ZYG9_CAEEL
ID ZYG9_CAEEL Reviewed; 1415 AA.
AC G5EEM5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Zygote defective protein 9 {ECO:0000303|PubMed:9606208};
GN Name=zyg-9 {ECO:0000312|EMBL:AAC17865.1, ECO:0000312|WormBase:F22B5.7};
GN ORFNames=F22B5.7 {ECO:0000312|WormBase:F22B5.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=9606208; DOI=10.1083/jcb.141.5.1159;
RA Matthews L.R., Carter P., Thierry-Mieg D., Kemphues K.J.;
RT "ZYG-9, a Caenorhabditis elegans protein required for microtubule
RT organization and function, is a component of meiotic and mitotic spindle
RT poles.";
RL J. Cell Biol. 141:1159-1168(1998).
RN [2] {ECO:0000312|EMBL:CAA90359.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=7371984; DOI=10.1016/0012-1606(80)90445-5;
RA Wood W.B., Hecht R., Carr S., Vanderslice R., Wolf N., Hirsh D.;
RT "Parental effects and phenotypic characterization of mutations that affect
RT early development in Caenorhabditis elegans.";
RL Dev. Biol. 74:446-469(1980).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=6684994; DOI=10.1016/0092-8674(83)90203-9;
RA Strome S., Wood W.B.;
RT "Generation of asymmetry and segregation of germ-line granules in early C.
RT elegans embryos.";
RL Cell 35:15-25(1983).
RN [5] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=3949074; DOI=10.1016/0012-1606(86)90180-6;
RA Kemphues K.J., Wolf N., Wood W.B., Hirsh D.;
RT "Two loci required for cytoplasmic organization in early embryos of
RT Caenorhabditis elegans.";
RL Dev. Biol. 113:449-460(1986).
RN [6] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=3224814; DOI=10.1093/genetics/120.4.977;
RA Kemphues K.J., Kusch M., Wolf N.;
RT "Maternal-effect lethal mutations on linkage group II of Caenorhabditis
RT elegans.";
RL Genetics 120:977-986(1988).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=2249759; DOI=10.1093/genetics/126.3.593;
RA Mains P.E., Kemphues K.J., Sprunger S.A., Sulston I.A., Wood W.B.;
RT "Mutations affecting the meiotic and mitotic divisions of the early
RT Caenorhabditis elegans embryo.";
RL Genetics 126:593-605(1990).
RN [8] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=1614224; DOI=10.1016/0047-6374(92)90002-u;
RA Honda S., Matsuo M.;
RT "Lifespan shortening of the nematode Caenorhabditis elegans under higher
RT concentrations of oxygen.";
RL Mech. Ageing Dev. 63:235-246(1992).
RN [9] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RC STRAIN=Bristol N2;
RX PubMed=10085292; DOI=10.1083/jcb.144.5.927;
RA Gonczy P., Schnabel H., Kaletta T., Amores A.D., Hyman T., Schnabel R.;
RT "Dissection of cell division processes in the one cell stage Caenorhabditis
RT elegans embryo by mutational analysis.";
RL J. Cell Biol. 144:927-946(1999).
RN [10] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RC STRAIN=Bristol N2;
RX PubMed=12011109; DOI=10.1083/jcb.200202047;
RA Hannak E., Oegema K., Kirkham M., Gonczy P., Habermann B., Hyman A.A.;
RT "The kinetically dominant assembly pathway for centrosomal asters in
RT Caenorhabditis elegans is gamma-tubulin dependent.";
RL J. Cell Biol. 157:591-602(2002).
RN [11] {ECO:0000305}
RP FUNCTION, HETERODIMER WITH TAC-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=12956952; DOI=10.1016/s0960-9822(03)00597-9;
RA Srayko M., Quintin S., Schwager A., Hyman A.A.;
RT "Caenorhabditis elegans TAC-1 and ZYG-9 form a complex that is essential
RT for long astral and spindle microtubules.";
RL Curr. Biol. 13:1506-1511(2003).
RN [12] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=12885567; DOI=10.1016/s0012-1606(03)00216-1;
RA Yang H.-Y., McNally K., McNally F.J.;
RT "MEI-1/katanin is required for translocation of the meiosis I spindle to
RT the oocyte cortex in C elegans.";
RL Dev. Biol. 260:245-259(2003).
RN [13] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=15866166; DOI=10.1016/j.devcel.2005.03.007;
RA Kimura A., Onami S.;
RT "Computer simulations and image processing reveal length-dependent pulling
RT force as the primary mechanism for C. elegans male pronuclear migration.";
RL Dev. Cell 8:765-775(2005).
RN [14] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=16054029; DOI=10.1016/j.devcel.2005.07.003;
RA Srayko M., Kaya A., Stamford J., Hyman A.A.;
RT "Identification and characterization of factors required for microtubule
RT growth and nucleation in the early C. elegans embryo.";
RL Dev. Cell 9:223-236(2005).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16971515; DOI=10.1091/mbc.e06-02-0107;
RA DeBella L.R., Hayashi A., Rose L.S.;
RT "LET-711, the Caenorhabditis elegans NOT1 ortholog, is required for spindle
RT positioning and regulation of microtubule length in embryos.";
RL Mol. Biol. Cell 17:4911-4924(2006).
RN [16] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-203; GLY-488; ILE-862 AND GLU-1317.
RC STRAIN=Bristol N2;
RX PubMed=17666432; DOI=10.1242/jcs.004812;
RA Bellanger J.M., Carter J.C., Phillips J.B., Canard C., Bowerman B.,
RA Gonczy P.;
RT "ZYG-9, TAC-1 and ZYG-8 together ensure correct microtubule function
RT throughout the cell cycle of C. elegans embryos.";
RL J. Cell Sci. 120:2963-2973(2007).
RN [17] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 602-867, AND TOG DOMAIN.
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).
CC -!- FUNCTION: Plays a major role in organizing microtubules and spindle
CC poles during mitosis and meiosis in one-cell stage embryos
CC (PubMed:16971515). Required for default nucleus positioning in oocytes
CC (PubMed:16971515). {ECO:0000269|PubMed:12956952,
CC ECO:0000269|PubMed:15866166, ECO:0000269|PubMed:16054029,
CC ECO:0000269|PubMed:16971515, ECO:0000269|PubMed:17666432,
CC ECO:0000269|PubMed:2249759, ECO:0000269|PubMed:3949074,
CC ECO:0000269|PubMed:6684994, ECO:0000269|PubMed:9606208}.
CC -!- SUBUNIT: Interacts with tac-1 to form a heterodimer.
CC {ECO:0000269|PubMed:12956952}.
CC -!- INTERACTION:
CC G5EEM5; G5ECG0: tac-1; NbExp=13; IntAct=EBI-320102, EBI-320612;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:10085292, ECO:0000269|PubMed:12011109,
CC ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432,
CC ECO:0000269|PubMed:9606208}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:10085292,
CC ECO:0000269|PubMed:12011109, ECO:0000269|PubMed:12956952,
CC ECO:0000269|PubMed:16971515, ECO:0000269|PubMed:17666432,
CC ECO:0000269|PubMed:9606208}. Cytoplasm {ECO:0000269|PubMed:10085292,
CC ECO:0000269|PubMed:12011109, ECO:0000269|PubMed:12956952,
CC ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:9606208}. Note=Cycles
CC between cytoplasm and centrosome during mitosis in a cell
CC cycle- dependent manner. Centrosomal recruitment requires tbg-1.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally during oogenesis. Observed
CC during mitotic cell cycle from interphase through to early anaphase.
CC {ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:3224814,
CC ECO:0000269|PubMed:3949074, ECO:0000269|PubMed:9606208}.
CC -!- DOMAIN: The TOG (tumor overexpressed gene) domains are arranged in the
CC N-terminal region with each domain composed of six (for the most part
CC non-canonical) HEAT repeats and forming a oblong paddle-like structure.
CC 3D-structure analysis shows the presence of additional HEAT repeats
CC that are not detected by sequence-based prediction programs. Intra-HEAT
CC loops are positioned along a face of the TOG domain and bind to a
CC single alpha/beta-tubulin heterodimer. The TOG domains seem to be
CC structurally and functionally polarized. Differential functions may
CC range from microtubule (MT) lattice binding and/or free tubulin
CC heterodimer binding to potentiating stable incorporation of tubulin
CC into the MT lattice. {ECO:0000305, ECO:0000305|PubMed:17355870}.
CC -!- DISRUPTION PHENOTYPE: Maternal-effect embryonic lethal with meiotic and
CC mitotic spindle positioning defects in one-cell stage embryos. RNAi-
CC mediated knockdown results in meiosis and mitosis defects in embryos
CC whereby embryos have one or both polar bodies absent, more than one
CC female pronucleus and display irregular female pronuclear migration,
CC which leads to delayed association with the male pronucleus
CC (PubMed:16971515). RNAi-mediated knockdown results in defective mitotic
CC spindle positioning and rotation in which spindles are established in
CC the posterior side of the embryo and on the wrong axis
CC (PubMed:16971515). RNAi-mediated knockdown results in a decrease in
CC length of astral microtubules in embryos, with fewer microtubules
CC extending from their centrosomes during cold conditions
CC (PubMed:16971515). RNAi-mediated knockdown in a let-711 heteroallelic
CC s2587 and it150 mutant background results in inviable embryos which do
CC not hatch, however the astral microtubule length, polar body, female
CC pronuclear migration and mitotic spindle defects of the single zyg-9
CC RNAi mutant are partially suppressed (PubMed:16971515).
CC {ECO:0000269|PubMed:12885567, ECO:0000269|PubMed:12956952,
CC ECO:0000269|PubMed:15866166, ECO:0000269|PubMed:16054029,
CC ECO:0000269|PubMed:1614224, ECO:0000269|PubMed:16971515,
CC ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:2249759,
CC ECO:0000269|PubMed:3949074, ECO:0000269|PubMed:6684994,
CC ECO:0000269|PubMed:7371984, ECO:0000269|PubMed:9606208}.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000255}.
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DR EMBL; AF035197; AAC17865.1; -; mRNA.
DR EMBL; Z50044; CAA90359.1; -; Genomic_DNA.
DR PIR; T21244; T21244.
DR RefSeq; NP_495784.1; NM_063383.4.
DR PDB; 2OF3; X-ray; 1.90 A; A=602-867.
DR PDBsum; 2OF3; -.
DR AlphaFoldDB; G5EEM5; -.
DR SMR; G5EEM5; -.
DR BioGRID; 39679; 50.
DR ComplexPortal; CPX-372; Zyg-9/Tac-1 complex.
DR IntAct; G5EEM5; 4.
DR STRING; 6239.F22B5.7; -.
DR EPD; G5EEM5; -.
DR PaxDb; G5EEM5; -.
DR PeptideAtlas; G5EEM5; -.
DR EnsemblMetazoa; F22B5.7.1; F22B5.7.1; WBGene00006994.
DR GeneID; 174350; -.
DR KEGG; cel:CELE_F22B5.7; -.
DR CTD; 174350; -.
DR WormBase; F22B5.7; CE20707; WBGene00006994; zyg-9.
DR eggNOG; KOG1820; Eukaryota.
DR HOGENOM; CLU_251066_0_0_1; -.
DR InParanoid; G5EEM5; -.
DR OMA; GRMADKD; -.
DR OrthoDB; 33681at2759; -.
DR PhylomeDB; G5EEM5; -.
DR EvolutionaryTrace; G5EEM5; -.
DR PRO; PR:G5EEM5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006994; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0072687; C:meiotic spindle; IDA:UniProtKB.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:ComplexPortal.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:ComplexPortal.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:WormBase.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IBA:GO_Central.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:WormBase.
DR GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IDA:ComplexPortal.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; IMP:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
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 InterPro; IPR029632; Zyg-9.
DR PANTHER; PTHR12609; PTHR12609; 1.
DR PANTHER; PTHR12609:SF1; PTHR12609:SF1; 1.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Meiosis; Microtubule; Mitosis; Reference proteome; Repeat.
FT CHAIN 1..1415
FT /note="Zygote defective protein 9"
FT /id="PRO_0000416050"
FT REPEAT 30..68
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 95..132
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 135..172
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 179..217
FT /note="HEAT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 339..377
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 381..418
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 420..457
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 464..502
FT /note="HEAT 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 706..743
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 764..801
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 804..841
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REGION 1..250
FT /note="TOG 1"
FT /evidence="ECO:0000305|PubMed:17355870"
FT REGION 243..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..530
FT /note="TOG 2"
FT /evidence="ECO:0000305|PubMed:17355870"
FT REGION 544..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..867
FT /note="TOG 3"
FT /evidence="ECO:0000305|PubMed:17355870"
FT REGION 867..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..48
FT /evidence="ECO:0000255"
FT COMPBIAS 251..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 203
FT /note="G->E: In or628; decrease in abundance at
FT centromeres."
FT /evidence="ECO:0000269|PubMed:17666432"
FT MUTAGEN 488
FT /note="G->E: In or593; decrease in abundance at
FT centromeres."
FT /evidence="ECO:0000269|PubMed:17666432"
FT MUTAGEN 862
FT /note="I->K: In or635; reduction in tac-1 binding."
FT /evidence="ECO:0000269|PubMed:17666432"
FT MUTAGEN 1317
FT /note="E->K: In or643; decrease in abundance at centromeres
FT and in the cytoplasm and reduction in tac-1 binding."
FT /evidence="ECO:0000269|PubMed:17666432"
FT HELIX 611..620
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 634..645
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 650..656
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 661..677
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 679..684
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 686..696
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 702..721
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 728..740
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 741..743
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 747..764
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 766..775
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 782..799
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 802..807
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 809..813
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 814..818
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 822..839
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 842..847
FT /evidence="ECO:0007829|PDB:2OF3"
FT HELIX 852..865
FT /evidence="ECO:0007829|PDB:2OF3"
SQ SEQUENCE 1415 AA; 156189 MW; 9518FFA233ABB3A6 CRC64;
MSNWDYLDEV DILPKLPPNF DELRESKKWQ ERKEALEALL KVLTDNERLS TKASYAELIG
HLQMVLAKDA NINCQALAAK CIGKFATGLR AKFSSFAGPL LPVIFEKMKE KKPMLREPLV
DCSNEVGRTM QSLETGQEDI LAALAKPNPQ IKQQTALFVA RQLDLVVPAK QPKGFIKAVV
PVFGKLTGDA DQDVREASLQ GLGAVQRIIG DKNVKNLLGD ASSDEGKMKK IGEYAEKSTA
SFAEEQAKNA PPVAPTSSTP SASAASGDPS GGTATAVVSS GAPVAEADPW DFLDAFDVLS
KMPDGFDTNI ESKKWQERKE ALEGLLQLIT ANPKLDPKAN YGALVERLQK VLEKDANINV
AALAANCITG IANGLRTKFQ PFAVSVTPII FEKFKEKKPT LRDPLVACID AVVATTNLEA
VGEIVLAALG KPNPSIKTQT DLFLQRCFMK LNSQTMPKKT LKTLIPSLIK HSGDSDSEVR
EASYAAMGAM MRAIGEKPSL QLLADIASDN LKMSKIKEFH QKALDEAGPA EIAEMVKSIH
KADAPPAAAP PKKTAPPKKQ PEDEEVVEEE DEPLKPPPGD KKKKVPVKEN EENEPPVVAP
KAELLLSDNE DKKQRIKEEK QLKLVKWNFQ APTDEHISQL QTLLGNQAKV SLMSQLFHKD
FKQHLAALDS LVRLADTSPR SLLSNSDLLL KWCTLRFFET NPAALIKVLE LCKVIVELIR
DTETPMSQEE VSAFVPYLLL KTGEAKDNMR TSVRDIVNVL SDVVGPLKMT PMLLDALKSK
NARQRSECLL VIEYYITNAG ISPLKSLSVE KTVAPFVGDK DVNVRNAAIN VLVACFKFEG
DQMWKAAGRM ADKDKSLVEE RIKRTGVKPG SGVVTSPPTG GPKILVPQQQ GSVVRRPASR
SRTREPEPEE VQSDTFTIRQ DTMPPKTSSR YALRDDVFSS AMGRLDGTQV ITPPQPVNGW
SNNTFQMKRT NSSSSISSID TSDQIQRSIN NISSSLADVA QDAMFQVTYV LNQPEQRHLV
DRRADLVFRA SAAQLDLVIE EFNAGRDVSG TMDACTQMLF ILMGGVETEH GLEPLNASPD
TVKAIISSVL RCIIQIGNTE SGYGMARSLN RLAMRLIYRV ELSNLLCGLI LAMTESLQMN
TGITELVSKL SSKWCDELEK RRAQLRASDI VDSFNAFYVC ALTELKMDIS DSHILIVDNY
LERVILQQGD VVLDAARRLS RPHMHLTSMI NKILQMMRER KIDPIMPGTL EARMPQEDEA
VVVRSGVQVS IDNILRDTSM AVKHIEQLNI LIASSDRSWN EYMEYLKNNP MGELIKELVG
ECSRKKRIDF NLSHVVKSSM AVFKAMAATG PVQEEGRITP TDINRMDTMI VGTPLSRGDA
TITRARGNMI RPKRTTLSRD QMANIRHTLD RVKNH
