ID A0A5F7ZS71_MACMU Unreviewed; 3397 AA.
AC A0A5F7ZS71;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Versican core protein {ECO:0000256|ARBA:ARBA00044099};
DE AltName: Full=Chondroitin sulfate proteoglycan core protein 2 {ECO:0000256|ARBA:ARBA00044230};
DE AltName: Full=Large fibroblast proteoglycan {ECO:0000256|ARBA:ARBA00044263};
DE AltName: Full=PG-M {ECO:0000256|ARBA:ARBA00044266};
GN Name=VCAN {ECO:0000313|Ensembl:ENSMMUP00000068494.1,
GN ECO:0000313|VGNC:VGNC:79445};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000068494.1, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000068494.1}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000068494.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00043896}.
CC -!- SUBUNIT: Interacts with FBLN1. {ECO:0000256|ARBA:ARBA00044030}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000256|ARBA:ARBA00004504}. Secreted, extracellular space,
CC extracellular matrix, interphotoreceptor matrix
CC {ECO:0000256|ARBA:ARBA00004593}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000256|ARBA:ARBA00006838}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR SMR; A0A5F7ZS71; -.
DR STRING; 9544.ENSMMUP00000068494; -.
DR PaxDb; 9544-ENSMMUP00000015111; -.
DR Ensembl; ENSMMUT00000081221.1; ENSMMUP00000068494.1; ENSMMUG00000011513.4.
DR VEuPathDB; HostDB:ENSMMUG00000011513; -.
DR VGNC; VGNC:79445; VCAN.
DR GeneTree; ENSGT00940000156102; -.
DR InParanoid; A0A5F7ZS71; -.
DR OMA; ELTWKPE; -.
DR OrthoDB; 5323609at2759; -.
DR Proteomes; UP000006718; Chromosome 6.
DR Bgee; ENSMMUG00000011513; Expressed in fibroblast and 21 other cell types or tissues.
DR ExpressionAtlas; A0A5F7ZS71; baseline.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0072534; C:perineuronal net; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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:0010001; P:glial cell differentiation; IBA:GO_Central.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; 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 CDD; cd00054; EGF_CA; 2.
DR CDD; cd05901; Ig_Versican; 1.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF6; VERSICAN CORE PROTEIN; 1.
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; SM00445; LINK; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 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; 1.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..3397
FT /note="Versican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023922186"
FT DOMAIN 34..146
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 150..245
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 251..347
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 3090..3126
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3128..3164
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3177..3291
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3295..3355
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 413..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2097..2135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2338..2357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2373..2395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2446..2475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2493..2521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2825..2859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2882..2915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3372..3397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2100..2124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2446..2463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2493..2517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2825..2843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3379..3397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 196..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 294..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 3116..3125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3154..3163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3297..3340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 3326..3353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 3397 AA; 372940 MW; 666928BE22B5CA24 CRC64;
MLININSILW MCSTLIATHA LHKVKVGKSP PLRGSLSGKV SLPCHFSTMP TLPPSYNTSE
FLRIKWSKIE VDKNGKDLKE TTVLVAQNGN IKIGQDYKGR VSVPTHPEAV GDASLTVVKL
LASDAGLYRC DVMYGIDDTQ DTVSLAVDGV VFHYRASTSR YTLNFEAAQK ACLDIGAVIA
TPEQLFAAYE DGFEQCDAGW LADQTVRYPI RAPRVGCYGD MMGKAGVRTY GFRSPQETYD
VYCYVDHLDG DVFHLTAPSK FTFEEAAKEC ENQDARLATV GELQAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTGFPPPDSR FDAYCFKPKE ATTIDLSILA
ETASPSLSKE PQMVSDRTTP IIPLVDELPV IPTEFPPVGN IVDFEQKATV QPQAVTDSLA
TKLPTPTGSS KKPWDMDDYS PSASGPLGKP DISEFKDEVL QSTTVVSHYA TDSWDGVVED
TQTQESVTQI EQIEVGPLVT SMEILKHIPS KEFPVTETPL VTGRMTLESK TEKKTVSTVS
ELVTTGHYGF TLGEEDDEDR TLPVGSDEST LIFDQTPEVV TVSKTSEDTT DTQLEDLETV
LASTTVLPLI MPDNNGSSMD DWEQRETNGR ITEDFFGKYL STTPFPSQHH TEIELFPYSG
DKILVEGIST VIYPSPQTEM THRRERTETL IPEMRTDTYT DEIQEEITKS PFMGKTEEED
FSGMKLSTSP SEPIHVTESS VEMTKSFDFP TLTTKLSAEP TEVRDMEEEF TATPGTIKYD
ENTTTVHLTH STLSVEAATI SKWSWDEDNI TSKPLESTEP SASSKLPPAL LTTVGMNGKD
KEIPSFTEDG ADEFTLIPDS TQKQLEEITD EDIAVHGKFT IRFQPTTSIG IAEKSTLRDS
ITEEKVPPIT STEGRVYATM EGSTLGEVED VDLSKSVSTV PQLAHTSEAE GLAFVSYSST
QEPTTYVDSS HTIPLSVIPK TDWGVLVPSV PSEDEVLGEP SQDIRVIDQT HLEVTISPET
IRTTKLTEET TQEEFPWKEQ TAEKPVPALS STAWTPKEAV TPLDEQEGDG SAYTVSEDEL
LTGSESISVL ETTPVGKIDH SVSYPPGAIT EHKVKTVEVV TLTPSIGPKV SISPGPEQKY
ETEGSSTTGF TSSLSPFSTH VTQLMEETTA EKISLEDIDL GSGLFEKPKA TELIEFSTIK
ATVPSDITTA FSSVDRLHTT SALKPASAIT KKPPLIDREP GEETTSDMVI IGESTSHVPP
TTLEDIVAKE TETDIDREYF TTSSPPTTQP TRPPTVEDKE AFGPQALSTP QPPARTKFHP
DINVYIIEVR ENKTGRMSDL SVIGHPIDSE SKEDEPCSEE TDPVHDLMAE ILPEFPDIIE
IDLYHSEENE EEEEECANAT DVTTTPSVQY INGKHLVTTV PKDPEAAEAR RGQFESVAPS
QNFSDSSESD TRPFVIAETE LSTAVQPNGS TETTESLEIT WKPETYPETS EHFSGGEPDV
FPTVPFHEEF ESGTAIKGAE SVTERVTEVG HQAHEHIETV SLFPEESSGE IAIDQESQKI
AFARPTEVTF GEEVEKSTSV TYTPTVVPSS ASAYVSEEKA VTLIGNLWPD DLLSTKESWV
EATPRQVVEL SGSSSIPVTE GSGEAEADED TMFTIVTDLS QRNTTDTLIT LDTSRIITES
FFEVPATTIY SVSEQPSAKV VPTKFVSETD TSEWISSTSA EEEKRKEEEG TTGTASTVEV
YSPTQRSDQL ILPSELESSN VVVSNDSGTR KSFMSLTTPT QSEREMTDST LVFTETNTLE
NLEAQTTEHS SIHQPGVQEG LTTLPGSPAS LFMEQGSGEA AADPETTTVS SFSLNLEYEI
QAKKEAAGTL SPYVETTFST EPTGLVMSTV MDREVAENIS QTSREILISE RLGEPNHGAE
IRGFSTGFPL EEDFSGDFKE YSTVSHPIAK EETVMMEGSG DAAFRDTQTS PSTVLTSVHI
SHISDSEGPS STMVSTSAFP WEEFTSSAEG SGEQLVIVSS SVDPVLPSAI GRFSGTASSI
IDEGLGEVDT VNEIDRRSTI LPTAEVEGTK APVEKEEVKV SGTISTNFPQ TMEPAKLWSR
QEVNPERQEI ESETTSEEQI QEEKSFESPQ NSPATEQTIF DSQTFTETEL KTTGYSVLTT
KKTYSDDKEM EEEGTSLANM STPDPVANGM ESFTTLPEAT EKSHFFLATA LVTESIPAEH
VVTDSPIKEE ESTKHFPKGM RPTIQELDTE LLFSGLGSGE EVLPTLPTKS VNFTEVEQIR
NTFYPHSSQV ESTSSDKTED SNRMENVAKE VGPLVSQTDI FEGNESVTST TLIEILSDPG
AEGPTVAPLP FSANIGHPQN QTLRWAEEIQ TSRPQTITEQ DSNKNSSTAE INETTTSSTD
FLARVYGFEM AKEFVTSAPK PSDMFYEPSG EGSGEADIVD SFHTSATTQA TTQESSTTFV
SDGSLEKHPE VPSTKAVTAD GFPTIAAMLP FHSEQNKSSP DPTSTLSNTV SYERSTDGSF
QDHFREFEDS TLKPNRKKPT ENIIIDLDKE DKDLILTITE STILEILPEL TSDKNTIIDI
DHTKPVYEDI LGMQTDIDPE VPSEPHDSND ESNDYSTQVQ ETYEAAVNRS LTEETFEGSG
DVLLASYTQA THDESMTYED RSQLDHMDFN FTTGIPAPST ETELDILLPT ATSLPISRKS
ATVIPETEEI KAEAKALDDM FESSTLSDGQ AIADQSEIIP TLGQFERTQE EYEDKKHAGP
SFQPEFSSGV EEALVDHTPY LSIATTHLVD ESLTEVPNVM EGSNAPYYTD TTLAVSAFAK
LSSQTPSSPL TIYSGSEASG HTEIPQPSAL PGVDVGSSVM SPEDSFKEIH VNIEATFKPS
SEEYLHITEP PSISPDTKLE PSEEDGKPEL LEETEASPTE FIAVEGTEIL QDFQNKTDGQ
VSGEAIKMFP TIKTTEAGTV ITTANEIKLE GATQWPHSTS ASATYGIEAG VMPWLSPQTS
ERPTLSSSPD INPETQAALI RGQDSTVAAS EQQVTARILD SNNQATVSPV EFNTEVATPP
FSLLETSNET DFLIGINEES VEGTAIYLPG PDRCKMNPCL NGGTCYPTET SYVCTCVPGY
SGDQCELDFD ECHSNPCRNG ATCVDGFNTF RCLCLPSYVG ALCEQDTETC DYGWHKFQGQ
CYKYFAHRRT WDAAERECRL QGAHLTSILS HEEQTFVNRV GHDYQWIGLN DKMFEHDFRW
TDGSTLQYEN WRPNQPDSFF SAGEDCVVII WHENGQWNDV PCNYHLTYTC KKGTVACGQP
PVVENAKTFG KMKPRYEINS LIRYHCKDGF IQRHLPTIRC LGNGRWAIPK ITCMNPSAYQ
RTYSMKYFKN SSSAKDNSIN TSKHDHRWSR RWQETRR
//
