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Huntingtin (Huntington disease protein homolog) (HD protein homolog)

 HD_MOUSE                Reviewed;        3119 AA.
P42859;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 162.
RecName: Full=Huntingtin;
AltName: Full=Huntington disease protein homolog;
Short=HD protein homolog;
Name=Htt; Synonyms=Hd, Hdh;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
STRAIN=C57BL/6J; TISSUE=Brain, and Spleen;
PubMed=8162057; DOI=10.1093/hmg/3.1.85;
Lin B., Nasir J., Macdonald H., Hutchinson G., Graham R.K.,
Rommens J.M., Hayden M.R.;
"Sequence of the murine Huntington disease gene: evidence for
conservation, alternate splicing and polymorphism in a triplet (CCG)
repeat.";
Hum. Mol. Genet. 3:85-92(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
PubMed=8009370; DOI=10.1007/BF02290678;
Barnes G.T., Duyao M.P., Ambrose C.M., McNeil S., Persichetti F.,
Srinidhi J., Gusella J.F., Macdonald M.E.;
"Mouse Huntington's disease gene homolog (Hdh).";
Somat. Cell Mol. Genet. 20:87-97(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7647777; DOI=10.1038/ng0595-104;
Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C.,
Agid Y., Hirsch E.C., Mandel J.-L.;
"Cellular localization of the Huntington's disease protein and
discrimination of the normal and mutated form.";
Nat. Genet. 10:104-110(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
PubMed=7759106; DOI=10.1016/0888-7543(95)80014-D;
Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J.,
Goldberg Y.P., Hayden M.R.;
"Structural analysis of the 5' region of mouse and human Huntington
disease genes reveals conservation of putative promoter region and
di- and trinucleotide polymorphisms.";
Genomics 25:707-715(1995).
[5]
INTERACTION WITH SH3GLB1.
PubMed=12456676; DOI=10.1074/jbc.M208568200;
Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
"Characterization of endophilin B1b, a brain-specific membrane-
associated lysophosphatidic acid acyl transferase with properties
distinct from endophilin A1.";
J. Biol. Chem. 278:4160-4167(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-398; SER-411
AND SER-1853, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH ZDHHC17 AND ZDHHC13.
PubMed=26198635; DOI=10.1074/jbc.M115.657668;
Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
"Identification of a novel sequence motif recognized by the ankyrin
repeat domain of zDHHC17/13 S-acyltransferases.";
J. Biol. Chem. 290:21939-21950(2015).
-!- FUNCTION: May play a role in microtubule-mediated transport or
vesicle function.
-!- SUBUNIT: Interacts with PFN1 (By similarity). Interacts through
its N-terminus with PRPF40A (By similarity). Interacts with PQBP1
(By similarity). Interacts with SETD2 (By similarity). Interacts
with SH3GLB1 (PubMed:12456676). Interacts with SYVN (By
similarity). Interacts with TPR; the interaction is inhibited by
forms of Huntingtin with expanded polyglutamine stretch (By
similarity). Interacts with ZDHHC13 (via ANK repeats)
(PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats)
(PubMed:26198635). {ECO:0000250|UniProtKB:P42858,
ECO:0000269|PubMed:12456676, ECO:0000269|PubMed:26198635}.
-!- INTERACTION:
P70677:Casp3; NbExp=2; IntAct=EBI-5327353, EBI-1790419;
Q02248:Ctnnb1; NbExp=3; IntAct=EBI-5327353, EBI-397872;
Q8CIN4:Pak2; NbExp=2; IntAct=EBI-5327353, EBI-1559317;
O70405:Ulk1; NbExp=4; IntAct=EBI-5327353, EBI-8390771;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Shuttles between cytoplasm and nucleus in a
Ran GTPase-independent manner.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P42859-1; Sequence=Displayed;
Name=Short;
IsoId=P42859-2; Sequence=VSP_004282;
Note=Cannot be explained by a simple splicing event.;
-!- TISSUE SPECIFICITY: The highest level is seen throughout the
brain, but it is also found in the stomach, heart, testis, adipose
tissue, muscle, spleen, liver, and kidney.
-!- DEVELOPMENTAL STAGE: Predominant expression in neuronal tissues at
all developmental stages. In 14.5 day old embryos, it is also
detected in non-neuronal tissues. This expression is down-
regulated in later stages of development.
-!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
conformational flexibility and is likely to exist in a fluctuating
equilibrium of alpha-helical, random coil, and extended
conformations. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-1159 and Ser-1179 by CDK5 in response
to DNA damage in nuclei of neurons protects neurons against
polyglutamine expansion as well as DNA damage mediated toxicity.
-!- POLYMORPHISM: The poly-Gln region does not appear to be
polymorphic, explaining the absence of a murine HD-like disorder
(PubMed:8009370). {ECO:0000269|PubMed:8009370}.
-!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}.
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EMBL; L23312; AAA37799.1; -; mRNA.
EMBL; L23313; AAA37800.1; -; mRNA.
EMBL; L28827; AAA89100.1; ALT_SEQ; mRNA.
EMBL; U24233; AAC52218.1; -; mRNA.
EMBL; AH003368; AAA91085.1; -; Genomic_DNA.
PIR; I49729; I49729.
UniGene; Mm.209071; -.
ProteinModelPortal; P42859; -.
CORUM; P42859; -.
DIP; DIP-41430N; -.
IntAct; P42859; 22.
MINT; MINT-270833; -.
STRING; 10090.ENSMUSP00000078945; -.
ChEMBL; CHEMBL1250362; -.
iPTMnet; P42859; -.
PhosphoSitePlus; P42859; -.
SwissPalm; P42859; -.
EPD; P42859; -.
MaxQB; P42859; -.
PaxDb; P42859; -.
PeptideAtlas; P42859; -.
PRIDE; P42859; -.
MGI; MGI:96067; Htt.
eggNOG; ENOG410IDZV; Eukaryota.
eggNOG; ENOG410XSEC; LUCA.
HOGENOM; HOG000082472; -.
HOVERGEN; HBG005953; -.
InParanoid; P42859; -.
PhylomeDB; P42859; -.
ChiTaRS; Htt; mouse.
PRO; PR:P42859; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_HTT; -.
GO; GO:0005776; C:autophagosome; ISO:MGI.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005814; C:centriole; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016234; C:inclusion body; IDA:MGI.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
GO; GO:0050809; F:diazepam binding; IMP:MGI.
GO; GO:0034452; F:dynactin binding; ISO:MGI.
GO; GO:0045505; F:dynein intermediate chain binding; ISO:MGI.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0005522; F:profilin binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0008306; P:associative learning; IMP:MGI.
GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0007569; P:cell aging; IMP:MGI.
GO; GO:0007417; P:central nervous system development; IMP:MGI.
GO; GO:0000052; P:citrulline metabolic process; IMP:MGI.
GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
GO; GO:0016197; P:endosomal transport; IMP:MGI.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:MGI.
GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
GO; GO:0007369; P:gastrulation; IMP:MGI.
GO; GO:0007030; P:Golgi organization; ISO:MGI.
GO; GO:0007625; P:grooming behavior; IMP:MGI.
GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
GO; GO:0030073; P:insulin secretion; IMP:MGI.
GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
GO; GO:0051938; P:L-glutamate import; IMP:MGI.
GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IMP:MGI.
GO; GO:0007612; P:learning; IMP:MGI.
GO; GO:0007611; P:learning or memory; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0006839; P:mitochondrial transport; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:1901215; P:negative regulation of neuron death; IMP:MGI.
GO; GO:0021990; P:neural plate formation; IMP:MGI.
GO; GO:0022008; P:neurogenesis; IMP:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0048666; P:neuron development; IMP:MGI.
GO; GO:0021988; P:olfactory lobe development; IMP:MGI.
GO; GO:0048341; P:paraxial mesoderm formation; IMP:MGI.
GO; GO:0030072; P:peptide hormone secretion; IMP:MGI.
GO; GO:1905337; P:positive regulation of aggrephagy; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:MGI.
GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISO:MGI.
GO; GO:1904504; P:positive regulation of lipophagy; ISO:MGI.
GO; GO:1905505; P:positive regulation of motile cilium assembly; IMP:MGI.
GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:MGI.
GO; GO:0031648; P:protein destabilization; ISO:MGI.
GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
GO; GO:0019805; P:quinolinate biosynthetic process; IMP:MGI.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:MGI.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
GO; GO:0051592; P:response to calcium ion; IMP:MGI.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISO:MGI.
GO; GO:0035176; P:social behavior; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0021756; P:striatum development; IMP:MGI.
GO; GO:0000050; P:urea cycle; IMP:MGI.
GO; GO:0047496; P:vesicle transport along microtubule; IDA:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
GO; GO:0042297; P:vocal learning; ISO:MGI.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000091; Huntingtin.
InterPro; IPR028426; Huntingtin_fam.
InterPro; IPR024613; Huntingtin_middle-repeat.
PANTHER; PTHR10170; PTHR10170; 1.
Pfam; PF12372; DUF3652; 1.
PRINTS; PR00375; HUNTINGTIN.
SUPFAM; SSF48371; SSF48371; 5.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 3119 Huntingtin.
/FTId=PRO_0000083943.
REPEAT 183 220 HEAT 1.
REPEAT 225 262 HEAT 2.
REPEAT 782 819 HEAT 3.
REPEAT 882 920 HEAT 4.
REPEAT 1404 1441 HEAT 5.
MOTIF 2372 2381 Nuclear export signal. {ECO:0000250}.
COMPBIAS 18 24 Poly-Gln.
COMPBIAS 25 45 Poly-Pro.
COMPBIAS 49 59 Poly-Pro.
COMPBIAS 1417 1420 Poly-Thr.
COMPBIAS 1696 1699 Poly-Gly.
COMPBIAS 2615 2620 Poly-Glu.
MOD_RES 9 9 N6-acetyllysine.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 155 155 N6-acetyllysine.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 213 213 N6-acetyllysine.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 322 322 N6-acetyllysine.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 421 421 N6-acetyllysine.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 1159 1159 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 1179 1179 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P42858}.
MOD_RES 1853 1853 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1522 2001 Missing (in isoform Short).
{ECO:0000303|PubMed:8162057}.
/FTId=VSP_004282.
CONFLICT 2 2 A -> G (in Ref. 1; AAA37799/AAA37800 and
4; AAA91085). {ECO:0000305}.
CONFLICT 29 29 A -> P (in Ref. 2; AAA89100).
{ECO:0000305}.
CONFLICT 116 116 N -> D (in Ref. 2; AAA89100 and 4;
AAA91085). {ECO:0000305}.
CONFLICT 138 138 M -> L (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 521 521 S -> P (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 524 524 A -> P (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 533 533 A -> P (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 607 607 A -> T (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 769 769 D -> E (in Ref. 2; AAA89100).
{ECO:0000305}.
CONFLICT 972 972 S -> R (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 1106 1106 W -> C (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 1240 1240 T -> N (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 1384 1384 N -> T (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 1827 1827 H -> Y (in Ref. 1; AAA37799).
{ECO:0000305}.
CONFLICT 1979 1980 PF -> SS (in Ref. 1; AAA37799).
{ECO:0000305}.
CONFLICT 2062 2062 D -> G (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 2570 2570 S -> N (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 2866 2866 E -> V (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 2877 2877 V -> G (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 2882 2882 D -> G (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 2887 2887 Q -> H (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 2915 2915 A -> T (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 3025 3025 P -> S (in Ref. 3; AAC52218).
{ECO:0000305}.
CONFLICT 3062 3063 QV -> LM (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
CONFLICT 3095 3096 VV -> EE (in Ref. 1; AAA37799/AAA37800).
{ECO:0000305}.
SEQUENCE 3119 AA; 344690 MW; ECA42B5916F50F4F CRC64;
MATLEKLMKA FESLKSFQQQ QQQQPPPQAP PPPPPPPPQP PQPPPQGQPP PPPPPLPGPA
EEPLHRPKKE LSATKKDRVN HCLTICENIV AQSLRNSPEF QKLLGIAMEL FLLCSNDAES
DVRMVADECL NKVIKALMDS NLPRLQLELY KEIKKNGAPR SLRAALWRFA ELAHLVRPQK
CRPYLVNLLP CLTRTSKRPE ESVQETLAAA VPKIMASFGN FANDNEIKVL LKAFIANLKS
SSPTVRRTAA GSAVSICQHS RRTQYFYNWL LNVLLGLLVP MEEEHSTLLI LGVLLTLRCL
VPLLQQQVKD TSLKGSFGVT RKEMEVSPST EQLVQVYELT LHHTQHQDHN VVTGALELLQ
QLFRTPPPEL LQALTTPGGL GQLTLVQEEA RGRGRSGSIV ELLAGGGSSC SPVLSRKQKG
KVLLGEEEAL EDDSESRSDV SSSAFAASVK SEIGGELAAS SGVSTPGSVG HDIITEQPRS
QHTLQADSVD LSGCDLTSAA TDGDEEDILS HSSSQFSAVP SDPAMDLNDG TQASSPISDS
SQTTTEGPDS AVTPSDSSEI VLDGADSQYL GMQIGQPQED DEEGAAGVLS GEVSDVFRNS
SLALQQAHLL ERMGHSRQPS DSSIDKYVTR DEVAEASDPE SKPCRIKGDI GQPNDDDSAP
LVHCVRLLSA SFLLTGEKKA LVPDRDVRVS VKALALSCIG AAVALHPESF FSRLYKVPLN
TTESTEEQYV SDILNYIDHG DPQVRGATAI LCGTLVYSIL SRSRLRVGDW LGNIRTLTGN
TFSLVDCIPL LQKTLKDESS VTCKLACTAV RHCVLSLCSS SYSDLGLQLL IDMLPLKNSS
YWLVRTELLD TLAEIDFRLV SFLEAKAESL HRGAHHYTGF LKLQERVLNN VVIYLLGDED
PRVRHVAATS LTRLVPKLFY KCDQGQADPV VAVARDQSSV YLKLLMHETQ PPSHFSVSTI
TRIYRGYSLL PSITDVTMEN NLSRVVAAVS HELITSTTRA LTFGCCEALC LLSAAFPVCT
WSLGWHCGVP PLSASDESRK SCTVGMASMI LTLLSSAWFP LDLSAHQDAL ILAGNLLAAS
APKSLRSSWT SEEEANSAAT RQEEIWPALG DRTLVPLVEQ LFSHLLKVIN ICAHVLDDVT
PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASTPMSP KKVGEASAAS RQSDTSGPVT
ASKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST EKFGGFLRSA LDVLSQILEL
ATLQDIGKCV EEVLGYLKSC FSREPMMATV CVQQLLKTLF GTNLASQFDG LSSNPSKSQC
RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ AEQERDASGW FDVLQKVSAQ
LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT SVQLQKQVLD LLAQLVQLRV
NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF LVLLSYERYH SKQIIGIPKI
IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA GKELETQKEV VVSMLLRLIQ
YHQVLEMFIL VLQQCHKENE DKWKRLSRQV ADIILPMLAK QQMHIDSHEA LGVLNTLFEI
LAPSSLRPVD MLLRSMFITP STMASVSTVQ LWISGILAIL RVLISQSTED IVLCRIQELS
FSPHLLSCPV INRLRGGGGN VTLGECSEGK QKSLPEDTFS RFLLQLVGIL LEDIVTKQLK
VDMSEQQHTF YCQELGTLLM CLIHIFKSGM FRRITAAATR LFTSDGCEGS FYTLESLNAR
VRSMVPTHPA LVLLWCQILL LINHTDHRWW AEVQQTPKRH SLSCTKSLNP QKSGEEEDSG
SAAQLGMCNR EIVRRGALIL FCDYVCQNLH DSEHLTWLIV NHIQDLISLS HEPPVQDFIS
AIHRNSAASG LFIQAIQSRC ENLSTPTTLK KTLQCLEGIH LSQSGAVLTL YVDRLLGTPF
RALARMVDTL ACRRVEMLLA ANLQSSMAQL PEEELNRIQE HLQNSGLAQR HQRLYSLLDR
FRLSTVQDSL SPLPPVTSHP LDGDGHTSLE TVSPDKDWYL QLVRSQCWTR SDSALLEGAE
LVNRIPAEDM NDFMMSSEFN LSLLAPCLSL GMSEIANGQK SPLFEAARGV ILNRVTSVVQ
QLPAVHQVFQ PFLPIEPTAY WNKLNDLLGD TTSYQSLTIL ARALAQYLVV LSKVPAHLHL
PPEKEGDTVK FVVMTVEALS WHLIHEQIPL SLDLQAGLDC CCLALQVPGL WGVLSSPEYV
THACSLIHCV RFILEAIAVQ PGDQLLGPES RSHTPRAVRK EEVDSDIQNL SHVTSACEMV
ADMVESLQSV LALGHKRNST LPSFLTAVLK NIVISLARLP LVNSYTRVPP LVWKLGWSPK
PGGDFGTVFP EIPVEFLQEK EILKEFIYRI NTLGWTNRTQ FEETWATLLG VLVTQPLVME
QEESPPEEDT ERTQIHVLAV QAITSLVLSA MTVPVAGNPA VSCLEQQPRN KPLKALDTRF
GRKLSMIRGI VEQEIQEMVS QRENTATHHS HQAWDPVPSL LPATTGALIS HDKLLLQINP
EREPGNMSYK LGQVSIHSVW LGNNITPLRE EEWDEEEEEE SDVPAPTSPP VSPVNSRKHR
AGVDIHSCSQ FLLELYSRWI LPSSAARRTP VILISEVVRS LLVVSDLFTE RTQFEMMYLT
LTELRRVHPS EDEILIQYLV PATCKAAAVL GMDKTVAEPV SRLLESTLRS SHLPSQIGAL
HGILYVLECD LLDDTAKQLI PVVSDYLLSN LKGIAHCVNI HSQQHVLVMC ATAFYLMENY
PLDVGPEFSA SVIQMCGVML SGSEESTPSI IYHCALRGLE RLLLSEQLSR LDTESLVKLS
VDRVNVQSPH RAMAALGLML TCMYTGKEKA SPGRASDPSP ATPDSESVIV AMERVSVLFD
RIRKGFPCEA RVVARILPQF LDDFFPPQDV MNKVIGEFLS NQQPYPQFMA TVVYKVFQTL
HSAGQSSMVR DWVMLSLSNF TQRTPVAMAM WSLSCFLVSA STSPWVSAIL PHVISRMGKL
EQVDVNLFCL VATDFYRHQI EEEFDRRAFQ SVFEVVAAPG SPYHRLLACL QNVHKVTTC


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