EXT1_MOUSE
ID EXT1_MOUSE Reviewed; 746 AA.
AC P97464; Q61546;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Exostosin-1;
DE EC=2.4.1.224;
DE EC=2.4.1.225;
DE AltName: Full=Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
DE AltName: Full=Multiple exostoses protein 1 homolog;
GN Name=Ext1;
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 STRAIN=C57BL/6 X CBA;
RX PubMed=9186511; DOI=10.1159/000134536;
RA Lohmann D.R., Buiting K., Luedecke H.-J., Horsthemke B.;
RT "The murine Ext1 gene shows a high level of sequence similarity with its
RT human homologue and is part of a conserved linkage group on chromosome
RT 15.";
RL Cytogenet. Cell Genet. 76:164-166(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=9254013; DOI=10.3109/10425179709034035;
RA Lin X., Wells D.;
RT "Isolation of the mouse cDNA homologous to the human EXT1 gene responsible
RT for hereditary multiple exostoses.";
RL DNA Seq. 7:199-202(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9703997; DOI=10.1006/bbrc.1998.9050;
RA Lin X., Gan L., Klein W.H., Wells D.;
RT "Expression and functional analysis of mouse EXT1, a homolog of the human
RT multiple exostoses type 1 gene.";
RL Biochem. Biophys. Res. Commun. 248:738-743(1998).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9620772; DOI=10.1038/514;
RA McCormick C., Leduc Y., Martindale D., Mattison K., Esford L.E., Dyer A.P.,
RA Tufaro F.;
RT "The putative tumour suppressor EXT1 alters the expression of cell-surface
RT heparan sulfate.";
RL Nat. Genet. 19:158-161(1998).
RN [6]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=10639137; DOI=10.1073/pnas.97.2.668;
RA McCormick C., Duncan G., Goutsos K.T., Tufaro F.;
RT "The putative tumor suppressors EXT1 and EXT2 form a stable complex that
RT accumulates in the Golgi apparatus and catalyzes the synthesis of heparan
RT sulfate.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:668-673(2000).
CC -!- FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-
CC sulfate. The EXT1/EXT2 complex possesses substantially higher
CC glycosyltransferase activity than EXT1 or EXT2 alone. Required for the
CC exosomal release of SDCBP, CD63 and syndecan (By similarity).
CC {ECO:0000250|UniProtKB:Q16394}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-
CC beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-
CC seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D-
CC GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:16213, Rhea:RHEA-COMP:12621,
CC Rhea:RHEA-COMP:12623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416;
CC EC=2.4.1.224; Evidence={ECO:0000305|PubMed:10639137};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-
CC GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-
CC O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n+1)-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:20908, Rhea:RHEA-COMP:12623,
CC Rhea:RHEA-COMP:14295, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416;
CC EC=2.4.1.225; Evidence={ECO:0000305|PubMed:10639137};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Forms a homo/heterooligomeric complex with EXT2. Interacts
CC with NDST1. {ECO:0000250|UniProtKB:Q16394}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9620772, ECO:0000269|PubMed:9703997}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:9620772,
CC ECO:0000269|PubMed:9703997}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:10639137}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q16394}; Single-pass type II membrane
CC protein {ECO:0000255}. Note=The EXT1/EXT2 complex is localized in the
CC Golgi apparatus. {ECO:0000269|PubMed:10639137}.
CC -!- TISSUE SPECIFICITY: Expressed in maturing chondrocytes.
CC -!- DEVELOPMENTAL STAGE: Initially expressed at 6.5 dpc, which coincides
CC with gastrulation of the embryo. High level of expression in developing
CC limb buds at 10.5 to 12.5 dpc. {ECO:0000269|PubMed:9703997}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; U78539; AAB41728.1; -; mRNA.
DR EMBL; X96639; CAA65443.1; -; mRNA.
DR EMBL; BC004741; AAH04741.1; -; mRNA.
DR CCDS; CCDS27466.1; -.
DR RefSeq; NP_034292.2; NM_010162.2.
DR AlphaFoldDB; P97464; -.
DR SMR; P97464; -.
DR BioGRID; 199556; 4.
DR STRING; 10090.ENSMUSP00000076505; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR GlyGen; P97464; 2 sites.
DR iPTMnet; P97464; -.
DR PhosphoSitePlus; P97464; -.
DR CPTAC; non-CPTAC-3915; -.
DR PaxDb; P97464; -.
DR PeptideAtlas; P97464; -.
DR PRIDE; P97464; -.
DR ProteomicsDB; 275805; -.
DR Antibodypedia; 26732; 251 antibodies from 30 providers.
DR DNASU; 14042; -.
DR Ensembl; ENSMUST00000077273; ENSMUSP00000076505; ENSMUSG00000061731.
DR GeneID; 14042; -.
DR KEGG; mmu:14042; -.
DR UCSC; uc007vrh.2; mouse.
DR CTD; 2131; -.
DR MGI; MGI:894663; Ext1.
DR VEuPathDB; HostDB:ENSMUSG00000061731; -.
DR eggNOG; KOG1021; Eukaryota.
DR GeneTree; ENSGT00940000155321; -.
DR HOGENOM; CLU_013906_4_0_1; -.
DR InParanoid; P97464; -.
DR OMA; YHRYYNT; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; P97464; -.
DR TreeFam; TF314231; -.
DR BRENDA; 2.4.1.224; 3474.
DR BRENDA; 2.4.1.225; 3474.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14042; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Ext1; mouse.
DR PRO; PR:P97464; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P97464; protein.
DR Bgee; ENSMUSG00000061731; Expressed in embryonic post-anal tail and 289 other tissues.
DR ExpressionAtlas; P97464; baseline and differential.
DR Genevisible; P97464; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISO:MGI.
DR GO; GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISO:MGI.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050509; F:N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0098868; P:bone growth; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0045453; P:bone resorption; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
DR GO; GO:0016043; P:cellular component organization; IMP:MGI.
DR GO; GO:0033692; P:cellular polysaccharide biosynthetic process; ISO:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:MGI.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IMP:MGI.
DR GO; GO:0098586; P:cellular response to virus; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0003415; P:chondrocyte hypertrophy; IMP:MGI.
DR GO; GO:0035988; P:chondrocyte proliferation; IMP:MGI.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:MGI.
DR GO; GO:0070593; P:dendrite self-avoidance; IMP:MGI.
DR GO; GO:0036336; P:dendritic cell migration; IMP:MGI.
DR GO; GO:0060560; P:developmental growth involved in morphogenesis; IMP:MGI.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
DR GO; GO:0072498; P:embryonic skeletal joint development; IMP:MGI.
DR GO; GO:0003416; P:endochondral bone growth; IMP:MGI.
DR GO; GO:0060350; P:endochondral bone morphogenesis; IMP:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0007492; P:endoderm development; IMP:MGI.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR GO; GO:0060429; P:epithelium development; IMP:MGI.
DR GO; GO:0042596; P:fear response; IMP:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0042044; P:fluid transport; IGI:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IMP:MGI.
DR GO; GO:0032836; P:glomerular basement membrane development; IMP:MGI.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISO:MGI.
DR GO; GO:0022405; P:hair cycle process; IMP:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IGI:MGI.
DR GO; GO:0003128; P:heart field specification; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; IMP:MGI.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; ISO:MGI.
DR GO; GO:0030210; P:heparin biosynthetic process; IMP:MGI.
DR GO; GO:0030202; P:heparin metabolic process; IMP:MGI.
DR GO; GO:0002524; P:hypersensitivity; IMP:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:MGI.
DR GO; GO:0036022; P:limb joint morphogenesis; IMP:MGI.
DR GO; GO:0036339; P:lymphocyte adhesion to endothelial cell of high endothelial venule; IMP:MGI.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; IMP:MGI.
DR GO; GO:1901706; P:mesenchymal cell differentiation involved in bone development; IMP:MGI.
DR GO; GO:0060485; P:mesenchyme development; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0061744; P:motor behavior; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IGI:MGI.
DR GO; GO:0014033; P:neural crest cell differentiation; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:0021554; P:optic nerve development; IMP:MGI.
DR GO; GO:0001503; P:ossification; ISO:MGI.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:MGI.
DR GO; GO:0061974; P:perichondral bone morphogenesis; IMP:MGI.
DR GO; GO:0072112; P:podocyte differentiation; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR GO; GO:0070848; P:response to growth factor; IMP:MGI.
DR GO; GO:0071503; P:response to heparin; IMP:MGI.
DR GO; GO:1990823; P:response to leukemia inhibitory factor; IMP:MGI.
DR GO; GO:0009642; P:response to light intensity; IMP:MGI.
DR GO; GO:0009615; P:response to virus; IMP:MGI.
DR GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0060506; P:smoothened signaling pathway involved in lung development; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0055078; P:sodium ion homeostasis; IGI:MGI.
DR GO; GO:0017145; P:stem cell division; IMP:MGI.
DR GO; GO:0062094; P:stomach development; IMP:MGI.
DR GO; GO:0051923; P:sulfation; IDA:MGI.
DR GO; GO:0060792; P:sweat gland development; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0120193; P:tight junction organization; IMP:MGI.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IMP:MGI.
DR GO; GO:0007033; P:vacuole organization; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; IGI:MGI.
DR GO; GO:0071625; P:vocalization behavior; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR027670; Exostosin-1.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR PANTHER; PTHR11062:SF97; PTHR11062:SF97; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..746
FT /note="Exostosin-1"
FT /id="PRO_0000149649"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..746
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 654
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 544..549
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 565..567
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 567
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 595
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 650..654
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 688..701
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 652..704
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CONFLICT 16
FT /note="C -> S (in Ref. 2; CAA65443)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..61
FT /note="DA -> EP (in Ref. 2; CAA65443)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> T (in Ref. 2; CAA65443)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="A -> P (in Ref. 2; CAA65443)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="Missing (in Ref. 2; CAA65443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 86308 MW; 5AC7F24BECEEDFF9 CRC64;
MQAKKRYFIL LSAGSCLALL FYFGGVQFRA SRSHSRREEH SGRNGLHQPS PDHFWPRFPD
ALRPFFPWDQ LENEDSSVHI SPRQKRDANS SIYKGKKCRM ESCFDFTLCK KNGFKVYVYP
QQKGEKIAES YQNILAAIEG SRFYTSDPSQ ACLFVLSLDT LDRDQLSPQY VHNLRSKVQS
LHLWNNGRNH LIFNLYSGTW PDYTEDVGFD IGQAMLAKAS ISTENFRPNF DVSIPLFSKD
HPRTGGERGF LKFNTIPPLR KYMLVFKGKR YLTGIGSDTR NALYHVHNGE DVLLLTTCKH
GKDWQKHKDS RCDRDNTEYE KYDYREMLHN ATFCLVPRGR RLGSFRFLEA LQAACVPVML
SNGWELPFSE VINWNQAAVI GDERLLLQIP STIRSIHQDK ILALRQQTQF LWEAYFSSVE
KIVLTTLEII QDRIFKHISR NSLIWNKHPG GLFVLPQYSS YLGDFPYYYA NLGLKPPSKF
TAVIHAVTPL VSQSQPVLKL LVAAAKSQYC AQIIVLWNCD KPLPAKHRWP ATAVPVIVIE
GESKVMSSRF LPYDNIITDA VLSLDEDTVL STTEVDFAFT VWQSFPERIV GYPARSHFWD
NSKERWGYTS KWTNDYSMVL TGAAIYHKYY HYLYSHYLPA SLKNMVDQLA NCEDILMNFL
VSAVTKLPPI KVTQKKQYKE TMMGQTSRAS RWADPDHFAQ RQSCMNTFAS WFGYMPLIHS
QMRLDPVLFK DQVSILRKKY RDIERL
