CSPG2_RAT
ID CSPG2_RAT Reviewed; 2738 AA.
AC Q9ERB4; O08592; O88564; Q9R1K4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Versican core protein;
DE AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
DE Short=Chondroitin sulfate proteoglycan 2;
DE AltName: Full=Glial hyaluronate-binding protein;
DE Short=GHAP;
DE AltName: Full=Large fibroblast proteoglycan;
DE AltName: Full=PG-M;
DE Flags: Precursor; Fragments;
GN Name=Vcan; Synonyms=Cspg2;
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 [MRNA] OF 349-2738 (ISOFORM V0), NUCLEOTIDE SEQUENCE
RP [MRNA] (ISOFORM V3), AND NUCLEOTIDE SEQUENCE [MRNA] OF 2657-2738 (ISOFORM
RP VINT).
RC STRAIN=Wistar Kyoto;
RX PubMed=10397680; DOI=10.1161/01.atv.19.7.1630;
RA Lemire J.M., Braun K.R., Maurel P., Kaplan E.D., Schwartz S.M., Wight T.N.;
RT "Versican/PG-M isoforms in vascular smooth muscle cells.";
RL Arterioscler. Thromb. Vasc. Biol. 19:1630-1639(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 349-2738 (ISOFORM V0).
RC STRAIN=Wistar Kyoto;
RX PubMed=9642104; DOI=10.1006/bbrc.1998.8759;
RA Milev P., Maurel P., Chiba A., Mevissen M., Popp S., Yamaguchi Y.,
RA Margolis R.K., Margolis R.U.;
RT "Differential regulation of expression of hyaluronan-binding proteoglycans
RT in developing brain: aggrecan, versican, neurocan, and brevican.";
RL Biochem. Biophys. Res. Commun. 247:207-212(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2421-2463 (ISOFORM V0).
RC TISSUE=Kidney;
RX PubMed=9434070; DOI=10.1159/000190325;
RA Pyke C., Kristensen P., Ostergaard P.B., Oturai P.S., Romer J.;
RT "Proteoglycan expression in the normal rat kidney.";
RL Nephron 77:461-470(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2535-2738.
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RA Blomberg L.A., Chan W.-Y., Clerch L., Massaro D.;
RT "Molecular cloning and characterization of two developmentally regulated
RT genes in rat lung.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in intercellular signaling and in connecting
CC cells with the extracellular matrix. May take part in the regulation of
CC cell motility, growth and differentiation. Binds hyaluronic acid.
CC -!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P13611}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:P13611}. Secreted,
CC extracellular space, extracellular matrix, interphotoreceptor matrix
CC {ECO:0000250|UniProtKB:P13611}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=V0;
CC IsoId=Q9ERB4-1; Sequence=Displayed;
CC Name=V3;
CC IsoId=Q9ERB4-2; Sequence=VSP_003091;
CC Name=Vint;
CC IsoId=Q9ERB4-3; Sequence=VSP_003092;
CC -!- TISSUE SPECIFICITY: In kidney is expressed in the papillary area, but
CC not in glomeruli.
CC -!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P13611}.
CC -!- PTM: Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the
CC pericellular matrix surrounding myoblasts, facilitating myoblast
CC contact and fusion which is required for skeletal muscle development
CC and regeneration. {ECO:0000250|UniProtKB:Q62059}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
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DR EMBL; AF062402; AAC40166.1; -; mRNA.
DR EMBL; U75306; AAB51125.1; -; mRNA.
DR EMBL; AF084544; AAD48544.1; -; mRNA.
DR EMBL; AF072892; AAC26116.1; -; mRNA.
DR EMBL; AY007691; AAG16631.1; -; mRNA.
DR RefSeq; NP_001164029.1; NM_001170558.1.
DR RefSeq; NP_001164030.1; NM_001170559.1. [Q9ERB4-2]
DR RefSeq; NP_001164031.1; NM_001170560.1.
DR SMR; Q9ERB4; -.
DR BioGRID; 250300; 1.
DR IntAct; Q9ERB4; 1.
DR MINT; Q9ERB4; -.
DR GlyGen; Q9ERB4; 17 sites.
DR PhosphoSitePlus; Q9ERB4; -.
DR PaxDb; Q9ERB4; -.
DR PRIDE; Q9ERB4; -.
DR ABCD; Q9ERB4; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000063821; ENSRNOP00000062961; ENSRNOG00000029212. [Q9ERB4-2]
DR GeneID; 114122; -.
DR KEGG; rno:114122; -.
DR UCSC; RGD:619940; rat. [Q9ERB4-1]
DR CTD; 1462; -.
DR RGD; 619940; Vcan.
DR eggNOG; ENOG502QRBE; Eukaryota.
DR GeneTree; ENSGT00940000156102; -.
DR InParanoid; Q9ERB4; -.
DR OrthoDB; 74642at2759; -.
DR PhylomeDB; Q9ERB4; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-RNO-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0072534; C:perineuronal net; IDA:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; TAS:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0031103; P:axon regeneration; IEP:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0008347; P:glial cell migration; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 3.
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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; PF00008; EGF; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 3.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS01241; LINK_1; 2.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell projection; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW Immunoglobulin domain; Lectin; Phosphoprotein; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..2738
FT /note="Versican core protein"
FT /id="PRO_0000017524"
FT DOMAIN 21..146
FT /note="Ig-like V-type"
FT DOMAIN 150..245
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 251..347
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 2431..2467
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2469..2505
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2518..2632
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 2636..2696
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION <349..695
FT /note="GAG-alpha (glucosaminoglycan attachment domain)"
FT REGION 641..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..2431
FT /note="GAG-beta"
FT REGION 1064..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1671..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2166..2187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2229..2287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2714..2738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2166..2186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2233..2249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2252..2266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2267..2284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2720..2738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 788..789
FT /note="Cleavage; by ADAMTS15"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT MOD_RES 1963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT MOD_RES 1964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2004
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..130
FT /evidence="ECO:0000250"
FT DISULFID 172..243
FT /evidence="ECO:0000250"
FT DISULFID 196..217
FT /evidence="ECO:0000250"
FT DISULFID 270..345
FT /evidence="ECO:0000250"
FT DISULFID 294..315
FT /evidence="ECO:0000250"
FT DISULFID 2435..2446
FT /evidence="ECO:0000250"
FT DISULFID 2440..2455
FT /evidence="ECO:0000250"
FT DISULFID 2457..2466
FT /evidence="ECO:0000250"
FT DISULFID 2473..2484
FT /evidence="ECO:0000250"
FT DISULFID 2478..2493
FT /evidence="ECO:0000250"
FT DISULFID 2495..2504
FT /evidence="ECO:0000250"
FT DISULFID 2511..2522
FT /evidence="ECO:0000250"
FT DISULFID 2539..2631
FT /evidence="ECO:0000250"
FT DISULFID 2607..2623
FT /evidence="ECO:0000250"
FT DISULFID 2638..2681
FT /evidence="ECO:0000250"
FT DISULFID 2667..2694
FT /evidence="ECO:0000250"
FT VAR_SEQ 349..2431
FT /note="Missing (in isoform V3)"
FT /evidence="ECO:0000303|PubMed:10397680"
FT /id="VSP_003091"
FT VAR_SEQ 2697..2738
FT /note="PSAYQRTYSKKYLKNSSSVKDNSINTSKHEHRWSRRWQETRR -> RKWSFR
FT KNGQPCFNKY (in isoform Vint)"
FT /evidence="ECO:0000303|PubMed:10397680"
FT /id="VSP_003092"
FT CONFLICT 2535..2539
FT /note="AEREC -> NSARG (in Ref. 4)"
FT /evidence="ECO:0000305"
FT NON_CONS 348..349
FT /evidence="ECO:0000305"
SQ SEQUENCE 2738 AA; 300008 MW; 12CA626D58BD8C6A CRC64;
MLINMNGILW MCSTLLLTHA LHKAKMEENP PVKGSLSGKV ILPCHFSTLP TLPPDYNTSE
FLRIKWSKIE VDKNGKDIKE TTVLVAQDGN IKIGQDYKGR VSVPTHPDDV GDASLTMVKL
RASDAGVYRC DVMYGIEDTQ NTMSLAVDGV VFHYRAATSR YTLNFESAQQ ACLDIGAVIA
TPEQLFAAYE DGFEQCDAGW LSDQTVRYPI RAPREGCYGD MMGKEGVRTY GFRSPQETYD
VYCYVDHLDG DVFHITAPSK FTFEEAEAEC ANRDARLATV GELHAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTCFPLPDSR FDAYCFKRSP LSIIPKTEWS
VSETSVPLED EVLGKSDQDT LEQTHLEATM SPEALSTIEV TQGETQEEPQ TPGIPFPALS
STAVMTKETT AFEEEGEGST YTLSEDRLMT DSEIVPSLET TPVGTSYPGG AMTQQEVEMD
TMVTQMSSIR PTVVLSTEPE VSYEAEGSSP MEFASTLKPF GTQVTQLVEE TTEEGKKTPL
DYTDLGSGLF EQPRVTELPD FSMTPSDISV FTAIDSLHRT TPLRPPSPFT EEPHIFEKEP
SEKTTGDIIL PRESVTQHPL TTLMDIIAKK TESDIDHEYH MTSKPPVMQP TRPSVVERKT
TSKPQELSTS PPPAGTKFHP DINVYIIEVR ENKTGRMSDM VVNGHPIDSE SKEEEPCSEE
TDPLHDLFAE ILPELPDSFE IDIYHSEEDE DGEEDCVNAT DVTTTPSVQY ITGKPHVTTV
PKNPEAAEAR RGLYESVAPS QNFSNTSATD THQFIPAETE LSTTMQFTKS KEATELLEIT
WKPETYPETP EHFSSGEPDV FPTLPSHDGK TTKWSEFITE SNPNTENPEH KQPKPIPLFP
EEFSGEGAID QASQQTIFSR ATEVALGKET DQSPTISTSS IRSGSVSVHA LEEDPIALTG
ISQTDESMST VESWVEMTPS QTVEFSGSSS APTIEGSGEV EEYTNKIFNT VTDLPQREPT
DTLIPLDMSN IMITDHHIYT PATTAPLDSQ LPSTDARPTQ FGIQTTTSEW VSSTSFEGRK
TEEDKERDTN AAHTGEVQPA TERSDRLLLT SELESSNVAA SSPLDTWEGF VPETTSTVSE
KEMANTTPVF TETSDVANLE TQSFEHSSSS QPRVQEELTT LSGKPPLIFM DLGSGDASTD
MEFITASSFT LDLESDTKVK KELPSTLSPS VETSSSSEPI GLAPSTVLDI EIVEVMNQTS
KKTLISELSG KPTSQAEVRD LYPGLGEDFS GDSSEYPTVS STTMKEETVG MGGSENERVK
DTQTLSSIPP TSDNINPVPD SKGFGSTVAS TTAFPWEEFM TSAEGSGEEL SSVRSSVSLV
LPLGVDILPT TESPYFDQEF EEAAAVTEAG KQSALPIAVS GNTVDLTENR DIEVNSTMSV
DLPQTMEPAK LWSKPEVNPE KQEIGSETVT QDKAQGQKSF ESLHSSLAPE QTTLESQSLI
ETEVQTSYYS MLTTMKTYNT NEEVEEEGTS IAHMSTPGPG IKGLESYPTH PEATGKSYSF
SASALVTESG PARSVVMDSS TQEEESIKLF QKDMILTHKE SNSDLSFSGL GSGEALPPLP
TTSVSLTDMG KINSTLYPET SHMESLGTSI LGDNHERMKN VSNEVRTLIS ETGSISQDST
EAPNTTLSDT RTEESTTSPL PFMKLMDTEH SPKQTLRWEE EIQTHRPQTM TGQMTNDNSS
VSEAEAAATS APAFLPETYS VEMTKAFATS PSQTSDLFDA NSGEGSGEVD GLDLVYTSRT
TQASSQGDSM FASHGFIEKH PEVSRTETGA TDGSPTASAM FLHQSEYNES SLYPTSTLPS
TVTYESPSEG IADGLQDHIR FEVSTLKPSR RKATESVIID LDKEDSKDLG LAITESAIVE
ILPELTSDRN IIIDIDHTKP VYEYIPGIQT DLDSDIPLGS HGSSEESLEV QEKYEATINL
SPTEEAFDGS GDALPAGHTQ AIYNESVTPS DGKQPEDISF SFATGIPVSS TETELNTFFP
TVSTLHIPSK LTTASPEIDK PNIEAISLDD IFESSTLSDG QAIADQSEVI STLGHLEKTQ
EEYEEKKYGG PSFQPEFFSG VGEVFTDAPA YVSIGRTYSV AQPLTEFPNV VGQSDSTHYT
EATSAVSSVT ELSPQTPSSP SPVYIDSGVS EFTEVPHKSA QPAPTAASSQ KLIEGSFKKV
RANIEATIKS LGENDHGTES PSMSPSPALD ISEDDSKPKL LEDLETSPTK TETSQDSPNK
ANDQIPGKTA GILAGIKTTE SGPVVTAADD MELGDATQRP HSASAPAAFR VETSMVPQPI
PQEPERPTFP SLEINHETHT SLFEESILAT SEKQVSQRIL DYSNQATVST LDLNTEHSIP
PFSILDNSNE TAFLIGISEE TVEGTAVYLP GPDLCKTNPC LNGGTCYPTE TSYVCTCAPG
YSGDQCELDF DECHSNPCRN GATCVDGLNT FRCLCLPSYV GALCEQDTET CDYGWHKFQG
QCYKYFAHRR TWDAAERECR LQGAHLTSIL SHEEQMFVNR VGHDYQWIGL NDKMFEHDFR
WTDGSALQYE NWRPNQPDSF FSAGEDCVVI IWHENGQWND VPCNYHLTYT CKKGTVACGQ
PPVVENAKTF GKMKPRYEIN SLIRYHCKDG FIQRHLPTIR CLGNGRWAMP KITCMNPSAY
QRTYSKKYLK NSSSVKDNSI NTSKHEHRWS RRWQETRR
