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Database: UniProt
Entry: P46675
LinkDB: P46675
Original site: P46675 
ID   STU2_YEAST              Reviewed;         888 AA.
AC   P46675; D6VY47;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   07-OCT-2020, entry version 169.
DE   RecName: Full=Protein STU2;
DE   AltName: Full=Suppressor of tubulin 2;
GN   Name=STU2; OrderedLocusNames=YLR045C; ORFNames=L2108;
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 TUBULIN-BINDING.
RC   STRAIN=CUY696;
RX   PubMed=9382872; DOI=10.1083/jcb.139.5.1271;
RA   Wang P.J., Huffaker T.C.;
RT   "Stu2p: a microtubule-binding protein that is an essential component of the
RT   yeast spindle pole body.";
RL   J. Cell Biol. 139:1271-1280(1997).
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   INTERACTION WITH SPC72.
RX   PubMed=9606209; DOI=10.1083/jcb.141.5.1169;
RA   Chen X.P., Yin H., Huffaker T.C.;
RT   "The yeast spindle pole body component Spc72p interacts with Stu2p and is
RT   required for proper microtubule assembly.";
RL   J. Cell Biol. 141:1169-1179(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=11309422; DOI=10.1083/jcb.153.2.435;
RA   Severin F., Habermann B., Huffaker T., Hyman T.;
RT   "Stu2 promotes mitotic spindle elongation in anaphase.";
RL   J. Cell Biol. 153:435-442(2001).
RN   [6]
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   [7]
RP   TUBULIN-BINDING, SUBUNIT, FUNCTION, AND COILED COIL DOMAIN.
RX   PubMed=16567500; DOI=10.1083/jcb.200511010;
RA   Al-Bassam J., van Breugel M., Harrison S.C., Hyman A.;
RT   "Stu2p binds tubulin and undergoes an open-to-closed conformational
RT   change.";
RL   J. Cell Biol. 172:1009-1022(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, 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   [9]
RP   IDENTIFICATION BY 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   [10]
RP   TUBULIN-BINDING, TOG DOMAIN, AND MUTAGENESIS OF TRP-23; ARG-116 AND
RP   LYS-151.
RX   PubMed=17355870; DOI=10.1016/j.str.2007.01.012;
RA   Al-Bassam J., Larsen N.A., Hyman A.A., Harrison S.C.;
RT   "Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-
RT   family TOG domains and implications for tubulin binding.";
RL   Structure 15:355-362(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP   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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-813, AND
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   [13]
RP   FUNCTION.
RX   PubMed=25172511; DOI=10.1074/jbc.m114.584300;
RA   Podolski M., Mahamdeh M., Howard J.;
RT   "Stu2, the budding yeast XMAP215/Dis1 homolog, promotes assembly of yeast
RT   microtubules by increasing growth rate and decreasing catastrophe
RT   frequency.";
RL   J. Biol. Chem. 289:28087-28093(2014).
RN   [14]
RP   FUNCTION, INTERACTION WITH THE NDC80 COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=27156448; DOI=10.1016/j.cell.2016.04.030;
RA   Miller M.P., Asbury C.L., Biggins S.;
RT   "A TOG protein confers tension sensitivity to kinetochore-microtubule
RT   attachments.";
RL   Cell 165:1428-1439(2016).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 317-560.
RX   PubMed=17889670; DOI=10.1016/j.molcel.2007.07.023;
RA   Slep K.C., Vale R.D.;
RT   "Structural basis of microtubule plus end tracking by XMAP215, CLIP-170,
RT   and EB1.";
RL   Mol. Cell 27:976-991(2007).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-272 IN COMPLEX WITH TUBULIN
RP   HETERODIMER, TOG DOMAIN, AND MUTAGENESIS OF TRP-23; VAL-69; ARG-200 AND
RP   ARG-519.
RX   PubMed=22904013; DOI=10.1126/science.1221698;
RA   Ayaz P., Ye X., Huddleston P., Brautigam C.A., Rice L.M.;
RT   "A TOG:alphabeta-tubulin complex structure reveals conformation-based
RT   mechanisms for a microtubule polymerase.";
RL   Science 337:857-860(2012).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 318-560 IN COMPLEX WITH TUBULIN
RP   HETERODIMER, FUNCTION, TOG DOMAIN, AND MUTAGENESIS OF ARG-200; TRP-341 AND
RP   ARG-519.
RX   PubMed=25097237; DOI=10.7554/elife.03069;
RA   Ayaz P., Munyoki S., Geyer E.A., Piedra F.A., Vu E.S., Bromberg R.,
RA   Otwinowski Z., Grishin N.V., Brautigam C.A., Rice L.M.;
RT   "A tethered delivery mechanism explains the catalytic action of a
RT   microtubule polymerase.";
RL   Elife 3:E03069-E03069(2014).
CC   -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC       microtubule dynamics and microtubule organization. May play a role in
CC       the attachment, organization, and/or dynamics of microtubule ends at
CC       the spindle pole body. Stabilizes both cytoplasmic and nuclear
CC       microtubules. Promotes mitotic spindle elongation in anaphase. Has
CC       microtubule polymerase activity by accelerating microtubule growth and
CC       inhibiting catastrophe. The polymerase activity is proposed to involve
CC       a tethering mechanism at the microtubule plus end: a curved,
CC       longitudinally microtubule lattice-associated tubulin heterodimer (that
CC       cannot be incorporated into the microtubule lattice) is bound via one
CC       TOG domain while the other TOG domain binds to an unpolymerized tubulin
CC       heterodimer leading to lateral association of these tubulin
CC       heterodimers; polymerization-induced straightening of the tubulin
CC       heterodimer releases the polymerase (PubMed:11309422, PubMed:25172511,
CC       PubMed:16567500, PubMed:25097237). Is involved in regulation of
CC       kinetochore-microtubule attachments in a tension-dependent manner
CC       involving its association with the NDC80 complex; the function may be
CC       independent of its microtubule polymerase activity. Can either
CC       stabilize or destabilize kinetochore attachments, depending on the
CC       level of kinetochore tension and whether the microtubule tip is
CC       assembling or disassembling (PubMed:27156448).
CC       {ECO:0000269|PubMed:11309422, ECO:0000269|PubMed:16567500,
CC       ECO:0000269|PubMed:25172511, ECO:0000269|PubMed:27156448,
CC       ECO:0000305|PubMed:25097237}.
CC   -!- SUBUNIT: Binds to microtubules. Homodimer; each monomer can bind via
CC       its TOG domains to two alpha/beta-tubulin heterodimers. Interacts with
CC       SPC72. Associates with the NDC80 complex. {ECO:0000269|PubMed:16567500,
CC       ECO:0000269|PubMed:22904013, ECO:0000269|PubMed:25097237,
CC       ECO:0000269|PubMed:27156448, ECO:0000269|PubMed:9606209}.
CC   -!- INTERACTION:
CC       P46675; P53267: DAM1; NbExp=3; IntAct=EBI-18471, EBI-23268;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:9382872}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000269|PubMed:9382872}. Chromosome,
CC       centromere, kinetochore {ECO:0000269|PubMed:27156448}. Note=Localizes
CC       primarily to the spindle pole body (SPB) and to a lesser extent along
CC       spindle microtubules. {ECO:0000269|PubMed:9382872}.
CC   -!- DOMAIN: The coiled coil domain mediates homodimerization.
CC       {ECO:0000269|PubMed:16567500}.
CC   -!- DOMAIN: The TOG (tumor overexpressed gene) domains are composed of six
CC       (for the most part non-canonical) HEAT repeats each. Intra-HEAT loops
CC       are positioned along a face of the TOG domain and bind to a single
CC       alpha/beta-tubulin heterodimer. Two sets of TOG domains may wrap around
CC       a single free tubulin heterodimer accompanied by a open-to-closed
CC       conformational change of the STU2 homodimer. Both, TOG 1 and TOG 2 bind
CC       curved alpha/beta-tubulin with comparable affinity; the two TOG domains
CC       bind noncooperatively to two tubulin heterodimers. Free unpolymerized
CC       tubulin-binding is predominantly mediated by TOG 1, association with
CC       the microtubules plus ends is mediated by TOG 2 in cooperation with a
CC       C-terminal basic domain. {ECO:0000269|PubMed:25097237,
CC       ECO:0000305|PubMed:16567500, ECO:0000305|PubMed:22904013}.
CC   -!- MISCELLANEOUS: Mutations in STU2 suppress a cold-sensitive mutation in
CC       TUB2.
CC   -!- MISCELLANEOUS: Present with 1660 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000305}.
DR   EMBL; U35247; AAA79057.1; -; Genomic_DNA.
DR   EMBL; X94607; CAA64292.1; -; Genomic_DNA.
DR   EMBL; Z73217; CAA97574.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09363.1; -; Genomic_DNA.
DR   PIR; S61619; S61619.
DR   RefSeq; NP_013146.1; NM_001181932.1.
DR   PDB; 2QK1; X-ray; 1.70 A; A=317-560.
DR   PDB; 4FFB; X-ray; 2.88 A; C=1-272.
DR   PDB; 4U3J; X-ray; 2.81 A; C=318-560.
DR   PDB; 6BL7; X-ray; 2.50 A; A/B=655-760.
DR   PDBsum; 2QK1; -.
DR   PDBsum; 4FFB; -.
DR   PDBsum; 4U3J; -.
DR   PDBsum; 6BL7; -.
DR   SMR; P46675; -.
DR   BioGRID; 31320; 607.
DR   DIP; DIP-2462N; -.
DR   IntAct; P46675; 45.
DR   MINT; P46675; -.
DR   STRING; 4932.YLR045C; -.
DR   iPTMnet; P46675; -.
DR   MaxQB; P46675; -.
DR   PaxDb; P46675; -.
DR   PRIDE; P46675; -.
DR   TopDownProteomics; P46675; -.
DR   EnsemblFungi; YLR045C_mRNA; YLR045C; YLR045C.
DR   GeneID; 850734; -.
DR   KEGG; sce:YLR045C; -.
DR   EuPathDB; FungiDB:YLR045C; -.
DR   SGD; S000004035; STU2.
DR   eggNOG; KOG1820; Eukaryota.
DR   GeneTree; ENSGT00390000014757; -.
DR   HOGENOM; CLU_008401_1_1_1; -.
DR   InParanoid; P46675; -.
DR   KO; K16803; -.
DR   OMA; LCAFLKY; -.
DR   EvolutionaryTrace; P46675; -.
DR   PRO; PR:P46675; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P46675; protein.
DR   GO; GO:0005938; C:cell cortex; IDA:SGD.
DR   GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IDA:SGD.
DR   GO; GO:0000776; C:kinetochore; IDA:SGD.
DR   GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR   GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR   GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR   GO; GO:0008017; F:microtubule binding; IMP:SGD.
DR   GO; GO:0061863; F:microtubule plus end polymerase; IBA:GO_Central.
DR   GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IBA:GO_Central.
DR   GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IGI:SGD.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR034085; TOG.
DR   SMART; SM01349; TOG; 2.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Centromere; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Kinetochore; Microtubule; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..888
FT                   /note="Protein STU2"
FT                   /id="PRO_0000072295"
FT   REPEAT          51..88
FT                   /note="HEAT 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          175..216
FT                   /note="HEAT 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          411..448
FT                   /note="HEAT 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          453..490
FT                   /note="HEAT 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          503..541
FT                   /note="HEAT 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT   REGION          8..280
FT                   /note="TOG 1"
FT                   /evidence="ECO:0000305|PubMed:16567500"
FT   REGION          326..550
FT                   /note="TOG 1"
FT                   /evidence="ECO:0000305|PubMed:16567500"
FT   COILED          654..762
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18407956"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19779198"
FT   MOD_RES         813
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17330950,
FT                   ECO:0000244|PubMed:19779198"
FT   MUTAGEN         23
FT                   /note="W->A: Disrupts interaction with tubulin heterodimer.
FT                   Impairs polymerase activity under microtubule stress."
FT                   /evidence="ECO:0000269|PubMed:17355870,
FT                   ECO:0000269|PubMed:22904013"
FT   MUTAGEN         69
FT                   /note="V->D: Impairs polymerase activity under microtubule
FT                   stress."
FT                   /evidence="ECO:0000269|PubMed:22904013"
FT   MUTAGEN         116
FT                   /note="R->A: Decreases interaction with tubulin
FT                   heterodimer."
FT                   /evidence="ECO:0000269|PubMed:17355870"
FT   MUTAGEN         151
FT                   /note="K->A: Disrupts interaction with tubulin
FT                   heterodimer."
FT                   /evidence="ECO:0000269|PubMed:17355870"
FT   MUTAGEN         200
FT                   /note="R->A: No effect on polymerase activity under normal
FT                   conditions but impairs polymerase activity under
FT                   microtubule stress."
FT                   /evidence="ECO:0000269|PubMed:22904013,
FT                   ECO:0000269|PubMed:25097237"
FT   MUTAGEN         341
FT                   /note="W->A: Disrupts interaction with tubulin heterodimer.
FT                   Impairs polymerase activity under microtubule stress."
FT                   /evidence="ECO:0000269|PubMed:22904013,
FT                   ECO:0000269|PubMed:25097237"
FT   MUTAGEN         519
FT                   /note="R->A: Disrupts interaction with tubulin heterodimer.
FT                   No effect on polymerase activity under normal conditions
FT                   but impairs polymerase activity under microtubule stress."
FT                   /evidence="ECO:0000269|PubMed:22904013,
FT                   ECO:0000269|PubMed:25097237"
FT   HELIX           14..17
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           23..38
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           58..63
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           69..83
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           93..110
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           117..132
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   STRAND          134..137
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           138..144
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           145..149
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           153..170
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   TURN            171..174
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           177..184
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           185..187
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           188..192
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           197..211
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           231..241
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           256..268
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   HELIX           325..327
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           332..336
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           341..354
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           356..358
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           370..382
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           386..403
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   TURN            405..407
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           410..422
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           423..425
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           429..445
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           456..465
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           471..487
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           493..499
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   TURN            500..502
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           503..511
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           516..533
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           536..538
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           539..544
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           547..558
FT                   /evidence="ECO:0000244|PDB:2QK1"
FT   HELIX           658..754
FT                   /evidence="ECO:0000244|PDB:6BL7"
SQ   SEQUENCE   888 AA;  100918 MW;  7A49C3702E21C7BF CRC64;
     MSGEEEVDYT TLPLEERLTY KLWKARLEAY KELNQLFRNS VGDISRDDNI QIYWRDPTLF
     AQYITDSNVV AQEQAIVALN SLIDAFASSS LKNAHNITLI STWTPLLVEK GLTSSRATTK
     TQSMSCILSL CGLDTSITQS VELVIPFFEK KLPKLIAAAA NCVYELMAAF GLTNVNVQTF
     LPELLKHVPQ LAGHGDRNVR SQTMNLIVEI YKVTGNNSDL LEEILFKKLK PIQVKDLHKL
     FAKVGDEPSS SKMLFEWEKR ELEKKRSQEE EARKRKSILS NDEGEYQIDK DGDTLMGMET
     DMPPSKQQSG VQIDTFSMLP EETILDKLPK DFQERITSSK WKDRVEALEE FWDSVLSQTK
     KLKSTSQNYS NLLGIYGHII QKDANIQAVA LAAQSVELIC DKLKTPGFSK DYVSLVFTPL
     LDRTKEKKPS VIEAIRKALL TICKYYDPLA SSGRNEDMLK DILEHMKHKT PQIRMECTQL
     FNASMKEEKD GYSTLQRYLK DEVVPIVIQI VNDTQPAIRT IGFESFAILI KIFGMNTFVK
     TLEHLDNLKR KKIEETVKTL PNFSIASGST HSTIETNKQT GPMENKFLLK KSSVLPSKRV
     ASSPLRNDNK SKVNPIGSVA SASKPSMVAA NNKSRVLLTS KSLATPKNVV ANSTDKNEKL
     IEEYKYRLQK LQNDEMIWTK ERQSLLEKMN NTENYKIEMI KENEMLREQL KEAQSKLNEK
     NIQLRSKEID VNKLSDRVLS LENELRNMEI ELDRNKKRND TNLQSMGTIS SYSIPSSTVS
     SNYGVKSLSS ALPFKEEEDV RRKEDVNYER RSSESIGDLP HRVNSLNIRP YRKNGTGVSS
     VSDDLDIDFN DSFASEESYK RAAAVTSTLK ARIEKMKAKS RREGTTRT
//
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