PGCA_MOUSE
ID PGCA_MOUSE Reviewed; 2132 AA.
AC Q61282; E9QLS9; Q64021;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Aggrecan core protein;
DE AltName: Full=Cartilage-specific proteoglycan core protein;
DE Short=CSPCP;
DE Flags: Precursor;
GN Name=Acan; Synonyms=Agc, Agc1;
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=BALB/cJ; TISSUE=Cartilage;
RX PubMed=7806222; DOI=10.1006/geno.1994.1396;
RA Walcz E., Deak F., Erhardt P., Coulter S.N., Fueloep C., Horvath P.,
RA Doege K.J., Glant T.T.;
RT "Complete coding sequence, deduced primary structure, chromosomal
RT localization, and structural analysis of murine aggrecan.";
RL Genomics 22:364-371(1994).
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 [GENOMIC DNA] OF 211-326.
RC STRAIN=129/Sv;
RX PubMed=7920633; DOI=10.1038/ng0694-154;
RA Watanabe H., Kimata K., Line S., Strong D., Gao L.-Y., Kozak C.A.,
RA Yamada Y.;
RT "Mouse cartilage matrix deficiency (cmd) caused by a 7 bp deletion in the
RT aggrecan gene.";
RL Nat. Genet. 7:154-157(1994).
RN [4]
RP INTERACTION WITH FBLN1.
RX PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
RA Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
RT "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
RT versican.";
RL J. Biol. Chem. 274:20444-20449(1999).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7524681; DOI=10.1016/0167-4781(94)90220-8;
RA Glumoff V., Savontaus M., Vehanen J., Vuorio E.;
RT "Analysis of aggrecan and tenascin gene expression in mouse skeletal
RT tissues by northern and in situ hybridization using species specific cDNA
RT probes.";
RL Biochim. Biophys. Acta 1219:613-622(1994).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: This proteoglycan is a major component of extracellular
CC matrix of cartilagenous tissues. A major function of this protein is to
CC resist compression in cartilage. It binds avidly to hyaluronic acid via
CC an N-terminal globular region. May play a regulatory role in the matrix
CC assembly of the cartilage.
CC -!- SUBUNIT: Interacts with COMP (By similarity). Interacts with FBLN1.
CC {ECO:0000250, ECO:0000269|PubMed:10400671}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in cartilage tissues.
CC {ECO:0000269|PubMed:7524681}.
CC -!- DEVELOPMENTAL STAGE: Expressed in chondrocytes throughout the
CC developing skeleton in a pattern very similar but not identical to
CC those of type II and IX collagen. In the newborn mouse skeleton it is
CC expressed essentially in a mutually exclusive manner with tenascin,
CC which is expressed osteoblasts, periosteal and perichondrial cells, and
CC in cells at articular surfaces. {ECO:0000269|PubMed:7524681}.
CC -!- DOMAIN: Two globular domains, G1 and G2, comprise the N-terminus of the
CC proteoglycan, while another globular region, G3, makes up the C-
CC terminus. G1 contains Link domains and thus consists of three
CC disulfide-bonded loop structures designated as the A, B, B' motifs. G2
CC is similar to G1. The keratan sulfate (KS) and the chondroitin sulfate
CC (CS) attachment domains lie between G2 and G3.
CC -!- PTM: Contains mostly chondroitin sulfate, but also keratan sulfate
CC chains, N-linked and O-linked oligosaccharides.
CC -!- DISEASE: Note=Defects in Acan are the cause of cartilage matrix
CC deficiency (CMD). CMD is an autosomal recessive syndrome characterized
CC by cleft palate, short limbs, tail and snout. Mutation in strain CMD
CC causes absence of aggrecan by truncation of the protein (mutation in
CC the G1 domain).
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Aggrecan;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_283";
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DR EMBL; L07049; AAC37670.1; -; mRNA.
DR EMBL; AC110520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S73722; AAB32160.1; -; Genomic_DNA.
DR EMBL; S73721; AAB32160.1; JOINED; Genomic_DNA.
DR CCDS; CCDS21377.1; -.
DR PIR; A55182; A55182.
DR RefSeq; NP_031450.2; NM_007424.2.
DR AlphaFoldDB; Q61282; -.
DR SMR; Q61282; -.
DR BioGRID; 198020; 5.
DR STRING; 10090.ENSMUSP00000032835; -.
DR GlyConnect; 2114; 2 N-Linked glycans (1 site).
DR GlyGen; Q61282; 9 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q61282; -.
DR PhosphoSitePlus; Q61282; -.
DR MaxQB; Q61282; -.
DR PaxDb; Q61282; -.
DR PeptideAtlas; Q61282; -.
DR PRIDE; Q61282; -.
DR ProteomicsDB; 288181; -.
DR Antibodypedia; 4288; 547 antibodies from 32 providers.
DR DNASU; 11595; -.
DR Ensembl; ENSMUST00000032835; ENSMUSP00000032835; ENSMUSG00000030607.
DR GeneID; 11595; -.
DR KEGG; mmu:11595; -.
DR UCSC; uc009hxw.1; mouse.
DR CTD; 176; -.
DR MGI; MGI:99602; Acan.
DR VEuPathDB; HostDB:ENSMUSG00000030607; -.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR GeneTree; ENSGT00940000155971; -.
DR HOGENOM; CLU_000303_2_0_1; -.
DR InParanoid; Q61282; -.
DR OMA; HPLQFEN; -.
DR OrthoDB; 156064at2759; -.
DR PhylomeDB; Q61282; -.
DR TreeFam; TF332134; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 11595; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Acan; mouse.
DR PRO; PR:Q61282; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61282; protein.
DR Bgee; ENSMUSG00000030607; Expressed in humerus cartilage element and 83 other tissues.
DR ExpressionAtlas; Q61282; baseline and differential.
DR Genevisible; Q61282; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0072534; C:perineuronal net; ISO:MGI.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; IDA:SynGO.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 5.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033987; CSPG_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 4.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 4.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 5.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
DR PROSITE; PS01241; LINK_1; 4.
DR PROSITE; PS50963; LINK_2; 4.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Immunoglobulin domain; Lectin; Metal-binding; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2132
FT /note="Aggrecan core protein"
FT /id="PRO_0000017507"
FT DOMAIN 34..147
FT /note="Ig-like V-type"
FT DOMAIN 153..248
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 254..350
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 487..582
FT /note="Link 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 588..684
FT /note="Link 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 1918..2044
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 2047..2107
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 48..140
FT /note="G1-A"
FT REGION 152..247
FT /note="G1-B"
FT REGION 253..349
FT /note="G1-B'"
FT REGION 486..580
FT /note="G2-B"
FT REGION 587..682
FT /note="G2-B'"
FT REGION 685..803
FT /note="KS"
FT REGION 737..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..1231
FT /note="CS-1"
FT REGION 1108..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1917
FT /note="CS-2"
FT REGION 1299..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1782..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..2132
FT /note="G3"
FT MOTIF 1171..1173
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 778..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1805..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1983
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1987
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1987
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 2007
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2009
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2010
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2016
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2016
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2017
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2017
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 2030
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2031
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 376
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..133
FT /evidence="ECO:0000250"
FT DISULFID 175..246
FT /evidence="ECO:0000250"
FT DISULFID 199..220
FT /evidence="ECO:0000250"
FT DISULFID 273..348
FT /evidence="ECO:0000250"
FT DISULFID 297..318
FT /evidence="ECO:0000250"
FT DISULFID 509..580
FT /evidence="ECO:0000250"
FT DISULFID 533..554
FT /evidence="ECO:0000250"
FT DISULFID 607..682
FT /evidence="ECO:0000250"
FT DISULFID 631..652
FT /evidence="ECO:0000250"
FT DISULFID 1922..1933
FT /evidence="ECO:0000250"
FT DISULFID 1950..2042
FT /evidence="ECO:0000250"
FT DISULFID 2018..2034
FT /evidence="ECO:0000250"
FT DISULFID 2049..2092
FT /evidence="ECO:0000250"
FT DISULFID 2078..2105
FT /evidence="ECO:0000250"
FT CONFLICT 482
FT /note="R -> H (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="V -> I (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="G -> R (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="G -> E (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1701..1702
FT /note="TP -> IS (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1705
FT /note="F -> S (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1729
FT /note="I -> V (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1938
FT /note="H -> P (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
FT CONFLICT 2119
FT /note="S -> T (in Ref. 1; AAC37670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2132 AA; 221941 MW; 17298662D95E1921 CRC64;
MTTLLLVFVT LRVIAAVISE EVPDHDNSLS VSIPQPSPLK VLLGSSLTIP CYFIDPMHPV
TTAPSTAPLT PRIKWSRVSK EKEVVLLVAT EGQVRVNSIY QDKVSLPNYP AIPSDATLEI
QNLRSNDSGI YRCEVMHGIE DSEATLEVIV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
TYDVYCFAEE MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QGGMDMCSAG
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN
FFGVGGEDDI TIQTVTWPDL ELPLPRNVTE GEALGSVILT AKPIFDLSPT ISEPGEALTL
APEVGSTAFP EAEERTGEAT RPWGFPAEVT RGPDSATAFA SEDLVVRVTI SPGAAEVPGQ
PRLPGGVVFH YRPGSTRYSL TFEEAQQACM HTGAVIASPE QLQAAYEAGY EQCDAGWLQD
QTVRYPIVSP RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATRLEQFTF
QEARAFCAAQ NATLASTGQL YAAWSQGLDK CYAGWLADGT LRYPIITPRP ACGGDKPGVR
TVYLYPNQTG LPDPLSKHHA FCFRGVSVAP SPGEEGGSTP TSPSDIEDWI VTQVGPGVDA
VPLEPKTTEV PYFTTEPRKQ TEWEPAYTPV GTSPQPGIPP TWLPTLPAAE EHTESPSASE
EPSASAVPST SEEPYTSSFA VPSMTELPGS GEASGAPDLS GDFTGSGDAS GRLDSSGQPS
GGIESGLPSG DLDSSGLSPT VSSGLPVESG SASGDGEVPW SHTPTVGRLP SGGESPEGSA
SASGTGDLSG LPSGGEITET STSGAEETSG LPSGGDGLET STSGVDDVSG IPTGREGLET
SASGVEDLSG LPSGEEGSET STSGIEDISV LPTGGESLET SASGVGDLSG LPSGGESLET
SASGAEDVTQ LPTERGGLET SASGVEDITV LPTGRESLET SASGVEDVSG LPSGREGLET
SASGIEDISV FPTEAEGLDT SASGGYVSGI PSGGDGTETS ASGVEDVSGL PSGGEGLETS
ASGVEDLGPS TRDSLETSAS GVDVTGFPSG RGDPETSVSG VGDDFSGLPS GKEGLETSAS
GAEDLSGLPS GKEDLVGSAS GALDFGKLPP GTLGSGQTPE VNGFPSGFSG EYSGADIGSG
PSSGLPDFSG LPSGFPTVSL VDSTLVEVIT ATTSSELEGR GTIGISGSGE VSGLPLGELD
SSADISGLPS GTELSGQASG SPDSSGETSG FFDVSGQPFG SSGVSEETSG IPEISGQPSG
TPDTTATSGV TELNELSSGQ PDVSGDGSGI LFGSGQSSGI TSVSGETSGI SDLSGQPSGF
PVFSGTATRT PDLASGTISG SGESSGITFV DTSFVEVTPT TFREEEGLGS VELSGFPSGE
TELSGTSGTV DVSEQSSGAI DSSGLTSPTP EFSGLPSGVA EVSGEFSGVE TGSSLPSGAF
DGSGLVSGFP TVSLVDRTLV ESITQAPTAQ EAGEGPSGIL EFSGAHSGTP DISGELSGSL
DLSTLQSGQM ETSTETPSSP YFSGDFSSTT DVSGESIAAT TGSGESSGLP EVTLNTSELV
EGVTEPTVSQ ELGHGPSMTY TPRLFEASGD ASASGDLGGA VTNFPGSGIE ASVPEASSDL
SAYPEAGVGV SAAPEASSKL SEFPDLHGIT SAFHETDLEM TTPSTEVNSN PWTFQEGTRE
GSAAPEVSGE SSTTSDIDTG TSGVPSATPM ASGDRTEISG EWSDHTSEVN VAISSTITES
EWAQPTRYPT ETLQEIESPN PSYSGEETQT AETTMSLTDA PTLSSSEGSG ETESTVADQE
QCEEGWTKFQ GHCYRHFHDR ETWVDAERRC REQQSHLSSI VTPEEQEFVN KNAQDYQWIG
LNDRTIEGDF RWSDGHSLQF EKWRPNQPDN FFATGEDCVV MIWHERGEWN DVPCNYQLPF
TCKKGTVACG DPPVVEHART LGQKKDRYEI SSLVRYQCTE GFVQRHVPTI RCQPSGHWEE
PRITCTDPNT YKHRLQKRSM RPTRRSRPSM AH
