HD_RAT
ID HD_RAT Reviewed; 3110 AA.
AC P51111;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Huntingtin;
DE AltName: Full=Huntington disease protein homolog;
DE Short=HD protein homolog;
DE Contains:
DE RecName: Full=Huntingtin, myristoylated N-terminal fragment {ECO:0000250|UniProtKB:P42858};
GN Name=Htt; Synonyms=Hd, Hdh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8528205; DOI=10.1093/hmg/4.7.1173;
RA Schmitt I., Baechner D., Megow D., Henklein P., Boulter J., Hameister H.,
RA Epplen J.T., Riess O.;
RT "Expression of the Huntington disease gene in rodents: cloning the rat
RT homologue and evidence for downregulation in non-neuronal tissues during
RT development.";
RL Hum. Mol. Genet. 4:1173-1182(1995).
RN [2]
RP PROTEIN SEQUENCE OF 356-384; 429-441; 767-795; 1760-1772; 1832-1838 AND
RP 2875-2898, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1773-1926.
RC TISSUE=Brain;
RX PubMed=8275091; DOI=10.1038/ng1193-259;
RA Strong T.V., Tagle D.A., Valdes J.M., Elmer L.W., Boehm K., Swaroop M.,
RA Kaatz K.W., Collins F.S., Albin R.L.;
RT "Widespread expression of the human and rat Huntington's disease gene in
RT brain and nonneural tissues.";
RL Nat. Genet. 5:259-265(1993).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: [Huntingtin]: May play a role in microtubule-mediated
CC transport or vesicle function. {ECO:0000250|UniProtKB:P42858}.
CC -!- FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the
CC formation of autophagic vesicles. {ECO:0000250|UniProtKB:P42858}.
CC -!- SUBUNIT: Interacts with PFN1. Interacts through its N-terminus with
CC PRPF40A. Interacts with PQBP1. Interacts with SETD2. Interacts with
CC SH3GLB1. Interacts with SYVN. Interacts with TPR; the interaction is
CC inhibited by forms of Huntingtin with expanded polyglutamine stretch.
CC Interacts with ZDHHC13 (via ANK repeats). Interacts with ZDHHC17 (via
CC ANK repeats). Interacts with F8A1/F8A2/F8A3 (By similarity). Found in a
CC complex with F8A1/F8A2/F8A3, HTT and RAB5A; mediates the recruitment of
CC HTT by RAB5A (By similarity). {ECO:0000250|UniProtKB:P42858,
CC ECO:0000250|UniProtKB:P42859}.
CC -!- INTERACTION:
CC P51111; P29994: Itpr1; NbExp=4; IntAct=EBI-9674649, EBI-8614640;
CC -!- SUBCELLULAR LOCATION: [Huntingtin]: Cytoplasm
CC {ECO:0000250|UniProtKB:P42858}. Nucleus {ECO:0000250|UniProtKB:P42858}.
CC Note=Shuttles between cytoplasm and nucleus in a Ran GTPase-independent
CC manner. {ECO:0000250|UniProtKB:P42858}.
CC -!- SUBCELLULAR LOCATION: [Huntingtin, myristoylated N-terminal fragment]:
CC Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:P42858}.
CC -!- TISSUE SPECIFICITY: Expressed to a high degree in all the regions of
CC the brain of adults and in meiotic cells of the testis. In addition,
CC very low levels are detected in various non-neuronal tissues (heart,
CC muscle, liver, lung and kidney).
CC -!- DEVELOPMENTAL STAGE: Identified at high levels in neuronal tissues of
CC embryos as early as day 14.5. This expression remains constant in all
CC further development stages (up to the adult). On the other hand the
CC expression in non-neuronal tissues is down-regulated from stage 17.5
CC day old embryos.
CC -!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
CC conformational flexibility and is likely to exist in a fluctuating
CC equilibrium of alpha-helical, random coil, and extended conformations.
CC {ECO:0000250|UniProtKB:P42858}.
CC -!- PTM: Phosphorylation at Ser-1150 and Ser-1170 by CDK5 in response to
CC DNA damage in nuclei of neurons protects neurons against polyglutamine
CC expansion as well as DNA damage mediated toxicity.
CC {ECO:0000250|UniProtKB:P42858}.
CC -!- PTM: [Huntingtin]: Cleaved by caspases downstream of the polyglutamine
CC stretch. {ECO:0000250|UniProtKB:P42858}.
CC -!- PTM: [Huntingtin, myristoylated N-terminal fragment]: Myristoylated at
CC Gly-522, following proteolytic cleavage at Asp-521.
CC {ECO:0000250|UniProtKB:P42858}.
CC -!- POLYMORPHISM: The poly-Gln region does not appear to be polymorphic,
CC explaining the absence of a rodent HD-like disorder.
CC {ECO:0000305|PubMed:8528205}.
CC -!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18650; AAA90987.1; ALT_SEQ; mRNA.
DR EMBL; U01022; AAC52133.1; -; mRNA.
DR PIR; S40522; S40522.
DR SMR; P51111; -.
DR CORUM; P51111; -.
DR IntAct; P51111; 1.
DR STRING; 10116.ENSRNOP00000054971; -.
DR ChEMBL; CHEMBL2439943; -.
DR iPTMnet; P51111; -.
DR PhosphoSitePlus; P51111; -.
DR jPOST; P51111; -.
DR PaxDb; P51111; -.
DR PeptideAtlas; P51111; -.
DR PRIDE; P51111; -.
DR RGD; 68337; Htt.
DR eggNOG; ENOG502QR1D; Eukaryota.
DR InParanoid; P51111; -.
DR PhylomeDB; P51111; -.
DR PRO; PR:P51111; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016234; C:inclusion body; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0050809; F:diazepam binding; ISO:RGD.
DR GO; GO:0034452; F:dynactin binding; ISO:RGD.
DR GO; GO:0045505; F:dynein intermediate chain binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:0005522; F:profilin binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0009653; P:anatomical structure morphogenesis; ISO:RGD.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0008088; P:axo-dendritic transport; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; ISO:RGD.
DR GO; GO:0007417; P:central nervous system development; IEP:RGD.
DR GO; GO:0000052; P:citrulline metabolic process; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:RGD.
DR GO; GO:0016197; P:endosomal transport; ISO:RGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:RGD.
DR GO; GO:0007369; P:gastrulation; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR GO; GO:0042445; P:hormone metabolic process; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0055072; P:iron ion homeostasis; ISO:RGD.
DR GO; GO:0019244; P:lactate biosynthetic process from pyruvate; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0099111; P:microtubule-based transport; IBA:GO_Central.
DR GO; GO:0006839; P:mitochondrial transport; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0051028; P:mRNA transport; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IMP:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0021990; P:neural plate formation; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0021988; P:olfactory lobe development; ISO:RGD.
DR GO; GO:0048341; P:paraxial mesoderm formation; ISO:RGD.
DR GO; GO:0030072; P:peptide hormone secretion; ISO:RGD.
DR GO; GO:1905337; P:positive regulation of aggrephagy; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISO:RGD.
DR GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISO:RGD.
DR GO; GO:1904504; P:positive regulation of lipophagy; ISO:RGD.
DR GO; GO:1905505; P:positive regulation of motile cilium assembly; ISO:RGD.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISO:RGD.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0019805; P:quinolinate biosynthetic process; ISO:RGD.
DR GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; ISO:RGD.
DR GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:1904580; P:regulation of intracellular mRNA localization; IMP:RGD.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0021756; P:striatum development; ISO:RGD.
DR GO; GO:0000050; P:urea cycle; ISO:RGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR GO; GO:0042297; P:vocal learning; ISO:RGD.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000091; Huntingtin.
DR InterPro; IPR028426; Huntingtin_fam.
DR InterPro; IPR024613; Huntingtin_middle-repeat.
DR PANTHER; PTHR10170; PTHR10170; 1.
DR Pfam; PF12372; DUF3652; 1.
DR PRINTS; PR00375; HUNTINGTIN.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW Lipoprotein; Myristate; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..3110
FT /note="Huntingtin"
FT /id="PRO_0000083944"
FT CHAIN 522..555
FT /note="Huntingtin, myristoylated N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT /id="PRO_0000447488"
FT REPEAT 174..211
FT /note="HEAT 1"
FT REPEAT 216..253
FT /note="HEAT 2"
FT REPEAT 773..810
FT /note="HEAT 3"
FT REPEAT 873..911
FT /note="HEAT 4"
FT REPEAT 1395..1432
FT /note="HEAT 5"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..473
FT /note="Interaction with ZDHHC17"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT REGION 487..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2601..2628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2363..2372
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 482..483
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT SITE 499..500
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT SITE 521..522
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT SITE 555..556
FT /note="Cleavage; by caspase-6"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 2
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 313
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42859"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42859"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 412
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 1150
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 1170
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 1845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT LIPID 522
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
SQ SEQUENCE 3110 AA; 343762 MW; 33C357E8FC141550 CRC64;
MKAFESLKSF QQQQQQQQPP PQPPPPPPPP PQPPQPPPQG QPPPPPPLPG PAEEPLHRPK
KELSATKKDR VNHCLTICEN IVAQSLRNSP EFQKLLGIAM ELFLLCSDDA SRRRMVADEC
LNKVIKALMD SNLPRLQLEL YKEIKKNGAP RSLRAALWRF AELAHLVRPQ KCRPYLVNLL
PCLTRTSKRP EESVQETLAA AVPKIMASFG NFANDNEIKV LLKAFIANLK SSSPTVRRTA
AGSAVSICQH SRRTQYFYNW LLNVLLGLLV PMEEDHPTLL ILGVLLTLRC LVPLLQQQVK
DTSLKGSFGV TRKEMEVSPS AEQLVQVYEL TLHHTQHQDH NVVTGALELL QQLFRTPPPE
LLQALTTPGG LGQLTLVREE AGGRGRSGSI VELLAGGGSS CSPVLSRKQK GKVLLGEEEA
LEDDSESRSD VSSSAFAASV KSEIGGELAA SSSGVSTPGS VGHDIITEQP RSQHTLQADS
VDLSGCDLTS AATDGDEEDI LSHSSSQFSA VPSDPAMDLN DGTQASSPIS DSSQTTTEGP
DSAVTPSDSS EIVLDGADSQ YLGVQIGQPQ EEDREAAGVL SGEVSDVFRN SSLALQQAHL
LERMGHSRQP SDSSVDKFVS KDEVAEAGDP ESKPCRIKGD IGQPNDDDSA PLVHCVRLLS
ASFLLTGEKK ALVPDRDVRV SVKALALSCI GAAVALHPES FFSKLYKVPL STMESTEEQY
VSDILNYIDH GDPQVRGATA ILCGTLVYSI LSRSRLRVGD WLGTIRALTG NTFSLVDCIP
LLQKTLKDES SVTCKLACTA VRHCVLSLCS SSYSDLGLQL LIDMLPLKNS SYWLVRTELL
ETLAEIDFRL VSFLEAKAES LHRGPHHYTG FLKLQERVLN NVVIYLLGDE DPRVRHVAAT
TLTRLVPKLF YKCDQGQADP VEAVARDQSS VYLKLLMHET QPPSHFSVST ITRIYRGYSL
LPSVTDVTME NNLSRVVAAV SHELITSTTR ALTFGCCEAL CVLSAAFPVC TWSLGWHCGV
PPLSASDESR KSCTVGMASM ILTLLSSAWF PLDLSAIQDA LILAGNLLAA SAPKSLRSSW
ASEEEGSSAA TRQEEIWPAL GDRTLVPMVE QLFSHLLKVI NICAHVLDDE TPGPAIKAAL
PSLTNPPSLS PIRRKGKEKE PGEQTSTPMS PKKGGEASTA SRQSDTSGPV TASKSSSLGS
FYHLPSYLRL HDVLKATHAN YKVTLDLQNS TEKFGGFLRS ALDVLSQILE LATLQDIGKC
VEEVLGYLKS CFSREPMMAT VCVQQLLKTL FGTNLASQFD GLSSNPSKSQ CRAQRLGSSS
VRPGLYHYCF MAPYTHFTQA LADASLRNMV QADQEHDASG WFDVLQKVSA QLKTNLTSVT
KNRADKNAIH NHIRLFEPLV IKALKQYTTT TSVQLQKQVL DLLAQLVQLR VNYCLLDSDQ
VFIGFVLKQF EYIEVGQFRE SEAIIPNIFF FLVLLSYERY HSKQIIGIPK IIQLCDGIMA
SGRKAVTHAI PALQPIVHDL FVLRGTNKAD AGKELETQKE VVVSMLLRLI QYHQVLEMFI
LVLQQCHKEN EDKWKRLSRQ VADIILPMLA KQQMHIDSHE ALGVLNTLFE ILAPSSLRPV
DMLLRSMFIT PSTMASVSTV QLWISGILAI LRVLISQSTE DIVLSRIQEL SFSPYLISCP
VINRLRDGDS NPTLGERSRG KQVKNLPEDT FSRFLLQLVG ILLEDIVTKQ LKVDMSEQQH
TFYCQELGTL LMCLIHIFKS GMFRRITAAA TRLFTSDGCE GSFYTLDSLN ARVRAMVPTH
PALVLLWCQI LLLINHTDHR WWAEVQQTPK RHSLSCTKSL NPQISAEEDS GSAAQLGMCN
REIVRRGALI LFCDYVCQNL HDSEHLTWLI VNHIQDLISL SHEPPVQDFI SAIHRNSAAS
GLFIQAIQSR CENLSTPTTL KKTLQCLEGI HLSQSGAVLT LYVDRLLGTP FRALARMVDT
LACRRVEMLL AANLQSSMAQ LPEEELNRIQ EHLQNTGLAQ RHQRLYSLLD RFRLSTVQDS
LSPLPPVTSH PLDGDGHTSL ETVNPDKDWY LQLVRSQCWT RSDSALLEGA ELVNRIPAED
MSDFMMSSEF NLSLFAPCLS LGMSEIAGSQ KSPLFEAARR VTLDRVTNVV QQLPAVHQVF
QPFLPTEPTA YWSKLNDLFG DTTSYQSLTT LARALAQYLV VLSKVPAPLH LPPEKEGHTV
KFVVMTLEAL SWHLIHEQIP LSLDLQAGLD CCCLALQVPG LWGVLSSPEY VTHTCSLIHC
VRFILEAIAV QPGDQLLGPE SRSHTPRAVR KEEVDSDIQN LSHITSACEM VADMVESLQS
VLALGHKRNS TLPSFLTAVL KNIVVSLARL PLVNSYTRVP PLVWKLGWSP KPGGDFGTVF
PEIPVEFLQE KEVLKEFIYR INTLGWTSRT QFEETWATLL GVLVTQPLVM EQEESPPEED
TERTQIHVLA VQAITSLVLS AMAVPVAGNP AVSCLEQQPR NKPLKALDTR FGRKLSMIRG
IVEQEIQEMV SQRENTATHH SHQAWDPVPS LLPATTGALI SHDKLLLQIN SEREPGNMSY
KLGQVSIHSV WLGNNITPLR EEEWDEEEEE EADAPAPTSP PVSPVNSRKH RAGVDIHSCS
QFLLELYSRW ILPSSAARRT PVILISEVVR SLLVVSDLFT DVPQFEMMYL TLTELRRVHP
SEDEILIQYL VPATCKAAAV LGMDKTVAEP VSRLLESTLR STHLPSQIGA LHGILYVLEC
DLLDDTVKQL IPVVSDYLLS NLKGIAHCVN IHSQQHVLVM CATAFYLMEN YPLDVGPEFS
ASVIQMCGVM LSGSEESTPS VIYHCALRGL ERLLLSEQLS RLDTESLVKL SVDRVNVQSP
HRAMAALGLM LTCMYTGKEK ASPGRASDPS PATPDSESVI VAMERVSVLF DRIRKGFPCE
ARVVARILPQ FLDDFFPPQD VMNKVIGEFL SNQQPYPQFM ATVVYKVFQT LHSAGQSSMV
RDWVMLSLSN FTQRTPVAMA MWSLSCFLVS ASTSPWVSAI LPHVISRMGK LEQVDVNLFC
LVATDFYRHQ IEEEFDRRAF QSVFEVVAAP GSPYHRLLAC LQNVHKVTAC
