STU2_YEAST
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 03-AUG-2022, entry version 177.
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}.
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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 PDB; 7KDF; X-ray; 2.72 A; E=856-888.
DR PDBsum; 2QK1; -.
DR PDBsum; 4FFB; -.
DR PDBsum; 4U3J; -.
DR PDBsum; 6BL7; -.
DR PDBsum; 7KDF; -.
DR AlphaFoldDB; P46675; -.
DR SMR; P46675; -.
DR BioGRID; 31320; 609.
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 SGD; S000004035; STU2.
DR VEuPathDB; FungiDB:YLR045C; -.
DR eggNOG; KOG1820; Eukaryota.
DR GeneTree; ENSGT00390000014757; -.
DR HOGENOM; CLU_008401_1_1_1; -.
DR InParanoid; P46675; -.
DR OMA; HMGSRFE; -.
DR BioCyc; YEAST:G3O-32201-MON; -.
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: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:0051010; F:microtubule plus-end binding; IEA:InterPro.
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 InterPro; IPR045110; XMAP215.
DR PANTHER; PTHR12609; PTHR12609; 1.
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 REGION 756..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 654..762
FT /evidence="ECO:0000255"
FT COMPBIAS 761..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|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:0007829|PDB:4FFB"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:4FFB"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:4FFB"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:4FFB"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 341..354
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 386..403
FT /evidence="ECO:0007829|PDB:2QK1"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 429..445
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 471..487
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 493..499
FT /evidence="ECO:0007829|PDB:2QK1"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 503..511
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 516..533
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 547..558
FT /evidence="ECO:0007829|PDB:2QK1"
FT HELIX 658..754
FT /evidence="ECO:0007829|PDB:6BL7"
FT HELIX 865..881
FT /evidence="ECO:0007829|PDB:7KDF"
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
