MYO6_MOUSE
ID MYO6_MOUSE Reviewed; 1265 AA.
AC Q64331;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Unconventional myosin-VI;
DE AltName: Full=Protein twist {ECO:0000303|PubMed:17329413};
DE AltName: Full=Unconventional myosin-6;
GN Name=Myo6; Synonyms=Sv;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP SNELL'S WALTZER 766-PHE--LYS-1265 DEL.
RC TISSUE=Brain;
RX PubMed=7493015; DOI=10.1038/ng1295-369;
RA Avraham K.B., Hasson T., Steel K.P., Kingsley D.M., Russell L.B.,
RA Mooseker M.S., Copeland N.G., Jenkins N.A.;
RT "The mouse Snell's waltzer deafness gene encodes an unconventional myosin
RT required for structural integrity of inner ear hair cells.";
RL Nat. Genet. 11:369-375(1995).
RN [2]
RP FUNCTION, INTERACTION WITH DAB2, AND SUBCELLULAR LOCATION.
RX PubMed=11906161; DOI=10.1006/bbrc.2002.6636;
RA Inoue A., Sato O., Homma K., Ikebe M.;
RT "DOC-2/DAB2 is the binding partner of myosin VI.";
RL Biochem. Biophys. Res. Commun. 292:300-307(2002).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=17329413; DOI=10.1523/jneurosci.4975-06.2007;
RA Schwander M., Sczaniecka A., Grillet N., Bailey J.S., Avenarius M.,
RA Najmabadi H., Steffy B.M., Federe G.C., Lagler E.A., Banan R., Hice R.,
RA Grabowski-Boase L., Keithley E.M., Ryan A.F., Housley G.D., Wiltshire T.,
RA Smith R.J., Tarantino L.M., Mueller U.;
RT "A forward genetics screen in mice identifies recessive deafness traits and
RT reveals that pejvakin is essential for outer hair cell function.";
RL J. Neurosci. 27:2163-2175(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; SER-1028 AND SER-1126,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=22039235; DOI=10.1167/iovs.11-8246;
RA Sokal I., Haeseleer F.;
RT "Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.";
RL Invest. Ophthalmol. Vis. Sci. 52:9131-9141(2011).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC (PubMed:11906161). Unconventional myosins serve in intracellular
CC movements (PubMed:11906161). Myosin 6 is a reverse-direction motor
CC protein that moves towards the minus-end of actin filaments (By
CC similarity). Has slow rate of actin-activated ADP release due to weak
CC ATP binding (By similarity). Functions in a variety of intracellular
CC processes such as vesicular membrane trafficking and cell migration (By
CC similarity). Required for the structural integrity of the Golgi
CC apparatus via the p53-dependent pro-survival pathway (By similarity).
CC Appears to be involved in a very early step of clathrin-mediated
CC endocytosis in polarized epithelial cells (By similarity). May act as a
CC regulator of F-actin dynamics (By similarity). As part of the DISP
CC complex, may regulate the association of septins with actin and thereby
CC regulate the actin cytoskeleton (By similarity). May play a role in
CC transporting DAB2 from the plasma membrane to specific cellular targets
CC (PubMed:11906161). May play a role in the extension and network
CC organization of neurites (PubMed:22039235). Required for structural
CC integrity of inner ear hair cells (PubMed:7493015). Modulates RNA
CC polymerase II-dependent transcription (By similarity).
CC {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q9UM54,
CC ECO:0000269|PubMed:11906161, ECO:0000269|PubMed:22039235,
CC ECO:0000269|PubMed:7493015}.
CC -!- SUBUNIT: Homodimer; dimerization seems to implicate the unfolding of
CC the three-helix bundle region creating an additional calmodulin binding
CC site, and cargo binding (By similarity). Able to function as a monomer
CC under specific conditions in vitro (By similarity). Forms a complex
CC with CFTR and DAB2 in the apical membrane of epithelial cells (By
CC similarity). Component of the DISP/DOCK7-induced septin displacement
CC complex, at least composed of DOCK7, LRCH3 and MYO6 (By similarity).
CC Binding to calmodulin through a unique insert, not found in other
CC myosins, located in the neck region between the motor domain and the IQ
CC domain appears to contribute to the directionality reversal (By
CC similarity). This interaction occurs only if the C-terminal lobe of
CC calmodulin is occupied by calcium (By similarity). Interaction with F-
CC actin/ACTN1 occurs only at the apical brush border domain of the
CC proximal tubule cells (By similarity). Interacts with DAB2
CC (PubMed:11906161). In vitro, the C-terminal globular tail binds a C-
CC terminal region of DAB2 (PubMed:11906161). Interacts with CFTR (By
CC similarity). Interacts with OPTN (By similarity). Interacts with CABP5
CC (By similarity). {ECO:0000250|UniProtKB:E1BPK6,
CC ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q9I8D1,
CC ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:11906161}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane,
CC clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell
CC projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection,
CC ruffle membrane {ECO:0000250|UniProtKB:Q9UM54}. Cell projection,
CC microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocyctic
CC vesicles (By similarity). Translocates from membrane ruffles, endocytic
CC vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and
CC nucleus through induction by p53 and p53-induced DNA damage (By
CC similarity). Recruited into membrane ruffles from cell surface by EGF-
CC stimulation (By similarity). Colocalizes with DAB2 in clathrin-coated
CC pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi
CC complex and in vesicular structures close to the plasma membrane (By
CC similarity). {ECO:0000250|UniProtKB:Q9I8D1,
CC ECO:0000250|UniProtKB:Q9UM54}.
CC -!- TISSUE SPECIFICITY: Within the cochlea, expressed specifically within
CC the sensory hair cells (at protein level) (PubMed:7493015). Expressed
CC in the inner and outer plexiform layer of the retina (at protein level)
CC (PubMed:22039235). Widely expressed (PubMed:7493015). Expressed in the
CC brain, kidney, liver, and testis (PubMed:7493015).
CC {ECO:0000269|PubMed:22039235, ECO:0000269|PubMed:7493015}.
CC -!- DOMAIN: Divided into three regions: a N-terminal motor (head) domain,
CC followed by a neck domain consisting of a calmodulin-binding linker
CC domain and a single IQ motif, and a C-terminal tail region with a
CC three-helix bundle region, a SAH domain and a unique globular domain
CC required for interaction with other proteins such as cargo-binding.
CC {ECO:0000250|UniProtKB:Q29122}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds (By similarity). Its contribution to
CC the mechanism confering the myosin movement on actin filaments is
CC debated (By similarity). {ECO:0000250|UniProtKB:Q9UM54}.
CC -!- PTM: Phosphorylation in the motor domain, induced by EGF, results in
CC translocation of MYO6 from the cell surface to membrane ruffles and
CC affects F-actin dynamics. Phosphorylated in vitro by p21-activated
CC kinase (PAK). {ECO:0000250|UniProtKB:Q9UM54}.
CC -!- DISEASE: Note=Defects in Myo6 are the cause of Snell's waltzer, a
CC condition characterized by circling, head-tossing, deafness and
CC hyperactivity. {ECO:0000269|PubMed:7493015}.
CC -!- DISRUPTION PHENOTYPE: Mice display hearing loss, hyperactivity and
CC circling behavior, suggesting vestibular defects.
CC {ECO:0000269|PubMed:17329413}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-6 (MYH6). {ECO:0000305}.
CC -!- CAUTION: Originally predicted to contain a coiled coil domain but
CC generally accepted to contain a stable SAH domain instead.
CC {ECO:0000305}.
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DR EMBL; U49739; AAB00194.1; -; mRNA.
DR PIR; A59299; A59299.
DR PDB; 2KIA; NMR; -; A=1137-1265.
DR PDB; 2LD3; NMR; -; A=843-925.
DR PDB; 3H8D; X-ray; 2.20 A; A/B/C/D=1137-1265.
DR PDB; 5V6E; X-ray; 3.51 A; B/D/F/H/J=1055-1099.
DR PDB; 5V6H; X-ray; 3.60 A; B/D/F/H/J=1055-1099.
DR PDBsum; 2KIA; -.
DR PDBsum; 2LD3; -.
DR PDBsum; 3H8D; -.
DR PDBsum; 5V6E; -.
DR PDBsum; 5V6H; -.
DR AlphaFoldDB; Q64331; -.
DR BMRB; Q64331; -.
DR SMR; Q64331; -.
DR IntAct; Q64331; 7.
DR MINT; Q64331; -.
DR STRING; 10090.ENSMUSP00000036181; -.
DR iPTMnet; Q64331; -.
DR PhosphoSitePlus; Q64331; -.
DR jPOST; Q64331; -.
DR MaxQB; Q64331; -.
DR PeptideAtlas; Q64331; -.
DR PRIDE; Q64331; -.
DR ProteomicsDB; 286130; -.
DR MGI; MGI:104785; Myo6.
DR eggNOG; KOG0163; Eukaryota.
DR InParanoid; Q64331; -.
DR PhylomeDB; Q64331; -.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR ChiTaRS; Myo6; mouse.
DR EvolutionaryTrace; Q64331; -.
DR PRO; PR:Q64331; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64331; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0098683; C:cochlear hair cell ribbon synapse; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IPI:MGI.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0098833; C:presynaptic endocytic zone; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; IPI:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IMP:MGI.
DR GO; GO:0014047; P:glutamate secretion; IMP:MGI.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0006605; P:protein targeting; IPI:MGI.
DR GO; GO:0051046; P:regulation of secretion; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01382; MYSc_Myo6; 1.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR032412; Myosin-VI_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR036114; MYSc_Myo6.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF16521; Myosin-VI_CBD; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cell projection; Coated pit; Cytoplasm; Cytoplasmic vesicle;
KW Deafness; Disease variant; Endocytosis; Golgi apparatus; Hearing; Membrane;
KW Motor protein; Myosin; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1265
FT /note="Unconventional myosin-VI"
FT /id="PRO_0000123465"
FT DOMAIN 2..53
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 57..774
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 817..837
FT /note="IQ"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 273..317
FT /note="Responsible for slow ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 668..675
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 785..813
FT /note="Required for binding calmodulin"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 838..919
FT /note="Three-helix bundle"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 920..987
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT REGION 936..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1089
FT /note="Interaction with OPTN"
FT /evidence="ECO:0000250|UniProtKB:Q9I8D1"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VARIANT 766..1265
FT /note="Missing (in Snell's waltzer)"
FT /evidence="ECO:0000269|PubMed:7493015"
FT HELIX 843..861
FT /evidence="ECO:0007829|PDB:2LD3"
FT HELIX 867..889
FT /evidence="ECO:0007829|PDB:2LD3"
FT HELIX 895..922
FT /evidence="ECO:0007829|PDB:2LD3"
FT HELIX 1138..1142
FT /evidence="ECO:0007829|PDB:2KIA"
FT STRAND 1147..1156
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 1158..1160
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 1165..1167
FT /evidence="ECO:0007829|PDB:3H8D"
FT STRAND 1170..1178
FT /evidence="ECO:0007829|PDB:3H8D"
FT STRAND 1181..1188
FT /evidence="ECO:0007829|PDB:3H8D"
FT STRAND 1190..1192
FT /evidence="ECO:0007829|PDB:3H8D"
FT STRAND 1195..1198
FT /evidence="ECO:0007829|PDB:3H8D"
FT TURN 1199..1205
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 1211..1214
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 1216..1218
FT /evidence="ECO:0007829|PDB:3H8D"
FT TURN 1220..1222
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 1226..1235
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 1238..1247
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 1255..1263
FT /evidence="ECO:0007829|PDB:3H8D"
SQ SEQUENCE 1265 AA; 146409 MW; 4F51ABC72463148C CRC64;
MEDGKPVWAP HPTDGFQMGN IVDIGPDSLT IEPLNQKGKT FGALINQVFP AEEDSKKDVE
DNCSLMYLNE ATLLHNVKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSD TIKSYQGKSL
GTMPPHVFGI ADKAFRDMKV LKMSQSIIVS GESGAGKTEN TKFGSKIPDR ILWTGQDIDD
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK
EERNHHIFYR LCAGASEDIR EKLHLSSPDN FRYLNRGCTR FFANKETDKQ ILQNRKSPEY
VKAGSLEGSS IRRPWRFYQD VHSHEKNWFG MMKKNFDLFR VVAGVLHLGN IDLEEAGSTS
GGCNLKNKSA PSLEYCAELL GLDQDDLRVS LTTRVMLTTA GGTKGTVIKV PLKVEQANNA
RDALAKTVYS HLFDHVVNRV NQCFPFETSS YFIGVLDIAG FEYFEHNSFE QFCINYCNEK
LQQFFNERIL KEEQELYQKE GLGVNEVHYV DNQDCIELIE VKLVGILDIL DEENRLPQPS
DQHFTSVVHQ KHKDHFRLTI PRKSKLAVHR NLRDDEGFII RQLCRGRVLR RQPQYGGGKN
NDALHMSLES LICESRDKFI RALFESSTNN SKDTKQKAGK LSFISVGNKF KTQLNLLLDK
LRSTGASFIR CIKPNLKMAS HHFEGAQILS QLQCSGMVSV LDLMQGGFPS RASFHELYNM
YKKYMPEKLP RLDPRLFCKP LFKALGLNEV DYKFGLTQVF FRPGKFAEFD QIMKSDPDHL
AELVKRVNLW LVCSRWKKVQ WCSLSVIKLK NKIKYRAEAC IKMQKPIRMW LCKRRHNPRI
DGLVKVGTLK KRLDKFNEVV SALKDGKPEV NRQIKNLEIS IDALMAKFTS TMMTREQIQK
EYDALVKSSE DLLSALQKKK QQEEEAERLR RIQEEMEKER KRREEDEERR RKEEEERRMK
LEMEPKRKQE EEERKKREDD EKRIQSEVEA QLARQREEES QQQAVLAQEC RDRELALRIA
QNESELISDE AQGDMALRRG PAVQATKAAS GTKKHDLSKW KYAELRDTIN TSCDIELLAA
CREEFHRRLK VYHAWKSKNK KRNTETEQRA PKSVTDYDFA PFLNNSPQQN PAAQLPARQQ
EIDMKRQQRF FRIPFIRPAD QYKDPQNKKK GWWYAHFDGP WIARQMELHP DKPPILLVAG
KDDMEMCELN LEETGLTRKR GAEILPRQFE EIWERCGGIQ YLQSAIESRQ ARPTYATAML
QNLLK
