LARG1_MOUSE
ID LARG1_MOUSE Reviewed; 756 AA.
AC Q9Z1M7; Q497S9; Q6P7U2; Q80TW0;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Xylosyl- and glucuronyltransferase LARGE1 {ECO:0000305};
DE EC=2.4.-.- {ECO:0000250|UniProtKB:O95461};
DE AltName: Full=Acetylglucosaminyltransferase-like 1A;
DE AltName: Full=Glycosyltransferase-like protein;
DE AltName: Full=LARGE xylosyl- and glucuronyltransferase 1 {ECO:0000312|MGI:MGI:1342270};
DE Includes:
DE RecName: Full=Alpha-1,3-xylosyltransferase LARGE1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:O95461};
DE Includes:
DE RecName: Full=Beta-1,3-glucuronyltransferase LARGE1 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:25138275, ECO:0000269|PubMed:32975514};
GN Name=Large1 {ECO:0000312|MGI:MGI:1342270}; Synonyms=Kiaa0609, Large;
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].
RC TISSUE=Brain, and Embryo;
RX PubMed=9892679; DOI=10.1073/pnas.96.2.598;
RA Peyrard M., Seroussi E., Sandberg-Nordqvist A.-C., Xie Y.-G., Han F.-Y.,
RA Fransson I., Collins J.E., Dunham I., Kost-Alimova M., Imreh S.,
RA Dumanski J.P.;
RT "The human LARGE gene from 22q12.3-q13.1 is a new, distinct member of the
RT glycosyltransferase gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:598-603(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Embryonic stem cell, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP DISEASE.
RX PubMed=11381262; DOI=10.1038/88865;
RA Grewal P.K., Holzfeind P.J., Bittner R.E., Hewitt J.E.;
RT "Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan
RT in the myodystrophy mouse.";
RL Nat. Genet. 28:151-154(2001).
RN [5]
RP INTERACTION WITH DAG1.
RX PubMed=15210115; DOI=10.1016/j.cell.2004.06.003;
RA Kanagawa M., Saito F., Kunz S., Yoshida-Moriguchi T., Barresi R.,
RA Kobayashi Y.M., Muschler J., Dumanski J.P., Michele D.E., Oldstone M.B.,
RA Campbell K.P.;
RT "Molecular recognition by LARGE is essential for expression of functional
RT dystroglycan.";
RL Cell 117:953-964(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15958417; DOI=10.1093/glycob/cwi094;
RA Grewal P.K., McLaughlan J.M., Moore C.J., Browning C.A., Hewitt J.E.;
RT "Characterization of the LARGE family of putative glycosyltransferases
RT associated with dystroglycanopathies.";
RL Glycobiology 15:912-923(2005).
RN [7]
RP FUNCTION, AND PATHWAY.
RX PubMed=15184894; DOI=10.1038/nm1059;
RA Barresi R., Michele D.E., Kanagawa M., Harper H.A., Dovico S.A., Satz J.S.,
RA Moore S.A., Zhang W., Schachter H., Dumanski J.P., Cohn R.D., Nishino I.,
RA Campbell K.P.;
RL Nat. Med. 10:696-703(2004).
RN [8]
RP FUNCTION.
RX PubMed=23125099; DOI=10.1093/glycob/cws152;
RA Inamori K., Hara Y., Willer T., Anderson M.E., Zhu Z.,
RA Yoshida-Moriguchi T., Campbell K.P.;
RT "Xylosyl- and glucuronyltransferase functions of LARGE in alpha-
RT dystroglycan modification are conserved in LARGE2.";
RL Glycobiology 23:295-302(2013).
RN [9]
RP FUNCTION.
RX PubMed=23135544; DOI=10.1093/glycob/cws153;
RA Ashikov A., Buettner F.F., Tiemann B., Gerardy-Schahn R., Bakker H.;
RT "LARGE2 generates the same xylose- and glucuronic acid-containing glycan
RT structures as LARGE.";
RL Glycobiology 23:303-309(2013).
RN [10]
RP FUNCTION, AND PATHWAY.
RX PubMed=24132234; DOI=10.1038/nature12605;
RA Goddeeris M.M., Wu B., Venzke D., Yoshida-Moriguchi T., Saito F.,
RA Matsumura K., Moore S.A., Campbell K.P.;
RT "LARGE glycans on dystroglycan function as a tunable matrix scaffold to
RT prevent dystrophy.";
RL Nature 503:136-140(2013).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25138275; DOI=10.1074/jbc.m114.597831;
RA Inamori K., Willer T., Hara Y., Venzke D., Anderson M.E., Clarke N.F.,
RA Guicheney P., Bonnemann C.G., Moore S.A., Campbell K.P.;
RT "Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for
RT functional modification of alpha-dystroglycan in cells and tissues.";
RL J. Biol. Chem. 289:28138-28148(2014).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32975514; DOI=10.7554/elife.61388;
RA Walimbe A.S., Okuma H., Joseph S., Yang T., Yonekawa T., Hord J.M.,
RA Venzke D., Anderson M.E., Torelli S., Manzur A., Devereaux M., Cuellar M.,
RA Prouty S., Ocampo Landa S., Yu L., Xiao J., Dixon J.E., Muntoni F.,
RA Campbell K.P.;
RT "POMK regulates dystroglycan function via LARGE1-mediated elongation of
RT matriglycan.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Bifunctional glycosyltransferase with both alpha-1,3-
CC xylosyltransferase and beta-1,3-glucuronyltransferase activities
CC involved in the maturation of alpha-dystroglycan (DAG1) by
CC glycosylation leading to DAG1 binding to laminin G-like domain-
CC containing extracellular proteins with high affinity (PubMed:23125099,
CC PubMed:23135544, PubMed:25138275, PubMed:32975514). Elongates the
CC glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated
CC by B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-]
CC to produce a heteropolysaccharide (By similarity). Requires the
CC phosphorylation of core M3 (O-mannosyl trisaccharide) by POMK to
CC elongate the glucuronyl-beta-1,4-xylose-beta disaccharide primer
CC (PubMed:32975514). Plays a key role in skeletal muscle function and
CC regeneration (PubMed:15184894, PubMed:24132234).
CC {ECO:0000250|UniProtKB:O95461, ECO:0000269|PubMed:15184894,
CC ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:23135544,
CC ECO:0000269|PubMed:24132234, ECO:0000269|PubMed:25138275,
CC ECO:0000269|PubMed:32975514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-
CC beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-
CC [protein] + UDP-alpha-D-xylose = 3-O-[alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-
CC beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:57336, Rhea:RHEA-COMP:17482, Rhea:RHEA-COMP:17483,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177336, ChEBI:CHEBI:177352;
CC Evidence={ECO:0000250|UniProtKB:O95461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57337;
CC Evidence={ECO:0000250|UniProtKB:O95461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-
CC D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-
CC (1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-alpha-D-glucuronate =
CC 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-
CC beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-
CC GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:67924, Rhea:RHEA-COMP:17484, Rhea:RHEA-COMP:17486,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177354, ChEBI:CHEBI:177355;
CC Evidence={ECO:0000269|PubMed:25138275, ECO:0000269|PubMed:32975514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67925;
CC Evidence={ECO:0000269|PubMed:25138275, ECO:0000305|PubMed:32975514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-
CC alpha-D-xylose = 3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->](n+1)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+)
CC + UDP; Xref=Rhea:RHEA:68368, Rhea:RHEA-COMP:17485, Rhea:RHEA-
CC COMP:17486, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177354, ChEBI:CHEBI:177355;
CC Evidence={ECO:0000250|UniProtKB:O95461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68369;
CC Evidence={ECO:0000250|UniProtKB:O95461};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O95461};
CC Note=Binds 2 Mn(2+) ions per subunit. The xylosyltransferase part binds
CC one Mn(2+) and the beta-1,3-glucuronyltransferase part binds one
CC Mn(2+). {ECO:0000250|UniProtKB:O95461};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:15184894, ECO:0000269|PubMed:24132234}.
CC -!- SUBUNIT: Interacts with DAG1 (via the N-terminal domain of alpha-DAG1);
CC the interaction increases binding of DAG1 to laminin (PubMed:15210115).
CC Interacts with B4GAT1. {ECO:0000250|UniProtKB:O95461,
CC ECO:0000269|PubMed:15210115}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O95461}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O95461}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in heart, diaphragm
CC and brain, where it is especially found in cerebral cortex,
CC hippocampus, and trigeminal ganglion. {ECO:0000269|PubMed:15958417}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously found at 14.5 dpc with strong
CC expression in heart, central nervous system structures such as cerebral
CC cortex, hippocampus, olfactory lobe, trigeminal ganglion and spinal
CC cord. Also expressed in diaphragm and duodenum.
CC -!- DISEASE: Note=Defects in Large are the cause of myodystrophy (myd), an
CC autosomal recessive neuromuscular phenotype, probably due to abnormal
CC post-translational modification of alpha-dystroglycan.
CC {ECO:0000269|PubMed:15958417}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glycosyltransferase 49 family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61506.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65610.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Large
CC like-glycosyltransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_589";
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DR EMBL; AJ006278; CAA06945.1; -; mRNA.
DR EMBL; AK122328; BAC65610.1; ALT_FRAME; mRNA.
DR EMBL; BC061506; AAH61506.1; ALT_INIT; mRNA.
DR EMBL; BC100399; AAI00400.1; -; mRNA.
DR CCDS; CCDS22420.1; -.
DR RefSeq; NP_001304320.1; NM_001317391.1.
DR RefSeq; NP_034817.1; NM_010687.2.
DR AlphaFoldDB; Q9Z1M7; -.
DR SMR; Q9Z1M7; -.
DR STRING; 10090.ENSMUSP00000112617; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyGen; Q9Z1M7; 4 sites.
DR PhosphoSitePlus; Q9Z1M7; -.
DR MaxQB; Q9Z1M7; -.
DR PaxDb; Q9Z1M7; -.
DR PRIDE; Q9Z1M7; -.
DR ProteomicsDB; 265041; -.
DR Antibodypedia; 25305; 169 antibodies from 29 providers.
DR DNASU; 16795; -.
DR Ensembl; ENSMUST00000004497; ENSMUSP00000004497; ENSMUSG00000004383.
DR Ensembl; ENSMUST00000119826; ENSMUSP00000112617; ENSMUSG00000004383.
DR Ensembl; ENSMUST00000212459; ENSMUSP00000148336; ENSMUSG00000004383.
DR GeneID; 16795; -.
DR KEGG; mmu:16795; -.
DR UCSC; uc009mgs.1; mouse.
DR CTD; 9215; -.
DR MGI; MGI:1342270; Large1.
DR VEuPathDB; HostDB:ENSMUSG00000004383; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000158497; -.
DR HOGENOM; CLU_019238_3_2_1; -.
DR InParanoid; Q9Z1M7; -.
DR OMA; WNIQLSD; -.
DR OrthoDB; 729091at2759; -.
DR PhylomeDB; Q9Z1M7; -.
DR TreeFam; TF319168; -.
DR BRENDA; 2.4.1.B80; 3474.
DR BRENDA; 2.4.2.B18; 3474.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 16795; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Large1; mouse.
DR PRO; PR:Q9Z1M7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9Z1M7; protein.
DR Bgee; ENSMUSG00000004383; Expressed in decidua and 262 other tissues.
DR ExpressionAtlas; Q9Z1M7; baseline and differential.
DR Genevisible; Q9Z1M7; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:MGI.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0042285; F:xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; NAS:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; IDA:UniProtKB.
DR GO; GO:0060538; P:skeletal muscle organ development; IDA:UniProtKB.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese;
KW Membrane; Metal-binding; Multifunctional enzyme; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..756
FT /note="Xylosyl- and glucuronyltransferase LARGE1"
FT /id="PRO_0000206061"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..756
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 43..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..413
FT /note="Xylosyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT REGION 414..756
FT /note="Glucuronyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT COILED 53..95
FT /evidence="ECO:0000255"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT BINDING 563
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT BINDING 565
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 269
FT /note="L -> S (in Ref. 3; AAI00400)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="L -> H (in Ref. 3; AAI00400)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="D -> N (in Ref. 3; AAI00400)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="K -> E (in Ref. 3; AAI00400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 87964 MW; 37B32E039AB8895F CRC64;
MLGICRGRRK FLAASLTLLC IPAITWIYLF AGSFEDGKPV SLSPLESQAH SPRYTASSQR
ERESLEVRVR EVEEENRALR RQLSLAQGQS PAHHRGNHSK TYSMEEGTGD SENLRAGIVA
GNSSECGQQP AVEKCETIHV AIVCAGYNAS RDVVTLVKSV LFHRRNPLHF HLIADSIAEQ
ILATLFQTWM VPAVRVDFYN ADELKSEVSW IPNKHYSGIY GLMKLVLTKT LPANLERVIV
LDTDITFATD IAELWAVFHK FKGQQVLGLV ENQSDWYLGN LWKNHRPWPA LGRGYNTGVI
LLLLDKLRKM KWEQMWRLTA ERELMGMLST SLADQDIFNA VIKQNPFLVY QLPCFWNVQL
SDHTRSEQCY RDVSDLKVIH WNSPKKLRVK NKHVEFFRNL YLTFLEYDGN LLRRELFGCP
SETDVNNENL QKQLSELDED DLCYEFRRER FTVHRTHLYF LHYEFEPSAD NTDVTLVAQL
SMDRLQMLEA ICKHWEGPIS LALYLSDAEA QQFLRYAQGS EVLMSRQNVG YHIVYKEGQF
YPVNLLRNVA MKHISTPYMF LSDIDFLPMY GLYEYLRKSV IQLDLANTKK AMIVPAFETL
RYRLSFPKSK AELLSMLDMG TLFTFRYHVW TKGHAPTNFA KWRTATTPYQ VEWEADFEPY
VVVRRDCPEY DRRFVGFGWN KVAHIMELDA QEYEFTVLPN AYMIHMPHAP SFDITKFRSN
KQYRICLKTL KEEFQQDMSR RYGFAALKYL TAENNS
