CSPG2_BOVIN
ID CSPG2_BOVIN Reviewed; 3381 AA.
AC P81282; O77609; O77610; O77611; O77612;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
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;
GN Name=VCAN; Synonyms=CSPG2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0; V1; V2 AND V3).
RC TISSUE=Forebrain;
RX PubMed=9624174; DOI=10.1074/jbc.273.25.15758;
RA Schmalfeldt M., Dours-Zimmermann M.T., Winterhalter K.H., Zimmermann D.R.;
RT "Versican V2 is a major extracellular matrix component of the mature bovine
RT brain.";
RL J. Biol. Chem. 273:15758-15764(1998).
RN [2]
RP PROTEIN SEQUENCE OF 21-53; 78-96; 226-250; 262-277; 295-306; 314-324;
RP 329-331 AND 342-348.
RC TISSUE=Spinal cord;
RX PubMed=1720020; DOI=10.1016/0304-4165(91)90273-j;
RA Perides G., Biviano F., Bignami A.;
RT "Interaction of a brain extracellular matrix protein with hyaluronic
RT acid.";
RL Biochim. Biophys. Acta 1075:248-258(1991).
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=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=V0;
CC IsoId=P81282-1; Sequence=Displayed;
CC Name=V1;
CC IsoId=P81282-2; Sequence=VSP_003078, VSP_003079;
CC Name=V2;
CC IsoId=P81282-3; Sequence=VSP_003080;
CC Name=V3;
CC IsoId=P81282-4; Sequence=VSP_003078, VSP_003081;
CC -!- TISSUE SPECIFICITY: Cerebral white matter. Isoform V0 and isoform V1
CC are expressed in the central nervous system, and in a number of
CC mesenchymal and epithelial tissues; the major isoform V2 is restricted
CC to the central nervous system.
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; AF060456; AAC24358.1; -; mRNA.
DR EMBL; AF060457; AAC24359.1; -; mRNA.
DR EMBL; AF060458; AAC24360.1; -; mRNA.
DR EMBL; AF060459; AAC24361.1; -; mRNA.
DR PIR; T14274; T14274.
DR PIR; T42389; T42389.
DR RefSeq; NP_851378.1; NM_181035.2. [P81282-1]
DR RefSeq; XP_015327844.1; XM_015472358.1. [P81282-4]
DR SMR; P81282; -.
DR STRING; 9913.ENSBTAP00000019848; -.
DR PaxDb; P81282; -.
DR PeptideAtlas; P81282; -.
DR PRIDE; P81282; -.
DR Ensembl; ENSBTAT00000042717; ENSBTAP00000040348; ENSBTAG00000014906. [P81282-4]
DR GeneID; 282662; -.
DR KEGG; bta:282662; -.
DR CTD; 1462; -.
DR VEuPathDB; HostDB:ENSBTAG00000014906; -.
DR eggNOG; ENOG502QRBE; Eukaryota.
DR GeneTree; ENSGT00940000156102; -.
DR InParanoid; P81282; -.
DR OrthoDB; 74642at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014906; Expressed in granulosa cell and 104 other tissues.
DR ExpressionAtlas; P81282; baseline and differential.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
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:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
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; -; 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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell projection; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Hyaluronic acid; Immunoglobulin domain; Lectin; Phosphoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..3381
FT /note="Versican core protein"
FT /id="PRO_0000017521"
FT DOMAIN 21..147
FT /note="Ig-like V-type"
FT DOMAIN 151..246
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 252..348
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 3074..3110
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3112..3148
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3161..3275
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 3279..3339
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 349..1336
FT /note="GAG-alpha (glucosaminoglycan attachment domain)"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..3074
FT /note="GAG-beta"
FT REGION 1338..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1964..1986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2041..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2338..2388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2490..2512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2594..2615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2819..2893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3355..3381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2045..2062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2342..2388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2832..2855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3363..3381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1423..1424
FT /note="Cleavage; by ADAMTS15"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT MOD_RES 2109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13611"
FT MOD_RES 2607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT MOD_RES 2608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT MOD_RES 2612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13611"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2074
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..131
FT /evidence="ECO:0000250"
FT DISULFID 173..244
FT /evidence="ECO:0000250"
FT DISULFID 197..218
FT /evidence="ECO:0000250"
FT DISULFID 271..346
FT /evidence="ECO:0000250"
FT DISULFID 295..316
FT /evidence="ECO:0000250"
FT DISULFID 3078..3089
FT /evidence="ECO:0000250"
FT DISULFID 3083..3098
FT /evidence="ECO:0000250"
FT DISULFID 3100..3109
FT /evidence="ECO:0000250"
FT DISULFID 3116..3127
FT /evidence="ECO:0000250"
FT DISULFID 3121..3136
FT /evidence="ECO:0000250"
FT DISULFID 3138..3147
FT /evidence="ECO:0000250"
FT DISULFID 3154..3165
FT /evidence="ECO:0000250"
FT DISULFID 3182..3274
FT /evidence="ECO:0000250"
FT DISULFID 3250..3266
FT /evidence="ECO:0000250"
FT DISULFID 3281..3324
FT /evidence="ECO:0000250"
FT DISULFID 3310..3337
FT /evidence="ECO:0000250"
FT VAR_SEQ 349
FT /note="P -> R (in isoform V1 and isoform V3)"
FT /evidence="ECO:0000303|PubMed:9624174"
FT /id="VSP_003078"
FT VAR_SEQ 350..3074
FT /note="Missing (in isoform V3)"
FT /evidence="ECO:0000303|PubMed:9624174"
FT /id="VSP_003081"
FT VAR_SEQ 350..1336
FT /note="Missing (in isoform V1)"
FT /evidence="ECO:0000303|PubMed:9624174"
FT /id="VSP_003079"
FT VAR_SEQ 1337..3074
FT /note="Missing (in isoform V2)"
FT /evidence="ECO:0000303|PubMed:9624174"
FT /id="VSP_003080"
FT CONFLICT 25
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="Q -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="C -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3381 AA; 369990 MW; F09716FA7778D459 CRC64;
MLINIKSILW MCSTLIAAHA LQKVNMEKSP PVKGSLSGKV NLPCHFSTMP TLPPSYNTTS
EFLRIKWSKI ELDKTGKDLK ETTVLVAQNG NIKIGQDYKG RVSVPTHPED VGDASLTMVK
LLASDAGRYR CDVMYGIEDT QDTVSLTVEG VVFHYRAATS RYTLNFEMAQ KACVDIGAVI
ATPEQLHAAY EDGFEQCDAG WLSDQTVRYP IRVPREGCYG DMMGKEGVRT YGFRAPHETY
DVYCYVDHLD GDVFHITAPN KFTFEEAGEE CKTQDARLAT VGELQAAWRN GFDRCDYGWL
LDASVRHPVT VARAQCGGGL LGVRTLYRFE NQTGFPTPDS RFDAYCFKPK QNISEATTIE
LNMLAETVSP TLLEELQVGL DRMTPIVPLI TELPVITTKV PPIGNIVNFE QKSTVQPLTS
THRSATESLP PDGSMKKPWD MDYYSPSASG PLGEPDVSEI KEEVPQSTTV VSHHAPDSWD
GVKEDLQIKD SVTQIEQIEV GPLVTSMEIS KHIPSKEFTV TVTPFVSTTM TLESKTEKKA
ISTVSESVTT SHYGFTLREG DGEDRISTVR SGQSTSIFSQ IPEVITVSKT SEDTTRGQLE
DVESVSASTI VSPDSDGSPM DHRQEKQTHG RITEGFLGQY VSTTPFPSQH HTEVELFPYS
GDKRLVEGTS TVISPTPRTG RERTETLRPA MRTVTYTNDE IQEKITKDSS IEKIEEEGFS
GMKFPTASPE QIHHTKYSVG MTKSFESPAL MTTTKPGVTP TEATDVEEDF TTPSGLETDG
YQDTTEYEEG ITTVHLIQST LNVEVVTVSK WSLDEDNTTS KPLGSTEHVG SPKLPPALIT
TTGVSGKDKE MPSLTEDGRD EFTRIPGSTQ RPLEEFTEED TTDHEKFTVR FQPTTSIATT
EKSTLRDSIT EERVPPFTST EVRVTHATIE GSALDEGEDV DVSKPLSTVP QFAHPSDVEG
STFVNYSSTQ EPTTYVDTSH TIPLPVIPKT EWGVLVPSIP SEGEVLGEPS QDIRVINQTH
FEASMYPETV RTTTEITQEA TREDFLWKEQ TPEKPVSPPS STTDTAKETT PPLDEQESDG
SAYTVFEDRS VMGSDRVSVL VTTPIGKFEQ HTSFPPGAVT KAKTDEVVTL TPTTGSKVTF
SPWPKQKYET EGTSPRGFVS PFSIGVTQLI EETTTEKREK TSLDYIDLGS GLFEKPKATE
LPEFSTVKAT VPSDTAAFSS ADRLHTPSAS TEKPPLIDRE PDEETTSDMV IIGESTSRVP
PTTLEDIVAK KTETDIDREY FTTSSTSTTQ PTRPPTVEGK EAFGPQAFST PEPPAGTKFH
PDINVYIIEV RENKTGRMSD FSVSGHPIDS ESKEDEPCSE ETDPEHDLIA EILPELLGML
HSEEDEEDEE CANATDVTTT PSVQYINGKH VVTTVPKDPE AAEARRGQFE SVAPSQNFSD
SSESDSHQFI ITHAGLPTAM QPNESKETTE SLEITWRPEI YPETAEPFSS GEPDIFPTAS
IHEGEATEGP DSITEKNPEL DHLVHEHAES VPLFPEESSG DAAIDQESQK IIFSGATEGT
FGEEAEKSST THTPSMVASS VSAPVSEDAS FILTGTPQSD EPLSTVESWV EITPRHTVEF
SGSPSIPIPE GSGEAEEDKD KIFAMITDLS QRNTTDPRVT SDTSKIMITE SLVDVPTTTI
YSISEQVSAV VPTKFVRETD TYEWVFSPPL EETTRKEEEK GTTGTASTVE VHSPTQRLDQ
FVSPSELESS SETPPDDSAA ATRKSFTSQM TPTQSERETT SSTVVFKETE VLDNLAAQTT
DPSLSSQPGV LEVSPTVPGS PVSLFMEQGS GEAAVDPETT TVSSLSLNIE PEILAKEEAA
GAWSPNVETV FPFEPTEQVL STAVDREVAE TISQTSKENL VSEISGEPTH RAEIKGFSTD
FPLEEDFSGD FREYSTVSYP ITKEEIVMME GSGDAAFKDT QMLPSVTPTS DLSNHTADSE
EPGSTLVSTS AFPWEEFTAS AEGSGEPLLS VSSSVDQVFP SAAGKASGTD SPFIDQRLGE
EGAINETDQR STILPTAEAE STKASTEEGE VKENHTVSMD FPPTVEPDEL WPRQEVNPVR
QGNGSEIVSE EKTQEQESFE PLQSSVAPEQ TTFDSQTFPE PGLQTTGYFT LTTKKTYSTD
ERMEEEVISL ADVSTPTLDS KGLVLYTTLP EVTEKSHFFL ATASVTESVP AESVIAGSTI
KEEESIKPFP KVTSPIIKES DTDLIFSGLG SGEEVLPTLG SVNFTEIEQV LSTLYPLTSQ
VQSLEASILN DTSGDYEGME NVANEMRPLI SKTDSIFEDG ETASSTTLPE ILSDARTEGP
FTAPLTFSTG PGQPQNQTHR RAEEIQTSRP QPLTDQVSSE NSVTAETKET ATPATDFLAR
TYDLEMAKGF VTPTPKPSDL FYEHSGEGSG ELDAVGAEVH ASGMTQATRQ GSTTFVSDRS
LEKHPKVPSV EAVTVNGFPT VSMVLPLHPE QREGSPEATG TPASTASYEK ATEGAADSFQ
DHFWGFKDST LKPDKRKATE SIIIDLDKED KDLILTMTES TILEIIPELT SDKNTVIDID
HTKPIYEDIL GMQTDLDPEV PSGPPDSSEE STQVQEKYEA AVNLSSTEEN FEASGDILLA
NYTQATPESK APEDRNPLDH TDFIFTTGIP ILSSETELDV LLPTATSLPI PSKSATVNPE
SKTEAKTLED IFESSTLSDG QAIADQSEVI STLGYLERTQ NEDEAKKYVS PSFQPEFSSG
AEEALTDPTP YVSIGTTYLT AQSLTEAPDV MEGARLPDSI DTSTVSAFSE LLSQTPSFPP
LSIHLGSGDS EHSEDLQPSA LPSTDASTPP VSSGELANIE ATFKPSSEED FYITEPPSLP
PDTEPSEDES KPKLLEPTEA SATELIAQEE IEIFQNSDNT TSVQVSGEAV KVFPSIETPE
AEAIVTAASE TKLEGATLRP HSTSASVIHG VEAGVVPQPS PQTSERPTIL SPLEISPETQ
AALIRGEDST VAAPKQQVPT RMLDSNKQAT LSTTELNTEL ATPSFPLLET SNETSFLIGI
NEESVEGTAV YLPGPDRCKM NPCLNGGTCY PTETSYVCTC VPGYSGDRCE LDFDECHSNP
CRNGATCIDG FNTFRCLCLP SYVGALCEQD TETCDYGWHK FQGQCYKYFA HRRTWDAAER
ECRLQGAHLT SILSHEEQMF VNRVGHDYQW IGLNDKMFEH DFRWTDGSTL QYENWRPNQP
DSFFSTGEDC VVIIWHENGQ WNDVPCNYHL TYTCKKGTVA CGQPPVVENA KTFGKMKPRY
EINSLIRYHC KDGFIQRHLP TIRCLGNGRW AMPKITCLNP SAYQRTYSKK YFKNSSSAKD
NSINTSKHDH RWSRRWQESR R
