FINC_BOVIN
ID FINC_BOVIN Reviewed; 2478 AA.
AC P07589;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 4.
DT 25-MAY-2022, entry version 172.
DE RecName: Full=Fibronectin {ECO:0000250|UniProtKB:P02751};
DE Short=FN;
DE Contains:
DE RecName: Full=Anastellin;
DE Flags: Precursor;
GN Name=FN1 {ECO:0000250|UniProtKB:P02751};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP PROTEIN SEQUENCE OF 33-2478.
RX PubMed=3780752; DOI=10.1111/j.1432-1033.1986.tb10464.x;
RA Skorstengaard K., Jensen M.S., Sahl P., Petersen T.E., Magnusson S.;
RT "Complete primary structure of bovine plasma fibronectin.";
RL Eur. J. Biochem. 161:441-453(1986).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-2476.
RX PubMed=6218503; DOI=10.1073/pnas.80.1.137;
RA Petersen T.E., Thorgersen H.C., Skorstengaard K., Vibe-Pedersen K.,
RA Sahl P., Sottrup-Jensen L., Magnusson S.;
RT "Partial primary structure of bovine plasma fibronectin: three types of
RT internal homology.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:137-141(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2383-2478.
RX PubMed=6304699; DOI=10.1073/pnas.80.11.3218;
RA Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.;
RT "Isolation and characterization of cDNA clones for human and bovine
RT fibronectins.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3218-3222(1983).
RN [5]
RP GLYCOSYLATION AT THR-280, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19674964; DOI=10.1074/mcp.m900211-mcp200;
RA Darula Z., Medzihradszky K.F.;
RT "Affinity enrichment and characterization of mucin core-1 type
RT glycopeptides from bovine serum.";
RL Mol. Cell. Proteomics 8:2515-2526(2009).
RN [6]
RP SEROTONYLATION.
RX PubMed=25128524; DOI=10.1152/ajplung.00162.2014;
RA Penumatsa K.C., Toksoz D., Warburton R.R., Hilmer A.J., Liu T., Khosla C.,
RA Comhair S.A., Fanburg B.L.;
RT "Role of hypoxia-induced transglutaminase 2 in pulmonary artery smooth
RT muscle cell proliferation.";
RL Am. J. Physiol. 307:L576-L585(2014).
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 -!- FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation.
CC This fibronectin polymer, named superfibronectin, exhibits enhanced
CC adhesive properties. Both anastellin and superfibronectin inhibit tumor
CC growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and
CC inhibits lysophospholipid signaling. {ECO:0000250|UniProtKB:P02751}.
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 -!- INTERACTION:
CC P07589; Q15113: PCOLCE; Xeno; NbExp=2; IntAct=EBI-11147184, EBI-8869614;
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 domain which can
CC be either included or excluded (partially or completely for the V
CC region). {ECO:0000305};
CC Name=1;
CC IsoId=P07589-1; 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: Proteolytic processing produces the C-terminal NC1 peptide,
CC anastellin. {ECO:0000250}.
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:0000269|PubMed:25128524}.
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DR EMBL; AAFC03125045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03065407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K00800; AAA30521.2; -; mRNA.
DR PIR; A26452; FNBO.
DR AlphaFoldDB; P07589; -.
DR SMR; P07589; -.
DR IntAct; P07589; 7.
DR STRING; 9913.ENSBTAP00000010925; -.
DR GlyConnect; 721; 1 O-Linked glycan (1 site).
DR iPTMnet; P07589; -.
DR PaxDb; P07589; -.
DR PeptideAtlas; P07589; -.
DR PRIDE; P07589; -.
DR eggNOG; ENOG502QPTS; Eukaryota.
DR InParanoid; P07589; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0043394; F:proteoglycan binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007044; P:cell-substrate junction assembly; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
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; 16.
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; 12.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 16.
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 1: Evidence at protein level;
KW Acute phase; Alternative splicing; Angiogenesis; Cell adhesion; Cell shape;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparin-binding; Isopeptide bond; Oxidation; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..32
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT CHAIN 33..2478
FT /note="Fibronectin"
FT /id="PRO_0000158527"
FT CHAIN 628..702
FT /note="Anastellin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390478"
FT DOMAIN 51..91
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 96..139
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 140..183
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 185..229
FT /note="Fibronectin type-I 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 230..274
FT /note="Fibronectin type-I 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 307..344
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 356..404
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 416..464
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 469..517
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 517..559
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 560..603
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 611..706
FT /note="Fibronectin type-III 1"
FT DOMAIN 718..813
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 814..903
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 910..1001
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1002..1089
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1090..1176
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1177..1271
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1272..1360
FT /note="Fibronectin type-III 8; extra domain B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1361..1452
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1453..1541
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1542..1635
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1636..1727
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1728..1815
FT /note="Fibronectin type-III 13; extra domain A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1816..1909
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1910..1996
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1997..2087
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2195..2289
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2296..2340
FT /note="Fibronectin type-I 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2341..2383
FT /note="Fibronectin type-I 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2385..2428
FT /note="Fibronectin type-I 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND 908..1173
FT REGION 53..273
FT /note="Fibrin- and heparin-binding 1"
FT REGION 309..609
FT /note="Collagen-binding"
FT REGION 465..478
FT /note="Critical for collagen binding"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1359..1632
FT /note="Cell-attachment"
FT REGION 1484..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1666..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1813..2083
FT /note="Heparin-binding 2"
FT REGION 1905..2083
FT /note="Binds to FBLN1"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 2084..2203
FT /note="V region (type III connecting segment, IIICS)"
FT REGION 2150..2170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2298..2429
FT /note="Fibrin-binding 2"
FT MOTIF 1616..1618
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOTIF 2183..2185
FT /note="Cell attachment site"
FT /evidence="ECO:0000250"
FT COMPBIAS 1485..1499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 664
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT SITE 667
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 33
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT MOD_RES 877
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 882
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2394
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 2476
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6218503"
FT CARBOHYD 280
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19674964"
FT CARBOHYD 431
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 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2156
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3780752"
FT CARBOHYD 2157
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3780752"
FT CARBOHYD 2200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..79
FT /evidence="ECO:0000250"
FT DISULFID 77..88
FT /evidence="ECO:0000250"
FT DISULFID 98..126
FT /evidence="ECO:0000250"
FT DISULFID 124..136
FT /evidence="ECO:0000250"
FT DISULFID 142..170
FT /evidence="ECO:0000250"
FT DISULFID 168..180
FT /evidence="ECO:0000250"
FT DISULFID 187..216
FT /evidence="ECO:0000250"
FT DISULFID 214..226
FT /evidence="ECO:0000250"
FT DISULFID 232..261
FT /evidence="ECO:0000250"
FT DISULFID 259..271
FT /evidence="ECO:0000250"
FT DISULFID 309..336
FT /evidence="ECO:0000250"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 361..387
FT /evidence="ECO:0000250"
FT DISULFID 375..402
FT /evidence="ECO:0000250"
FT DISULFID 421..447
FT /evidence="ECO:0000250"
FT DISULFID 435..462
FT /evidence="ECO:0000250"
FT DISULFID 471..499
FT /evidence="ECO:0000250"
FT DISULFID 497..509
FT /evidence="ECO:0000250"
FT DISULFID 519..546
FT /evidence="ECO:0000250"
FT DISULFID 544..556
FT /evidence="ECO:0000250"
FT DISULFID 562..590
FT /evidence="ECO:0000250"
FT DISULFID 588..600
FT /evidence="ECO:0000250"
FT DISULFID 2298..2327
FT /evidence="ECO:0000250"
FT DISULFID 2325..2337
FT /evidence="ECO:0000250"
FT DISULFID 2343..2370
FT /evidence="ECO:0000250"
FT DISULFID 2368..2380
FT /evidence="ECO:0000250"
FT DISULFID 2387..2413
FT /evidence="ECO:0000250"
FT DISULFID 2411..2422
FT /evidence="ECO:0000250"
FT DISULFID 2459
FT /note="Interchain (with C-2462)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 2463
FT /note="Interchain (with C-2458)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT CROSSLNK 35
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 36
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 48
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
SQ SEQUENCE 2478 AA; 272154 MW; 2BAD301A8112FEDC CRC64;
MLGGPGPGLL LLLAVLSLGT AVPSAGASKS RRQAQQIVQP QSPLTVSQSK PGCYDNGKHY
QINQQWERTY LGSALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYRVG DTYERPKDSM
IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDTWRRPHE TGGYMLECVC LGNGKGEWTC
KPIAEKCFDQ AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG SGRITCTSRN RCNDQDTRTS
YRIGDTWSKK DNRGNLLQCI CTGNGRGEWK CERHTSLQTT SAGSGSFTDV RTAIYQPQPH
PQPPPYGHCV TDSGVVYSVG MQWLKTQGNK QMLCTCLGNG VSCQETAVTQ TYGGNSNGEP
CVLPFTYNGK TFYSCTTEGR QDGHLWCSTT SNYEQDQKYS FCTDHTVLVQ TRGGNSNGAL
CHFPFLYNNH NYTDCTSEGR RDNMKWCGTT QNYDADQKFG FCPMAAHEEI CTTNEGVMYR
IGDQWDKQHD MGHMMRCTCV GNGRGEWTCV AYSQLRDQCI VDGITYNVND TFHKRHEEGH
MLNCTCFGQG RGRWKCDPVD QCQDSETRTF YQIGDSWEKY LQGVRYQCYC YGRGIGEWAC
QPLQTYPDTS GPVQVIITET PSQPNSHPIQ WSAPESSHIS KYILRWKPKN SPDRWKEATI
PGHLNSYTIK GLRPGVVYEG QLISVQHYGQ REVTRFDFTT TSTSPAVTSN TVTGETTPLS
PVVATSESVT EITASSFVVS WVSASDTVSG FRVEYELSEE GDEPQYLDLP STATSVNIPD
LLPGRKYTVN VYEISEEGEQ NLILSTSQTT APDAPPDPTV DQVDDTSIVV RWSRPRAPIT
GYRIVYSPSV EGSSTELNLP ETANSVTLSD LQPGVQYNIT IYAVEENQES TPVFIQQETT
GVPRSDKVPP PRDLQFVEVT DVKITIMWTP PESPVTGYRV DVIPVNLPGE HGQRLPVSRN
TFAEVTGLSP GVTYHFKVFA VNQGRESKPL TAQQATKLDA PTNLQFINET DTTVIVTWTP
PRARIVGYRL TVGLTRGGQP KQYNVGPAAS QYPLRNLQPG SEYAVSLVAV KGNQQSPRVT
GVFTTLQPLG SIPHYNTEVT ETTIVITWTP APRIGFKLGV RPSQGGEAPR EVTSESGSIV
VSGLTPGVEY VYTISVLRDG QERDAPIVKK VVTPLSPPTN LHLEANPDTG VLTVSWERST
TPDITGYRIT TTPTNGQQGY SLEEVVHADQ SSCTFENLSP GLEYNVSVYT VKDDKESVPI
SDTIIPEVPQ LTDLSFVDIT DSSIGLRWTP LNSSTIIGYR ITVVAAGEGI PIFEDFVDSS
VGYYTVTGLE PGIDYDISVI TLINGGESAP TTLTQQTAVP PPTDLRFTNV GPDTMRVTWA
PPSSIELTNL LVRYSPVKNE EDVAELSISP SDNAVVLTNL LPGTEYLVSV SSVYEQHESI
PLRGRQKTAL DSPSGIDFSD ITANSFTVHW IAPRATITGY RIRHHPENMG GRPREDRVPP
SRNSITLTNL NPGTEYVVSI VALNSKEESL PLVGQQSTVS DVPRDLEVIA ATPTSLLISW
DAPAVTVRYY RITYGETGGS SPVQEFTVPG SKSTATISGL KPGVDYTITV YAVTGRGDSP
ASSKPVSINY RTEIDKPSQM QVTDVQDNSI SVRWLPSSSP VTGYRVTTAP KNGPGPSKTK
TVGPDQTEMT IEGLQPTVEY VVSVYAQNQN GESQPLVQTA VTNIDRPKGL AFTDVDVDSI
KIAWESPQGQ VSRYRVTYSS PEDGIHELFP APDGEEETAE LQGLRPGSEY TVSVVALHDD
MESQPLIGTQ STTIPAPTNL KFTQVTPTSL TAQWTAPNVQ LTGYRVRVTP KEKTGPMKEI
NLAPDSSSVV VSGLMVATKY EVSVYALKDT LTSRPAQGVV TTLENVSPPR RARVTDATET
TITISWRTKT ETITGFQVDA IPANGQTPIQ RTIRPDVRSY TITGLQPGTD YKIHLYTLND
NARSSPVVID ASTAIDAPSN LRFLATTPNS LLVSWQPPRA RITGYIIKYE KPGSPPREVV
PRPRPGVTEA TITGLEPGTE YTIQVIALKN NQKSEPLIGR KKTDELPQLV TLPHPNLHGP
EILDVPSTVQ KTPFITNPGY DTGNGIQLPG TSGQQPSLGQ QMIFEEHGFR RTTPPTTATP
VRHRPRPYPP NVNEEIQIGH VPRGDVDHHL YPHVVGLNPN ASTGQEALSQ TTISWTPFQE
SSEYIISCHP VGIDEEPLQF RVPGTSASAT LTGLTRGATY NIIVEAVKDQ QRQKVREEVV
TVGNSVDQGL SQPTDDSCFD PYTVSHYAIG EEWERLSDSG FKLSCQCLGF GSGHFRCDSS
KWCHDNGVNY KIGEKWDRQG ENGQMMSCTC LGNGKGEFKC DPHEATCYDD GKTYHVGEQW
QKEYLGAICS CTCFGGQRGW RCDNCRRPGA EPGNEGSTAH SYNQYSQRYH QRTNTNVNCP
IECFMPLDVQ ADREDSRE
