FINC_RABIT
ID FINC_RABIT Reviewed; 2427 AA.
AC Q28749; G1U9R6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Fibronectin {ECO:0000250|UniProtKB:P02751};
DE Short=FN;
DE Flags: Fragment;
GN Name=FN1 {ECO:0000250|UniProtKB:P02751};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred;
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2328-2427.
RX PubMed=7579058; DOI=10.1681/asn.v5122087;
RA Sady S.P., Goyal M., Thomas P.E., Wharram B.L., Wiggins R.C.;
RT "Fibronectin mRNA in the developing glomerular crescent in rabbit
RT antiglomerular basement membrane disease.";
RL J. Am. Soc. Nephrol. 5:2087-2090(1995).
CC -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC including collagen, fibrin, heparin, DNA, and actin. Fibronectins are
CC involved in cell adhesion, cell motility, opsonization, wound healing,
CC and maintenance of cell shape (By similarity). Involved in osteoblast
CC compaction through the fibronectin fibrillogenesis cell-mediated matrix
CC assembly process, essential for osteoblast mineralization. Participates
CC in the regulation of type I collagen deposition by osteoblasts (By
CC similarity). {ECO:0000250|UniProtKB:P02751,
CC ECO:0000250|UniProtKB:P11276}.
CC -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC variants, connected by 2 disulfide bonds near the carboxyl ends; to a
CC lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and
CC COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP.
CC Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain);
CC this interaction enhances fibronectin fibril assembly. TNFAIP6 may act
CC as a bridging molecule between FN1 and THBS1 (By similarity). Interacts
CC with TNR; the interaction inhibits cell adhesion and neurite outgrowth
CC (By similarity). Interacts with FST3 and MYOC (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P02751}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. The diversity of isoforms
CC depends on the V region and either of the two extra domains which can
CC be either included or excluded (partially or completely for the V
CC region). {ECO:0000305};
CC Name=1;
CC IsoId=Q28749-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by
CC hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms),
CC made by fibroblasts, epithelial and other cell types, is deposited as
CC fibrils in the extracellular matrix.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.
CC -!- PTM: Forms covalent cross-links mediated by a transglutaminase, such as
CC F13A or TGM2, between a glutamine and the epsilon-amino group of a
CC lysine residue, forming homopolymers and heteropolymers (e.g.
CC fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
CC {ECO:0000250|UniProtKB:P11276}.
CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting
CC fibronectin activation and matrix formation.
CC {ECO:0000250|UniProtKB:P11276}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia.
CC {ECO:0000250|UniProtKB:P07589}.
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DR EMBL; AAGW02042615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S80206; AAB35493.1; -; mRNA.
DR AlphaFoldDB; Q28749; -.
DR SMR; Q28749; -.
DR STRING; 9986.ENSOCUP00000008718; -.
DR Ensembl; ENSOCUT00000010116; ENSOCUP00000008718; ENSOCUG00000010104. [Q28749-1]
DR eggNOG; ENOG502QPTS; Eukaryota.
DR GeneTree; ENSGT00940000155126; -.
DR HOGENOM; CLU_000916_0_0_1; -.
DR OMA; TTNPPMG; -.
DR TreeFam; TF329915; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000010104; Expressed in upper lobe of left lung and 15 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd00061; FN1; 12.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 17.
DR Gene3D; 2.10.10.10; -; 2.
DR Gene3D; 2.60.40.10; -; 17.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013806; Kringle-like.
DR Pfam; PF00039; fn1; 11.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 17.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 17.
DR SUPFAM; SSF49265; SSF49265; 11.
DR SUPFAM; SSF57440; SSF57440; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01253; FN1_1; 12.
DR PROSITE; PS51091; FN1_2; 12.
DR PROSITE; PS00023; FN2_1; 2.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 17.
PE 2: Evidence at transcript level;
KW Acute phase; Alternative splicing; Cell adhesion; Cell shape;
KW Disulfide bond; DNA-binding; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Oxidation; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Sulfation.
FT CHAIN <1..2427
FT /note="Fibronectin"
FT /id="PRO_0000158531"
FT DOMAIN <1..40
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 45..88
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 89..132
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 134..178
FT /note="Fibronectin type-I 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 179..223
FT /note="Fibronectin type-I 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 256..295
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 305..353
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 365..413
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 418..461
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 466..508
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 509..552
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 560..653
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 667..762
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 763..852
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 859..948
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 949..1038
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1039..1125
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1126..1220
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1221..1309
FT /note="Fibronectin type-III 8; extra domain B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1310..1402
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1403..1490
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1491..1584
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1585..1676
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1677..1764
FT /note="Fibronectin type-III 13; extra domain A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1765..1858
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1859..1945
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1946..2036
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2144..2238
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2245..2289
FT /note="Fibronectin type-I 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2290..2332
FT /note="Fibronectin type-I 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2334..2374
FT /note="Fibronectin type-I 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND 857..1122
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 2..222
FT /note="Fibrin- and heparin-binding 1"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 258..558
FT /note="Collagen-binding"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 414..427
FT /note="Critical for collagen binding"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1308..1581
FT /note="Cell-attachment"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1610..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..2032
FT /note="Heparin-binding 2"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1854..2032
FT /note="Binds to FBLN1"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 2033..2152
FT /note="V region (type III connecting segment, IIICS)"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 2247..2378
FT /note="Fibrin-binding 2"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOTIF 1565..1567
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT SITE 613
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT SITE 616
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 826
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 831
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 2425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1023
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 2..28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 47..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 73..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 91..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 117..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 136..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 163..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 181..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 208..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 258..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 283..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 310..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 324..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 370..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 384..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 420..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 446..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 468..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 493..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 511..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 537..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2247..2276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2274..2286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2292..2319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2317..2329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2336..2362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2360..2371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT NON_TER 1
SQ SEQUENCE 2427 AA; 267281 MW; 153E0231A30FEDDD CRC64;
GCYDNGKHYQ INQQWERTYL GNALVCTCYG GSRGFNCESK PEPEETCFDK YTGNTYRVGD
TYERPKDSMI WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL
GNGKGEWTCK PIAEKCFDHA AGTSYVVGET WEKPYQGWMM VDCTCLGEGS GRITCTSRNR
CNDQDTRTSY RIGDTWSKKD NRGNLLQCIC TGNGRGEWKC ERHASLQTTS TGSGPFSDVR
AAVYQPQPHP QPAPYGHCVT DSGVVYSEGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHTVLVQT
RGGNSNGALC HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC
TTNEGVMYRI GDQWDKQHDM GHMMRCTCVG NGRGEWTCVA YSQLRDQCIV DDITYNVNDT
FHKRHEEGHM LNCTCFGQGR GRWKCDPVDQ CQDSETRTFY QIGDSWEKYV HGVRYQCYCY
GRGIGEWHCQ PLQTYPGTSG PVQVIITETP SQPNSHPIQW NAPEPSHISK YILRWRPKNS
VGRWKEATIP GHLNSYTIKG LRPGVMYEGQ LISIQQYGHR EVTRFDFTTT STSTPVTSNT
VTGETTPLSP VVATSESVTE ITASSFVVSW VSASDTVSGF LVEYELSEEG DEPKYLDLPS
TVTSVNIPDL LPGRKYIVNV YQISEEGKQS LILSTSQTTA PDAPPDPTVD QVDDTSIVVR
WSRPQAPITG YRVVYSPSVE GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQESA
PVFIQQETTG VPRSDEVPPP KDLQFVEVTD VKVTIMWTPP DSAVTGYRVD VLPVHLPGEN
GQRLPVSRNT FAEITGLSPG VTYYFKVFAV NHGRESRPLT AQQATKLDAP TNLQFVNETD
SSVLVIWTPP RARITGYQLT IGPTRGGQPK QHNVGPTVSK YLLRNLQPGS EYTVTLIAVK
GNNQSPKVTG VFTTLQPQSS IPPYSTEVTE TSIVITWTPA PRIGFKLGVR PSQGGEAPRE
VTSESGSIVV SGLTPGVEYV YSIQVLRDGK ERDAPIVNTV VTPLSPPTNL HLEANPDTGV
LTVSWEKSTT PDITGYRITT TPTNGQQGYS LEEVVHADQN SCIFENLSPG LEYNVSVYTV
KDDKESVPVS DTIIPEVPQL TDLSFVDITD SSIGLRWTPL NSSTIIGYRI TVVAAGEGIP
IFEDFVDSSV GYYTVTGLEP GIDYDISVIT LINGGESAPT TLTQQTAVPS PTDLRFTNIG
PDTMRVTWAP PPSIELTNFL VRYSPVKNEE DVAELSISPS DNAVVLTNLL PGTEYLVSVS
SVYEQHESTP VRGRQKTGLD APTGIDFSDV TPNSFTVYWT PPRAPITGFW IRHHPEHGVG
RPREDRVPPS RNSITLTNLN PGTEYVVSIV ALNGREQSPP LIGQQSTVSD VPRDLEVIAS
TPTSLLISWE APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK PGADYTITVY
AVTGRGDSPA SSKPISIDYH TEIDKPSQMQ VTDVQDNSIS VRWLPSSSPV TGYRVTTTPK
NGAGPTKTKT AGPDQTEMTI EGLQPTVEYV VSVYAQNRNG ESQPLVQTAV TNIDRPKGLA
FTDVDVDSIK IAWESPQGQV SRYRVTYSSP EDGIHELFPA PDGEEDTAEL QGLRPGSEYT
VSVVALHDDM ESQPLIGTQS TAIPAPTNLK FTQVTPTSLS AQWTPPNVQL TGYRVRVTPK
EKTGPMKEIN LAPDSSSVVV SGLMVATKYE VSVYALKDTL TSRPVQGVIT TLENVSPPRR
ARVTDATETT ITISWRTKTE TITGFRVDAI PANGQNPIQR IIKPDVRSYT ITGLQPGTDY
KIHLYTLNDN AQSSPVIIDA STAIDAPSNL HFLATTPNSL LVSWQPPRAK ITGYIIKFEK
PGSPPREVVP RPRPGVTEAT ITGLEPGTEY TIYIIALKNN QKSDPLIGRK KTDELPQLVT
LPHPNLHGPE ILDVPSTVQK TPFITNPGYD TGNGIQLPGT SGQQPSVGQQ MIFEEHGFRR
TTPPTTATPV KLRPRPYLPN VDEDIQIGHV PRGDVDYHLY PHVLGLNPNA STGQEALSQT
TISWTPFQES SEYIISCHPV GTDEQPLQFR VPGTSTSATL TGLTRGATYN IIVEALKDQR
RHKVREEVVT VGNSVNEGLN QPTDDSCFDP YTVTHYAVGE EWERLSESGF KLSCQCLGFG
SGHFKCDSSK WCHDNGVNYK IGEKWDRQGE NGQMMSCTCL GNGKGEFKCD PHEATCYDDG
KTYHVGEQWQ KEYLGAICSC TCFGGQRGWR CDNCRRPGVE PSPDSSTGHS YNQYTQRYHQ
RTNTNVNCPI ECFMPLDVQA DREDSRE
