ITB4_MOUSE
ID ITB4_MOUSE Reviewed; 1818 AA.
AC A2A863; A2A865; A2A866; Q6PCS0; Q8R3J1; Q91W15;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Integrin beta-4;
DE AltName: CD_antigen=CD104;
DE Flags: Precursor;
GN Name=Itgb4;
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] (ISOFORM 2).
RX PubMed=8359687; DOI=10.1016/0378-1119(93)90421-x;
RA Kennel S.J., Foote L.J., Cimino L., Rizzo M.G., Chang L.Y., Sacchi A.;
RT "Sequence of a cDNA encoding the beta 4 subunit of murine integrin.";
RL Gene 130:209-216(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-1818 (ISOFORM 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1071 AND SER-1470, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
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).
CC -!- FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. It plays a
CC critical structural role in the hemidesmosome of epithelial cells. Is
CC required for the regulation of keratinocyte polarity and motility.
CC ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is
CC essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this
CC binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and
CC this binding is essential for IGF2 signaling.
CC {ECO:0000250|UniProtKB:P16144}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4 associates
CC with alpha-6. Interacts (via cytoplasmic region) with COL17A1 (via
CC cytoplasmic region). Interacts (via cytoplasmic region) with DST
CC isoform 3 (via N-terminus). Interacts (via cytoplasmic domain) with DST
CC (via N-terminus). Interacts with RAC1. ITGA6:ITGB4 is found in a
CC ternary complex with NRG1 and ERBB3. ITGA6:ITGB4 is found in a ternary
CC complex with IGF1 and IGF1R. ITGA6:ITGB4 interacts with IGF2.
CC {ECO:0000250|UniProtKB:P16144}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}. Cell junction, hemidesmosome {ECO:0000250}.
CC Note=Colocalizes with DST at the leading edge of migrating
CC keratinocytes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2A863-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A863-2; Sequence=VSP_037636;
CC Name=3;
CC IsoId=A2A863-3; Sequence=VSP_037636, VSP_037637;
CC -!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and plectin
CC and probably also recruit BP230. {ECO:0000250}.
CC -!- PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-
CC proximal region, enhancing stability and cell surface expression.
CC Palmitoylation also promotes secondary association with tertaspanins
CC (By similarity). {ECO:0000250|UniProtKB:P16144}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006632; AAH06632.1; -; mRNA.
DR EMBL; BC025194; AAH25194.1; -; mRNA.
DR EMBL; BC059192; AAH59192.1; -; mRNA.
DR PIR; JN0786; JN0786.
DR RefSeq; XP_006532635.1; XM_006532572.3. [A2A863-1]
DR RefSeq; XP_006532636.1; XM_006532573.3. [A2A863-3]
DR RefSeq; XP_006532637.1; XM_006532574.2. [A2A863-2]
DR AlphaFoldDB; A2A863; -.
DR SMR; A2A863; -.
DR BioGRID; 228715; 11.
DR ComplexPortal; CPX-3120; integrin alpha6-beta4 complex.
DR IntAct; A2A863; 2.
DR STRING; 10090.ENSMUSP00000102068; -.
DR GlyGen; A2A863; 5 sites.
DR iPTMnet; A2A863; -.
DR PhosphoSitePlus; A2A863; -.
DR MaxQB; A2A863; -.
DR PeptideAtlas; A2A863; -.
DR PRIDE; A2A863; -.
DR ProteomicsDB; 301690; -. [A2A863-1]
DR ProteomicsDB; 301691; -. [A2A863-2]
DR ProteomicsDB; 301692; -. [A2A863-3]
DR Antibodypedia; 3934; 1064 antibodies from 44 providers.
DR DNASU; 192897; -.
DR Ensembl; ENSMUST00000068981; ENSMUSP00000070811; ENSMUSG00000020758. [A2A863-2]
DR Ensembl; ENSMUST00000106458; ENSMUSP00000102066; ENSMUSG00000020758. [A2A863-1]
DR Ensembl; ENSMUST00000106460; ENSMUSP00000102068; ENSMUSG00000020758. [A2A863-3]
DR Ensembl; ENSMUST00000106461; ENSMUSP00000102069; ENSMUSG00000020758. [A2A863-1]
DR GeneID; 192897; -.
DR UCSC; uc007mji.1; mouse. [A2A863-2]
DR CTD; 3691; -.
DR MGI; MGI:96613; Itgb4.
DR VEuPathDB; HostDB:ENSMUSG00000020758; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_237558_0_0_1; -.
DR InParanoid; A2A863; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; A2A863; -.
DR TreeFam; TF105392; -.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR BioGRID-ORCS; 192897; 2 hits in 60 CRISPR screens.
DR ChiTaRS; Itgb4; mouse.
DR PRO; PR:A2A863; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A863; protein.
DR Bgee; ENSMUSG00000020758; Expressed in substantia propria of cornea and 127 other tissues.
DR ExpressionAtlas; A2A863; baseline and differential.
DR Genevisible; A2A863; MM.
DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0030056; C:hemidesmosome; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0031994; F:insulin-like growth factor I binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038132; F:neuregulin binding; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0046847; P:filopodium assembly; IMP:MGI.
DR GO; GO:0031581; P:hemidesmosome assembly; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IGI:MGI.
DR GO; GO:0035878; P:nail development; ISO:MGI.
DR GO; GO:0032290; P:peripheral nervous system myelin formation; IGI:MGI.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0043589; P:skin morphogenesis; ISO:MGI.
DR GO; GO:0061450; P:trophoblast cell migration; IMP:MGI.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR012013; Integrin_bsu-4.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 2.
DR PANTHER; PTHR10082:SF42; PTHR10082:SF42; 2.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002513; Integrin_B4; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00237; Calx_beta; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00187; INB; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF141072; SSF141072; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Disulfide bond; Glycoprotein; Integrin; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..1818
FT /note="Integrin beta-4"
FT /id="PRO_0000379078"
FT TOPO_DOM 29..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..1818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..74
FT /note="PSI"
FT DOMAIN 132..310
FT /note="VWFA"
FT REPEAT 458..504
FT /note="I"
FT REPEAT 505..544
FT /note="II"
FT REPEAT 545..583
FT /note="III"
FT REPEAT 584..621
FT /note="IV"
FT DOMAIN 981..1086
FT /note="Calx-beta"
FT DOMAIN 1131..1220
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1224..1323
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1526..1621
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1639..1735
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 195..200
FT /note="Involved in NRG1- and IGF1-binding"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT REGION 458..621
FT /note="Cysteine-rich tandem repeats"
FT REGION 734..751
FT /note="Palmitoylated on several cysteines"
FT /evidence="ECO:0000250"
FT REGION 1115..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 473..475
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1005..1007
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64632"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64632"
FT MOD_RES 1451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1483
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT MOD_RES 1490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64632"
FT MOD_RES 1526
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT MOD_RES 1787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64632"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..457
FT /evidence="ECO:0000250"
FT DISULFID 39..49
FT /evidence="ECO:0000250"
FT DISULFID 42..73
FT /evidence="ECO:0000250"
FT DISULFID 52..62
FT /evidence="ECO:0000250"
FT DISULFID 246..289
FT /evidence="ECO:0000250"
FT DISULFID 425..673
FT /evidence="ECO:0000250"
FT DISULFID 454..459
FT /evidence="ECO:0000250"
FT DISULFID 470..481
FT /evidence="ECO:0000250"
FT DISULFID 478..514
FT /evidence="ECO:0000250"
FT DISULFID 483..492
FT /evidence="ECO:0000250"
FT DISULFID 494..505
FT /evidence="ECO:0000250"
FT DISULFID 520..525
FT /evidence="ECO:0000250"
FT DISULFID 522..553
FT /evidence="ECO:0000250"
FT DISULFID 527..538
FT /evidence="ECO:0000250"
FT DISULFID 559..564
FT /evidence="ECO:0000250"
FT DISULFID 566..575
FT /evidence="ECO:0000250"
FT DISULFID 577..584
FT /evidence="ECO:0000250"
FT DISULFID 598..603
FT /evidence="ECO:0000250"
FT DISULFID 600..650
FT /evidence="ECO:0000250"
FT DISULFID 605..616
FT /evidence="ECO:0000250"
FT DISULFID 628..637
FT /evidence="ECO:0000250"
FT DISULFID 634..708
FT /evidence="ECO:0000250"
FT DISULFID 653..682
FT /evidence="ECO:0000250"
FT VAR_SEQ 1372..1436
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8359687"
FT /id="VSP_037636"
FT VAR_SEQ 1515
FT /note="Q -> QGLPPIWEDGRSRLPLSWTLGSLSRAHMKGVPASRGSPDSIILAGQS
FT AAPSWGT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037637"
FT CONFLICT 17
FT /note="A -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..68
FT /note="EL -> DV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="D -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="P -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="S -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 709..713
FT /note="PPGSF -> LPAPS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="E -> K (in Ref. 3; AAH59192)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="T -> A (in Ref. 1 and 3; AAH06632/AAH59192)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="G -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1105..1107
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="Q -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="E -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1537
FT /note="P -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1552
FT /note="M -> T (in Ref. 1 and 3; AAH06632/AAH25194/
FT AAH59192)"
FT /evidence="ECO:0000305"
FT CONFLICT 1564..1566
FT /note="NGG -> TCV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1590..1592
FT /note="HSY -> YSH (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1653
FT /note="L -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1662..1663
FT /note="RP -> SR (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1744
FT /note="H -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1759
FT /note="V -> M (in Ref. 3; AAH25194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1818 AA; 201650 MW; CA41A7E6B4E20B59 CRC64;
MAGPCCSPWV KLLLLAAMLS ASLPGDLANR CKKAQVKSCT ECIRVDKSCA YCTDELFKER
RCNTQAELLA AGCRGESILV MESSLEITEN TQIDTSLHRS QVSPQGLQVR LRPGEERSFV
FQVFEPLESP VDLYILMDFS NSMSDDLDNL KQMGQNLAKI LRQLTSDYTI GFGKFVDKVS
VPQTDMRPEK LKEPWPNSDP PFSFKNVISL TENVEEFWNK LQGERISGNL DAPEGGFDAI
LQTAVCTRDI GWRADSTHLL VFSTESAFHY EADGANVLAG IMNRNDEKCH LDASGAYTQY
KTQDYPSVPT LVRLLAKHNI IPIFAVTNYS YSYYEKLHKY FPVSSLGVLQ EDSSNIVELL
EEAFYRIRSN LDIRALDSPR GLRTEVTSDT LQKTETGSFH IKRGEVGTYN VHLRAVEDID
GTHVCQLAKE DQGGNIHLKP SFSDGLRMDA SVICDVCPCE LQKEVRSARC HFRGDFMCGH
CVCNEGWSGK TCNCSTGSLS DTQPCLREGE DKPCSGHGEC QCGRCVCYGE GRYEGHFCEY
DNFQCPRTSG FLCNDRGRCS MGECVCEPGW TGRSCDCPLS NATCIDSNGG ICNGRGYCEC
GRCHCNQQSL YTDTTCEINY SAIRLGLCED LRSCVQCQAW GTGEKKGRAC DDCPFKVKMV
DELKKAEEVV EYCSFRDEDD DCTYSYNVEG DGSPGPNSTV LVHKKKDCPP GSFWWLIPLL
IFLLLLLALL LLLCWKYCAC CKACLGLLPC CNRGHMVGFK EDHYMLRENL MASDHLDTPM
LRSGNLKGRD TVRWKITNNV QRPGFATHAA STSPTELVPY GLSLRLGRLC TENLMKPGTR
ECDQLRQEVE ENLNEVYRQV SGAHKLQQTK FRQQPNTGKK QDHTIVDTVL LAPRSAKQML
LKLTEKQVEQ GSFHELKVAP GYYTVTAEQD ARGMVEFQEG VELVDVRVPL FIRPEDDDEK
QLLVEAIDVP VGTATLGRRL VNITIIKEQA SGVVSFEQPE YSVSRGDQVA RIPVIRHILD
NGKSQVSYST QDNTAHGHRD YVPVEGELLF HPGETWKELQ VKLLELQEVD SLLRGRQVRR
FQVQLSNPKF GARLGQPSTT TVILGEHDET DRSLINQTLS SPPPPHGDLG APQNPNAKAA
GSRKIHFNWL PPPGKPMGYR VKYWIQGDSE SEAHLLDSKV PSVELTNLYP YCDYEMKVCA
YGAQGEGPYS SLVSCRTHQE VPSEPGRLAF NVVSSTVTQL SWAEPAETNG EITAYEVCYG
LVNEDNRPIG PMKKVLVDNP KNRMLLIENL RESQPYRYTV KARNGAGWGP EREAIINLAT
QPKRPMSIPI IPDIPIVDAQ GGEDYENFLM YSDDVLRSPA SSQRPSVSDD TGCGWKFEPL
LGEELDLRRV TWRLPPELIP RLSASSGRSD EDGSVAGGVE GEGSGWIRGA TPRPPGEHLV
NGRMDFAYPG SANSLHRMTA ANVAYGTHLS PHLSHRVLST SSTLTRDYHS LTRTEHSHSG
TLPRDYSTLT SLSSQDSRGA VGVPDTPTRL VFSALGPTSL KVSWQEPQCD RMLLGYSVEY
QLLNGGEMHR LNIPNPGQTS VVVEDLLPNH SYVFRVRAQS QEGWGREREG VITIESQVHP
QSPLCPLPGS AFTLSTPSAP GPLVFTALSP DSLQLSWERP RRPNGDILGY LVTCEMAQGG
APARTFRVDG DNPESRLTVP GLSENVPYKF KVQARTTEGF GPEREGIITI ESQVGGPFPQ
LGSHSGLFQN PVQSEFSSVT STHSTTTEPF LMDGLTLGTQ RLEAGGSLTR HVTQEFVTRT
LTASGSLSTH MDQQFFQT
