ID CSPG2_CHICK Reviewed; 3562 AA.
AC Q90953; Q90945;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 08-NOV-2023, entry version 147.
DE RecName: Full=Versican core protein;
DE AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
DE Short=Chondroitin sulfate proteoglycan 2;
DE AltName: Full=Large fibroblast proteoglycan;
DE AltName: Full=PG-M;
DE Flags: Precursor;
GN Name=VCAN; Synonyms=CSPG2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0 AND V1).
RC STRAIN=White leghorn; TISSUE=Limb bud;
RX PubMed=8314802; DOI=10.1016/s0021-9258(19)85261-4;
RA Shinomura T., Nishida Y., Ito K., Kimata K.;
RT "cDNA cloning of PG-M, a large chondroitin sulfate proteoglycan expressed
RT during chondrogenesis in chick limb buds. Alternative spliced multiforms of
RT PG-M and their relationships to versican.";
RL J. Biol. Chem. 268:14461-14469(1993).
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 -!- 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=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=V0;
CC IsoId=Q90953-1; Sequence=Displayed;
CC Name=V1;
CC IsoId=Q90953-2; Sequence=VSP_003093;
CC -!- TISSUE SPECIFICITY: Prechondrogenic condensation area of developing
CC limb buds.
CC -!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
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DR EMBL; X60226; CAA42787.1; -; mRNA.
DR EMBL; D13542; BAA02742.1; -; mRNA.
DR PIR; A47171; A47171.
DR RefSeq; NP_990118.1; NM_204787.1. [Q90953-1]
DR SMR; Q90953; -.
DR STRING; 9031.ENSGALP00000025144; -.
DR GlyCosmos; Q90953; 24 sites, No reported glycans.
DR PaxDb; 9031-ENSGALP00000025144; -.
DR GeneID; 395565; -.
DR KEGG; gga:395565; -.
DR CTD; 1462; -.
DR VEuPathDB; HostDB:geneid_395565; -.
DR eggNOG; ENOG502QRBE; Eukaryota.
DR InParanoid; Q90953; -.
DR PhylomeDB; Q90953; -.
DR PRO; PR:Q90953; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0072534; C:perineuronal net; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
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; 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; SM00406; IGv; 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; 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; Proteoglycan; Reference proteome; Repeat;
KW Secreted; Signal; Sushi.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..3562
FT /note="Versican core protein"
FT /id="PRO_0000017525"
FT DOMAIN 27..143
FT /note="Ig-like V-type"
FT DOMAIN 149..244
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 250..346
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 3254..3290
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3292..3328
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3341..3455
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 3459..3519
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 466..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2030..2063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2463..2482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2496..2522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2918..2947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2984..3006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3108..3144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3111..3131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P13611"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1628
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P13611"
FT CARBOHYD 1751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2082
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P13611"
FT CARBOHYD 2088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2089
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2386
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P13611"
FT CARBOHYD 2507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3069
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..129
FT /evidence="ECO:0000250"
FT DISULFID 171..242
FT /evidence="ECO:0000250"
FT DISULFID 195..216
FT /evidence="ECO:0000250"
FT DISULFID 269..344
FT /evidence="ECO:0000250"
FT DISULFID 293..314
FT /evidence="ECO:0000250"
FT DISULFID 3258..3269
FT /evidence="ECO:0000250"
FT DISULFID 3263..3278
FT /evidence="ECO:0000250"
FT DISULFID 3280..3289
FT /evidence="ECO:0000250"
FT DISULFID 3296..3307
FT /evidence="ECO:0000250"
FT DISULFID 3301..3316
FT /evidence="ECO:0000250"
FT DISULFID 3318..3327
FT /evidence="ECO:0000250"
FT DISULFID 3334..3345
FT /evidence="ECO:0000250"
FT DISULFID 3362..3454
FT /evidence="ECO:0000250"
FT DISULFID 3430..3446
FT /evidence="ECO:0000250"
FT DISULFID 3461..3504
FT /evidence="ECO:0000250"
FT DISULFID 3490..3517
FT /evidence="ECO:0000250"
FT VAR_SEQ 485..1411
FT /note="Missing (in isoform V1)"
FT /evidence="ECO:0000303|PubMed:8314802"
FT /id="VSP_003093"
SQ SEQUENCE 3562 AA; 388083 MW; 9BC566E88C1602D2 CRC64;
MLLNIKSIIW MCSTLAITYM LPKVKAEKKT LVKGSLSGTS VLPCFFSTTP TIASSYAAEY
LRIKWSKVEL DKSGKDAKET TVLVAQNGNI KIGQNYKDRV SVPTHSEETG DASLTFSRLR
ASDAGVYRCD VMYGVEDTQG IVSLAVDGVV FHYRAATSRY TLNFTQAQQT CLDNGAVIAS
PEQLKAAYED GFEQCDAGWL SDQTVRYPIR HPRIGCFGDK MGKKGVRTYG RRFPNETYDV
YCYVEHMQDE VVHVSVPEKL TFEEAKELCR KRDGVLASVG NMYVAWRNGF DQCDYGWLAD
GSVRYPASVA RPQCGGGLLG VRTLYRYENQ TGFPYPDSKF DAYCYERKKI VSEPTTVKLV
TTLKTDSVEL SSAKVTLKPS VFESSVTEVA VTKTKVPAWE EATLETEDTK MTTEVAEEKR
EMEVLMENIK LTTLLPQTVT DGEISPYDTL GRTEYDVSPR LTESTSAALE VEHTYSEAEL
SEEQGRSEST EDAFLTSVVF QDSTAVAKSS TGSWEDIETG DTQKHDGDNQ TEQIEVGPVM
TATDSLVPAS QRELPRTGSS VSLTKENLYL GSHSTKEPTK KSMEAKSDKK LTTVVIPKAL
FTDQYDLTTG GEGRESMYTV MPDRVSGVAL VSIPESDVPA VSETLMDELA VTTGQSSTAD
ESTPFIKFSS SATELDNEAS AEGSREDLKD VHLTTSSGIP VSFTLFTANE TGSEVTALSE
STSAPQKFEE GITSVLHSSQ QTEGSAILEK QEKTKEPEMS TIDAKVLYIT TVVPASVTAG
SEGRFGSEKF THTPPVSGMW LQTDKDQVYM TEETSHTKRI ELDTEDDISG MEPTSSPGQI
IEYTKHLGAP VSAVTDETKT SMETAETESD EEVVSADFDQ TKGTTEVFHT SSSLDLEKFT
LSKIPEDESS ATVKSFSSSS GTVLPTAVAT VLEVTDHEAD ETSGYVLNMT FSTPEGEQRK
ATEKSPATSA EDEVSTGTEI SKYTMTEGGQ ISSVTSAEKE SVAALQEREE QPSVGLPETK
EPFKFTDVTE IETTVPQREG DTSLVPVTVG SEDIGEMQVT DHTSFDSIIH TEATVTSTKA
SEVFPKELST KDQDRELGTA MGSTLPVTSV QMHEQKTTAG FESPQTTTQE KHDEMGSAYD
EMYPATELSV PALMLTEYGQ VSGPVETSTR SLHLTGTPKA ETATDQEEKI TEAVPVTFGT
QAKVYESKGT TTREEDRDVG SWNSVLPPHT MLSSPSTAGS ISLLTLGASP SQTPEGSGIS
EELEEVKTVP FSSRATDKTT VISDLTTSSI SAVDKIQPTS ASKPFVSSKS PRIIPEEDEE
VTSSDIIVID ESISPSKASA EDDLTGKMVE PEIDKEYFTS STATAVARPT APPTVMEATE
ALQPQEVSPT SHPDSGTDIR LYVIQITGND TDHPVNEFLD LFSRHILPHA VDETHTDAES
AQTEPCTSDS VQDSSEYIIL DPFFPNFMDF EEEEEDCENT TDVTTPPALQ FINGKQQVTS
APKSTKAEEA RSDQIESVAH SKNVTFSQIN ETNTFIISET EASGTMQPSK AGEVMGAFEV
TQPTADVAML EPVYSGESEV TTTDKYLEIT SVYEQSPKKN KETVMWHGTE ESSTKDTKNL
LLITNESSGD GSTESDLSRS VFTEILTMSS HEDSEKISHT TSVPTILSVE RSAVTAAPSA
DSDTATVGID VKDLIPKGGT ATPGNYYKST IKLDAEFPFE SNPEATSHTT KPDMTASSFI
VLEGSGDVEE NSTLASAMTT ETAVAETLSV QDTSLGSGTV LPTEISVTIS EITPALPGGT
RILYSTFDQS SEATVSTNFV SELIMEQVVG SSVATEKKVE DEKEVQTTVY SSQEISTTDA
KGKSELDEFG STTNEVRTVS QEPTPLREIV PITGTMHSEI KKVTATPFLR EKLFINEGSA
EEPADLFAGS PTRKVVSTDS PFTDSGSGDI DVITESATLT SVPSRSVIET QTVKHEGNIN
VISVSLKNTT TEYEEHIGTG GPVTSVSSTG SDGLTEESEV AIEMSENVFS TENQGEPTQE
AVPTYTAPSD IKSRLGSRRE VTSHVTPVIR TKDLETAEVT SSPESVVNNS TLDTMVTHGT
IRAVAESTES KKGKGSFSAV SLGKILMIEH GSGEELKVDS STTKLMSNGP TEKLLGSHFS
FFDQGSGEAE TLTESFTKAS VSPTGKPEPQ EQYGRKTVSM PSAVVHAYTA EPNELVTSTE
HDITSLQTVT DTEMEEKAAN ELTVTSFATN LPLSEDVHSW EDRPREILPK AIESSGEATE
DPFFISTQAN HEHVEFLSVP TIRPHSEENK VEAESDEKIL LPFNNDRVTE SAVIERKYLS
SPFTDTEQEE ELVQNIFPTE DIPRLFLTPK EEKPTNNELI SDPLFSGQGS GDEFTVIPSV
ESLAVKETTN TLSPWPFHPA SVGPKLSTDK TQVFESGSTD SNAEINEEIT TTAAELTETA
YSMATSSPAL EEESSSHSNS KDKDITHYFL VIEDPYNKEM DHRRGENGTS RPLPTPGDVS
LEESSHMLTT DDVTPVSVIL SETPYLEMGK SLATSATKMP SRVLPESSGE GSGWDGVSDS
FAPDTLTHST APSVMEVELT ASSHIPGVYS EVMTTHVPGD GSQTVITGLA SLFTEEKEIV
ANRTAADPKT GTSEELTSDT GMSLDIIPVV DDRRHVTLNV SVYGDITLIE ERLQIPSEKT
TIIDMDHSKS MPEDIISVQT MPNLVIRSTQ VSDDNMKAEE DKYDSILNFS TVEENSFGSG
DNLSLTTSIQ PSSESVTAGH GPKLVDKDLG SGYAMQFATE TLTTTVLNEL GIFLPTVPSL
VSPHMPHESK ESEFEAKHIG RTSTTDDVYE PYTSANNQVI TDQSKTMSIS GFSGMGQEES
GDKKPMIPSL TPDLTMETEK ALTTDTFDVS MVTTQSMSQH ATVSSSSSEE KHSTVYMQTK
SASTEYEETD SVSLNSVSQN PKSSVTVWLV NGVSKYPEVI IPSTSSAKDS DQSDHSSDGT
FKEVSSDMAA TYKPPTTDLD TTVSSLLVFS PEPESESIST ESTPHFNKFV TERSEETESS
VNDLIIEENA TVSGDSPSIH DYPTAFWNFG ERTSTDVPKL STIEVEFSSE RVKNPSQESD
RSTERERPRL SSAPVSDSPN SIEVGVFKPD QEAVTMLTSS LEPLDRSLET QSALLGPLLG
QQEITTISSN IATNNTAPGN NPYSNEQSTI SSELLNTIEL VTSSFSLPEV TNGSDFLIGT
SVGSVEGTAV QIPGQDPCKS NPCLNGGTCY PRGSFYICTC LPGFNGEQCE LDIDECQSNP
CRNGATCIDG LNTFTCLCLP SYIGALCEQD TETCDYGWHK FQGQCYKYFA HRRTWDTAER
ECRLQGAHLT SILSHEEQVF VNRIGHDYQW IGLNDKMFER DFRWTDGSPL QYENWRPNQP
DSFFSAGEDC VVIIWHENGQ WNDVPCNYHL TYTCKKGTVA CGQPPVVENA KTFGKMKPRY
EINSLIRYHC KDGFIQRHIP TIRCQGNGRW DMPKITCMNP STYQRTYSKK YYYKHSSSGK
GTSLNSSKHY HRWIRTWQDS RR
//
