR GeneTree; ENSGT00940000166329; -.
DR HOGENOM; CLU_000688_21_14_1; -.
DR InParanoid; P28737; -.
DR OMA; GPRWQQF; -.
DR BioCyc; YEAST:G3O-30752-MON; -.
DR Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:P28737; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P28737; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:SGD.
DR GO; GO:0140567; F:transmembrane protein dislocase activity; IDA:UniProtKB.
DR GO; GO:0140570; P:extraction of mislocalized protein from mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..362
FT /note="Outer mitochondrial transmembrane helix translocase"
FT /id="PRO_0000084757"
FT TOPO_DOM 1..12
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:28712723,
FT ECO:0000305|PubMed:8226973"
FT TRANSMEM 13..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28712723,
FT ECO:0000305|PubMed:8226973"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 12
FT /note="D->T: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 69
FT /note="L->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 72
FT /note="Y->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Impaired formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 73
FT /note="E->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 77
FT /note="L->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 81
FT /note="V->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 86
FT /note="I->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 93
FT /note="I->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 94
FT /note="G->A: Does not impair ability to extract tail-
FT anchored proteins from membranes. Does not affect formation
FT of a homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 95
FT /note="G->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 96
FT /note="L->A: Impaired ability to extract tail-anchored
FT proteins from membranes. Does not affect formation of a
FT homohexamer."
FT /evidence="ECO:0000269|PubMed:30858337"
FT MUTAGEN 122..123
FT /note="LL->DD: Impaired formation of a homohexamer.
FT Impaired ability to extract tail-anchored proteins from
FT membranes."
FT /evidence="ECO:0000269|PubMed:28712723,
FT ECO:0000269|PubMed:30858337, ECO:0000269|PubMed:31445887"
FT MUTAGEN 139
FT /note="K->A: Impaired ability to extract tail-anchored
FT proteins from membranes."
FT /evidence="ECO:0000269|PubMed:31445887"
FT MUTAGEN 166..167
FT /note="WY->AA: Abolished translocase activity,
FT characterized by impaired ability to unfold and extract
FT tail-anchored proteins from membranes."
FT /evidence="ECO:0000269|PubMed:28712723,
FT ECO:0000269|PubMed:32541053"
FT MUTAGEN 193
FT /note="E->Q: Loss of ATPase activity. Does not affect
FT formation of a homohexamer."
FT /evidence="ECO:0000269|PubMed:28712723,
FT ECO:0000269|PubMed:30858337, ECO:0000269|PubMed:31445887,
FT ECO:0000269|PubMed:32541053"
FT MUTAGEN 206..207
FT /note="HE->AA: Abolished translocase activity,
FT characterized by impaired ability to extract tail-anchored
FT proteins from membranes."
FT /evidence="ECO:0000269|PubMed:28712723"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:5W0T"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5W0T"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:5W0T"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:5W0T"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:5W0T"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:5W0T"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:5W0T"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:5W0T"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:5W0T"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 295..322
FT /evidence="ECO:0007829|PDB:5W0T"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:5W0T"
SQ SEQUENCE 362 AA; 40343 MW; 1B3562A32F47F434 CRC64;
MSRKFDLKTI TDLSVLVGTG ISLYYLVSRL LNDVESGPLS GKSRESKAKQ SLQWEKLVKR
SPALAEVTLD AYERTILSSI VTPDEINITF QDIGGLDPLI SDLHESVIYP LMMPEVYSNS
PLLQAPSGVL LYGPPGCGKT MLAKALAKES GANFISIRMS SIMDKWYGES NKIVDAMFSL
ANKLQPCIIF IDEIDSFLRE RSSTDHEVTA TLKAEFMTLW DGLLNNGRVM IIGATNRIND
IDDAFLRRLP KRFLVSLPGS DQRYKILSVL LKDTKLDEDE FDLQLIADNT KGFSGSDLKE
LCREAALDAA KEYIKQKRQL IDSGTIDVND TSSLKIRPLK TKDFTKKLRM DATSTLSSQP
LD
