UTRN_RAT
ID UTRN_RAT Reviewed; 3419 AA.
AC G3V7L1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Utrophin {ECO:0000305};
DE AltName: Full=Dystrophin-related protein 1;
DE Short=DRP-1;
GN Name=Utrn {ECO:0000312|RGD:3947};
GN ORFNames=rCG_57340 {ECO:0000312|EMBL:EDL93719.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PGM5.
RX PubMed=7890770; DOI=10.1074/jbc.270.11.6328;
RA Belkin A.M., Burridge K.;
RT "Association of aciculin with dystrophin and utrophin.";
RL J. Biol. Chem. 270:6328-6337(1995).
RN [4]
RP INTERACTION WITH DTNB.
RX PubMed=10545507; DOI=10.1083/jcb.147.3.645;
RA Blake D.J., Hawkes R., Benson M.A., Beesley P.W.;
RT "Different dystrophin-like complexes are expressed in neurons and glia.";
RL J. Cell Biol. 147:645-658(1999).
RN [5] {ECO:0007744|PubMed:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [6] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY 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: May play a role in anchoring the cytoskeleton to the plasma
CC membrane. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with the syntrophins SNTA1; SNTB1 and
CC SNTB2. Interacts with SYNM. Interacts (via its WWW and ZZ domains) with
CC DAG1 (via the PPXY motif of betaDAG1); the interaction is inhibited by
CC the tyrosine phosphorylation of the PPXY motif of DAG1 (By similarity).
CC Interacts with DTNB (PubMed:10545507). Interacts with PGM5
CC (PubMed:7890770). {ECO:0000250|UniProtKB:P46939,
CC ECO:0000269|PubMed:10545507, ECO:0000269|PubMed:7890770}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P46939}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P46939}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P46939}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P46939}. Note=Neuromuscular junction.
CC {ECO:0000250|UniProtKB:P46939}.
CC -!- DOMAIN: Actin binding affinity is primarily determined by CH domain 1.
CC {ECO:0000250|UniProtKB:P46939}.
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DR EMBL; AABR07000248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07000256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473994; EDL93719.1; -; Genomic_DNA.
DR RefSeq; XP_008756815.1; XM_008758593.1.
DR RefSeq; XP_008756816.1; XM_008758594.2.
DR SMR; G3V7L1; -.
DR IntAct; G3V7L1; 1.
DR STRING; 10116.ENSRNOP00000016273; -.
DR jPOST; G3V7L1; -.
DR PaxDb; G3V7L1; -.
DR PeptideAtlas; G3V7L1; -.
DR PRIDE; G3V7L1; -.
DR Ensembl; ENSRNOT00000016273; ENSRNOP00000016273; ENSRNOG00000011058.
DR GeneID; 25600; -.
DR CTD; 7402; -.
DR RGD; 3947; Utrn.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000153467; -.
DR HOGENOM; CLU_000246_2_0_1; -.
DR InParanoid; G3V7L1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR ExpressionAtlas; G3V7L1; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:RGD.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0017166; F:vinculin binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IDA:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEP:RGD.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 9.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035436; Dystrophin/utrophin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 8.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 20.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Membrane; Metal-binding; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Zinc;
KW Zinc-finger.
FT CHAIN 1..3419
FT /note="Utrophin"
FT /id="PRO_0000452823"
FT DOMAIN 31..135
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 150..255
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 312..416
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 421..525
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 532..636
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 690..795
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 801..901
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 910..1012
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 1019..1121
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1128..1229
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1236..1333
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1335..1436
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1438..1540
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1547..1648
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1653..1747
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1748..1840
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1841..1958
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1969..2070
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 2077..2176
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 2216..2319
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2336..2426
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2433..2542
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT REPEAT 2549..2674
FT /note="Spectrin 21"
FT /evidence="ECO:0000255"
FT REPEAT 2681..2783
FT /note="Spectrin 22"
FT /evidence="ECO:0000255"
FT DOMAIN 2799..2832
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 3052..3108
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..246
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT REGION 268..905
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT REGION 1336..1761
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT REGION 2616..2640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2785..3152
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT REGION 3277..3296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3344..3395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2620..2640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3344..3373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3057
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3060
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3081
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3084
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 4
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT MOD_RES 1998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT MOD_RES 2201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46939"
FT MOD_RES 3284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46939"
SQ SEQUENCE 3419 AA; 391312 MW; 9A4F88AA71A6E4D5 CRC64;
MAKYGHLEAS PDDGQNQFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPINDMFSDL
KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVELVNI GGTDIVDGNP
KLTLGLLWSI ILHWQVKDVM KDIMSDLQQT NSEKILLSWV RQTTRPYSQV NVLNFTTSWT
DGLAFNAVLH RHKPDLFSWD RVVKMSPTER LEHAFSKAHT YLGIEKLLDP EDVAVQLPDK
KSIIMYLTSL FEVLPQQVTI DAIREVETLP RKYKKECEGE EINIQSAVLT EEGQSPRAET
PSTVTEVDMD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEDVKEQFA THETFMMELT
AHQSSVGSVL QAGNQLMTQG TLSDEEEFEI QEQMTLLNAR WEALRVESME RQSRLHDALM
ELQKKQLQQL SGWLTLTEER IQKMESLPVG DDLPSLQNLL EEHKSLQSDL EAEQVKVNSL
THMVVIVDEN SGESATAVLE DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL
LEAWLTEKEE ALNKVQTGNF KDQKELGVSV RRLAILKEDM EMKRQTLDQL SEIGQDVGQL
LSNPKASEKM NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK DLLETVHVRE
QGMIKKPKQE LPPPPPPKKR QIHVDVEAKK KFDATSAELQ SWILRSKAAL QNTEMNEYKK
SQETSGVRKK WKGLEKEQKE KIPQLDELNQ TGQILQEQMG KEGLLAEEIN DVLERVLLEW
KMISQQLEDL GRKIQLQEDI NAYFRQLDAL EKTIRAKEEW LRDASFSESP QRSLPSLKDS
CQRELTDLLG LHPRIEILCA SCSALRSQPS VPGFVQQGFD DLRRHYQAVQ KALEEYQQQL
ENELKSQPEP AYLDTLNTLK KMLSESEKAA QASLSALNDP SAVEQALQEK KALDETLENQ
KPTLHKLSEE TKALEKNMLP DVGKTYRQEF DDAQGKWNKV KTKVSRDLRS LEEIIPRLRD
FKADSEVIEK WTNGVKDFLM KEQAAQGDTT ALQRQLDQCT TFANEIETIE SSLKNLRDIE
TSLQRCPVTG VKTWVQTRLA DYQSQLEKFS QEIDIQKSRL SDSQEKAMNL KKDLAEMQEW
MAQAEEDYLE RDFEYKSPEE LESAVEEMKR AKEDVLQKEV RVKILKDSIK LVAARVPSGG
QELTSEFNEV LESYQLLCNR IRGKCHTLEE VWSCWVELLH YLDLETSWLN TLEERMQSTE
ALPERAEAVH DALESLESVL RHPADNRTQI RELGQTLIDG GILDDIISEK LEAFNSRYEE
LSHLAESKQI SLEKQLQVLR ETDHMLQVLK ESLGELDKQL TTYLTDRIDA FQLPQEAQKI
QAEISAHELT LEELKKNVRP QPPTSPEGRT TRGGSQMDLL QRKLREVSTK FQLFQKPANF
EQRMLDCKRV LDGVKAELHV LSVKDVDPDV IQTHLDKCMK LYKTLSEVKL EVETVIKTGR
HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLSRKLK KEAAILSEWL
STTEAELVQK STSEGVIGDL DTEISWAKNI LKDLERRKVD LNAITESSAA LQHLVVGSES
VLEDTLCVLN AGWSRVRTWT EDWRNTLLNH QNQLEVFDGH VAHISTWLYQ AEALLDEIEK
KPASKQEEIV KRLLSELSDA SIQVENVREQ AIVLVNARGS SSRELVEPKL AELSKNFEKV
SQHINSAQML IGQDPAGTVE AVGPFSDLES LESDIENMLK VVEKHLDPSN DEKMDEERAQ
IEEVLQRGEH LLHEPMEDSK KEKIRLQLLL LHTRYNKIKA IPQRKTIPLS SGIMSSALPA
DYLVEINKIL LTLDDIELSL NIPELNTTVY EDFSFQEDSL KRIKDQLDRL GEQLAAVHEK
QPDVILEASG PEAIQIRDML SQLNAKWDRV NRLYSDRRGS FARAVEEWKQ FHCDLDDLTQ
WLSEAEDLLV GTCAPDGSLD LEKARTHQLE LEDGLSSHQP CLIDVNQKGE DIVQRLRPSD
ASFLKDKLAS LNQRWSALVA EVKDLQPRLK GESKQVSGYR KRLDEVVCWL TKVENAVQKR
STPDPEENPW ELTDLAQEMD AQAENIKWLN RAELEMLSDK NLSLCERDNL SESLRNVNTM
WTKICREVPS LLKTRTQDPC SAPQTRIAAH PNVQKVALVS SASDAPLRGP EISVPADLDK
TITELADWLV LIDQMLKSNI VTVGDVKEIN KTVSRMKITK ADLEQRHPQL DFVFTLAQNL
KNKASSSDLR TAITEKLEKL KTQWESTQHG VELRRQQLED MVVDSLQWDD HREETEELMR
KHEARFYMLQ QARRDPLSKQ VSDNQLLLQE LGSGDGVIMA FDNVLQKLLE EYSSDDTRNV
EETTEYLKTS WINLKQSIAD RQSALEAELR TVQTSRRDLE NFVKWLQEAE TTANVLADAS
QRENALQDSV LARQLRQQML DIQAEIDAHN DIFKSIDGNR QKMVKALGNS EEATMLQHRL
DDMNQRWNDL KAKSASIRAH LEASAEKWNR LLASLEELIK WLNMKDEELK KQMPIGGDVP
ALQLQYDHCK VLRRELKEKE YSVLNAVDQA RVFLADQPIE APEEPRRNPQ SKTELTPEER
AQKIAKAMRK QSSEVREKWE SLNAVTSTWQ KQVGKALEKL RDLQGAVDDL DADMKEVEAV
RNGWKPVGDL LIDSLQDHIE KTLAFREEIA PINLKVKTMN DLSSQLSPLD LHPSPKMSRQ
LDDLNMRWKL LQVSVEDRLK QLQEAHRDFG PSSQHFLSTS VQLPWQRSIS HNKVPYYINH
QTQTTCWDHP KMTELFQSLG DLNNVRFSAY RTAIKIRRLQ KALCLDLLEL NTTNEVFKQH
KLNQNDQLLS VPDVINCLTT TYDGLEQLHK DLVNVPLCVD MCLNWLLNVY DTGRTGKIRV
QSLKIGLMSL SKGLLEEKYR CLFKEVAGPT EMCDQRQLGL LLHDAIQIPR QLGEVAAFGG
SNIEPSVRSC FQQNNNKPEI SVKEFIDWMR LEPQSMVWLP VLHRVAAAET AKHQAKCNIC
KECPIVGFRY RSLKHFNYDV CQSCFFSGRT AKGHKLHYPM VEYCIPTTSG EDVRDFTKVL
KNKFRSKKYF AKHPRLGYLP VQTVLEGDNL ETPITLISMW PEHYDPSQSP QLFHDDTHSR
IEQYATRLAQ MERTNGSFLT DSSSTTGSVE DEHALIQQYC QTLGGESPVS QPQSPAQILK
SVEKEERGEL ERIIADLEEE QRNLQVEYEQ LKEQHLRRGL PLGSPPDSIV SPYHTSEDSE
LIAEAKLLRQ HKGRLEARMQ ILEDHNKQLE SQLHRLRQLL EQPDSDSRIN GVSPWASPQH
PSLSYSLDPD PGPQSHQAAS EDLLAPPHDT STDLTDVMEQ LNSTFPSCSP NVPSRPQAI
