FCGBP_HUMAN
ID FCGBP_HUMAN Reviewed; 5405 AA.
AC Q9Y6R7; O95784;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=IgGFc-binding protein;
DE AltName: Full=Fcgamma-binding protein antigen;
DE Short=FcgammaBP;
DE Flags: Precursor;
GN Name=FCGBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-2814; SER-4465; HIS-4906 AND
RP VAL-5017, FUNCTION, INTERACTION WITH IGG, AND TISSUE SPECIFICITY.
RC TISSUE=Colon epithelium;
RX PubMed=9182547; DOI=10.1074/jbc.272.24.15232;
RA Harada N., Iijima S., Kobayashi K., Yoshida T., Brown W.R., Hibi T.,
RA Oshima A., Morikawa M.;
RT "Human IgGFc binding protein (FcgammaBP) in colonic epithelial cells
RT exhibits mucin-like structure.";
RL J. Biol. Chem. 272:15232-15241(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11600203; DOI=10.1016/s0165-2478(01)00288-7;
RA Kobayashi K., Yagasaki M., Harada N., Chichibu K., Hibi T., Yoshida T.,
RA Brown W.R., Morikawa M.;
RT "Detection of Fcgamma binding protein antigen in human sera and its
RT relation with autoimmune diseases.";
RL Immunol. Lett. 79:229-235(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12208673; DOI=10.1677/joe.0.1740517;
RA O'Donovan N., Fischer A., Abdo E.-M., Simon F., Peter H.J., Gerber H.,
RA Buergi U., Marti U.;
RT "Differential expression of IgG Fc binding protein (FcgammaBP) in human
RT normal thyroid tissue, thyroid adenomas and thyroid carcinomas.";
RL J. Endocrinol. 174:517-524(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3719.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-75; ASN-91; ASN-1743; ASN-2138
RP AND ASN-2518.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2518.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [8]
RP INTERACTION WITH MUC2.
RX PubMed=19432394; DOI=10.1021/pr9002504;
RA Johansson M.E.V., Thomsson K.A., Hansson G.C.;
RT "Proteomic analyses of the two mucus layers of the colon barrier reveal
RT that their main component, the Muc2 mucin, is strongly bound to the Fcgbp
RT protein.";
RL J. Proteome Res. 8:3549-3557(2009).
RN [9]
RP GLYCOSYLATION AT ASN-1317.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: May be involved in the maintenance of the mucosal structure
CC as a gel-like component of the mucosa. {ECO:0000269|PubMed:9182547}.
CC -!- SUBUNIT: Interacts with the Fc portion of IgG and with MUC2.
CC {ECO:0000269|PubMed:19432394, ECO:0000269|PubMed:9182547}.
CC -!- INTERACTION:
CC Q9Y6R7; Q07654: TFF3; NbExp=2; IntAct=EBI-2869882, EBI-10224676;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in placenta and colon epithelium.
CC Expressed in thyroid, and down-regulated in thyroid carcinomas. Present
CC in serum, with higher levels in patients with various autoimmune
CC diseases (at protein level). {ECO:0000269|PubMed:11600203,
CC ECO:0000269|PubMed:12208673, ECO:0000269|PubMed:9182547}.
CC -!- DOMAIN: The N-terminal IgGFc-binding region is primate-specific.
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DR EMBL; D84239; BAA19526.1; -; mRNA.
DR EMBL; AC006950; AAD15624.1; -; Genomic_DNA.
DR EMBL; AC007842; AAD39266.1; -; Genomic_DNA.
DR EMBL; AC011536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_003881.2; NM_003890.2.
DR SMR; Q9Y6R7; -.
DR BioGRID; 114381; 17.
DR IntAct; Q9Y6R7; 8.
DR MEROPS; I08.954; -.
DR GlyConnect; 1386; 21 N-Linked glycans (10 sites).
DR GlyGen; Q9Y6R7; 18 sites, 27 N-linked glycans (10 sites), 1 O-linked glycan (3 sites).
DR iPTMnet; Q9Y6R7; -.
DR PhosphoSitePlus; Q9Y6R7; -.
DR BioMuta; FCGBP; -.
DR DMDM; 224471888; -.
DR CPTAC; non-CPTAC-1133; -.
DR EPD; Q9Y6R7; -.
DR jPOST; Q9Y6R7; -.
DR MassIVE; Q9Y6R7; -.
DR MaxQB; Q9Y6R7; -.
DR PaxDb; Q9Y6R7; -.
DR PeptideAtlas; Q9Y6R7; -.
DR PRIDE; Q9Y6R7; -.
DR ProteomicsDB; 86780; -.
DR DNASU; 8857; -.
DR Ensembl; ENST00000628705.2; ENSP00000487490.3; ENSG00000281123.3.
DR Ensembl; ENST00000639918.2; ENSP00000491148.2; ENSG00000281123.3.
DR GeneID; 8857; -.
DR KEGG; hsa:8857; -.
DR CTD; 8857; -.
DR DisGeNET; 8857; -.
DR GeneCards; FCGBP; -.
DR HGNC; HGNC:13572; FCGBP.
DR MIM; 617553; gene.
DR neXtProt; NX_Q9Y6R7; -.
DR PharmGKB; PA28059; -.
DR InParanoid; Q9Y6R7; -.
DR OrthoDB; 22053at2759; -.
DR PhylomeDB; Q9Y6R7; -.
DR TreeFam; TF316399; -.
DR PathwayCommons; Q9Y6R7; -.
DR SignaLink; Q9Y6R7; -.
DR BioGRID-ORCS; 8857; 14 hits in 1009 CRISPR screens.
DR ChiTaRS; FCGBP; human.
DR GeneWiki; FCGBP; -.
DR GenomeRNAi; 8857; -.
DR Pharos; Q9Y6R7; Tbio.
DR PRO; PR:Q9Y6R7; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9Y6R7; protein.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR035234; IgGFc-bd_N.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR025615; TILa_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF08742; C8; 12.
DR Pfam; PF17517; IgGFc_binding; 1.
DR Pfam; PF01826; TIL; 12.
DR Pfam; PF12714; TILa; 8.
DR Pfam; PF00094; VWD; 13.
DR SMART; SM00832; C8; 12.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00274; FOLN; 9.
DR SMART; SM00214; VWC; 7.
DR SMART; SM00215; VWC_out; 11.
DR SMART; SM00216; VWD; 13.
DR SUPFAM; SSF57567; SSF57567; 12.
DR PROSITE; PS51233; VWFD; 13.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..5405
FT /note="IgGFc-binding protein"
FT /id="PRO_0000256698"
FT DOMAIN 470..650
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 745..799
FT /note="TIL 1"
FT DOMAIN 862..1041
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1136..1189
FT /note="TIL 2"
FT DOMAIN 1250..1429
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1532..1585
FT /note="TIL 3"
FT DOMAIN 1671..1854
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1950..2007
FT /note="TIL 4"
FT DOMAIN 2070..2253
FT /note="VWFD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2337..2390
FT /note="TIL 5"
FT DOMAIN 2451..2630
FT /note="VWFD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2733..2786
FT /note="TIL 6"
FT DOMAIN 2872..3055
FT /note="VWFD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 3151..3208
FT /note="TIL 7"
FT DOMAIN 3271..3454
FT /note="VWFD 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 3538..3591
FT /note="TIL 8"
FT DOMAIN 3652..3831
FT /note="VWFD 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 3934..3987
FT /note="TIL 9"
FT DOMAIN 4073..4256
FT /note="VWFD 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 4352..4409
FT /note="TIL 10"
FT DOMAIN 4472..4655
FT /note="VWFD 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 4739..4792
FT /note="TIL 11"
FT DOMAIN 4854..5025
FT /note="VWFD 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 5121..5174
FT /note="TIL 12"
FT DOMAIN 5233..5404
FT /note="VWFD 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 24..450
FT /note="IgGFc-binding"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 1317
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 1743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 2138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 2518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:16740002"
FT CARBOHYD 3719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671"
FT CARBOHYD 4145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 472..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 494..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 864..1003
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 886..1040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1252..1390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1274..1428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1673..1815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1695..1853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1704..1812
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2072..2211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2094..2252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2453..2591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2475..2629
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2874..3016
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2896..3054
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2905..3013
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 3273..3412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 3295..3453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 3654..3792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 3676..3830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4075..4217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4097..4255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4106..4214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4474..4613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4496..4654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4856..4986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4878..5024
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 5235..5372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT VARIANT 732
FT /note="V -> A (in dbSNP:rs34181317)"
FT /id="VAR_054490"
FT VARIANT 770
FT /note="N -> S (in dbSNP:rs34939346)"
FT /id="VAR_054491"
FT VARIANT 929
FT /note="G -> R (in dbSNP:rs35338934)"
FT /id="VAR_054492"
FT VARIANT 971
FT /note="V -> M (in dbSNP:rs35922811)"
FT /id="VAR_054493"
FT VARIANT 1019
FT /note="G -> R (in dbSNP:rs34254649)"
FT /id="VAR_054494"
FT VARIANT 1340
FT /note="V -> L (in dbSNP:rs11083543)"
FT /id="VAR_028903"
FT VARIANT 1436
FT /note="P -> L (in dbSNP:rs36106401)"
FT /id="VAR_054495"
FT VARIANT 1445
FT /note="H -> D (in dbSNP:rs2909229)"
FT /id="VAR_054496"
FT VARIANT 1524
FT /note="T -> N (in dbSNP:rs34938990)"
FT /id="VAR_054497"
FT VARIANT 1616
FT /note="G -> V (in dbSNP:rs7248839)"
FT /id="VAR_028904"
FT VARIANT 1617
FT /note="M -> V (in dbSNP:rs7249743)"
FT /id="VAR_028905"
FT VARIANT 2089
FT /note="N -> D (in dbSNP:rs885723)"
FT /id="VAR_028906"
FT VARIANT 2646
FT /note="E -> D (in dbSNP:rs140171218)"
FT /id="VAR_028907"
FT VARIANT 2647
FT /note="E -> K (in dbSNP:rs1176978283)"
FT /id="VAR_028908"
FT VARIANT 2793
FT /note="A -> V (in dbSNP:rs2542316)"
FT /id="VAR_028909"
FT VARIANT 2814
FT /note="V -> A (in dbSNP:rs3746009)"
FT /evidence="ECO:0000269|PubMed:9182547"
FT /id="VAR_028910"
FT VARIANT 3264
FT /note="G -> S (in dbSNP:rs1290971390)"
FT /id="VAR_028911"
FT VARIANT 3920
FT /note="H -> Q (in dbSNP:rs2542318)"
FT /id="VAR_028912"
FT VARIANT 4015
FT /note="V -> A (in dbSNP:rs3746009)"
FT /id="VAR_028913"
FT VARIANT 4095
FT /note="G -> D (in dbSNP:rs1975181)"
FT /id="VAR_028914"
FT VARIANT 4465
FT /note="G -> S (in dbSNP:rs6508919)"
FT /evidence="ECO:0000269|PubMed:9182547"
FT /id="VAR_028915"
FT VARIANT 4906
FT /note="D -> H (in dbSNP:rs3746013)"
FT /evidence="ECO:0000269|PubMed:9182547"
FT /id="VAR_028916"
FT VARIANT 5017
FT /note="A -> V (in dbSNP:rs741143)"
FT /evidence="ECO:0000269|PubMed:9182547"
FT /id="VAR_054498"
FT CONFLICT 1961
FT /note="S -> P (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 2719
FT /note="Q -> H (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 2842
FT /note="N -> T (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 2976
FT /note="T -> A (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 3117
FT /note="R -> H (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 3668
FT /note="H -> R (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 3841
FT /note="A -> E (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 3847..3848
FT /note="DK -> EE (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 4043
FT /note="T -> N (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 4284
FT /note="S -> A (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 4318
FT /note="R -> H (in Ref. 1; BAA19526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5405 AA; 572017 MW; 6E502F782261355F CRC64;
MGALWSWWIL WAGATLLWGL TQEASVDLKN TGREEFLTAF LQNYQLAYSK AYPRLLISSL
SESPASVSIL SQADNTSKKV TVRPGESVMV NISAKAEMIG SKIFQHAVVI HSDYAISVQA
LNAKPDTAEL TLLRPIQALG TEYFVLTPPG TSARNVKEFA VVAGAAGASV SVTLKGSVTF
NGKFYPAGDV LRVTLQPYNV AQLQSSVDLS GSKVTASSPV AVLSGHSCAQ KHTTCNHVVE
QLLPTSAWGT HYVVPTLASQ SRYDLAFVVA SQATKLTYNH GGITGSRGLQ AGDVVEFEVR
PSWPLYLSAN VGIQVLLFGT GAIRNEVTYD PYLVLIPDVA AYCPAYVVKS VPGCEGVALV
VAQTKAISGL TIDGHAVGAK LTWEAVPGSE FSYAEVELGT ADMIHTAEAT TNLGLLTFGL
AKAIGYATAA DCGRTVLSPV EPSCEGMQCA AGQRCQVVGG KAGCVAESTA VCRAQGDPHY
TTFDGRRYDM MGTCSYTMVE LCSEDDTLPA FSVEAKNEHR GSRRVSYVGL VTVRAYSHSV
SLTRGEVGFV LVDNQRSRLP VSLSEGRLRV YQSGPRAVVE LVFGLVVTYD WDCQLALSLP
ARFQDQVCGL CGNYNGDPAD DFLTPDGALA PDAVEFASSW KLDDGDYLCE DGCQNNCPAC
TPGQAQHYEG DRLCGMLTKL DGPFAVCHDT LDPRPFLEQC VYDLCVVGGE RLSLCRGLSA
YAQACLELGI SVGDWRSPAN CPLSCPANSR YELCGPACPT SCNGAAAPSN CSGRPCVEGC
VCLPGFVASG GACVPASSCG CTFQGLQLAP GQEVWADELC QRRCTCNGAT HQVTCRDKQS
CPAGERCSVQ NGLLGCYPDR FGTCQGSGDP HYVSFDGRRF DFMGTCTYLL VGSCGQNAAL
PAFRVLVENE HRGSQTVSYT RAVRVEARGV KVAVRREYPG QVLVDDVLQY LPFQAADGQV
QVFRQGRDAV VRTDFGLTVT YDWNARVTAK VPSSYAEALC GLCGNFNGDP ADDLALRGGG
QAANALAFGN SWQEETRPGC GATEPGDCPK LDSLVAQQLQ SKNECGILAD PKGPFRECHS
KLDPQGAVRD CVYDRCLLPG QSGPLCDALA TYAAACQAAG ATVHPWRSEE LCPLSCPPHS
HYEACSYGCP LSCGDLPVPG GCGSECHEGC VCDEGFALSG ESCLPLASCG CVHQGTYHPP
GQTFYPGPGC DSLCHCQEGG LVSCESSSCG PHEACQPSGG SLGCVAVGSS TCQASGDPHY
TTFDGRRFDF MGTCVYVLAQ TCGTRPGLHR FAVLQENVAW GNGRVSVTRV ITVQVANFTL
RLEQRQWKVT VNGVDMKLPV VLANGQIRAS QHGSDVVIET DFGLRVAYDL VYYVRVTVPG
NYYQQMCGLC GNYNGDPKDD FQKPNGSQAG NANEFGNSWE EVVPDSPCLP PTPCPPGSED
CIPSHKCPPE LEKKYQKEEF CGLLSSPTGP LSSCHKLVDP QGPLKDCIFD LCLGGGNLSI
LCSNIHAYVS ACQAAGGHVE PWRTETFCPM ECPPNSHYEL CADTCSLGCS ALSAPPQCQD
GCAEGCQCDS GFLYNGQACV PIQQCGCYHN GVYYEPEQTV LIDNCRQQCT CHAGKGMVCQ
EHSCKPGQVC QPSGGILSCV TKDPCHGVTC RPQETCKEQG GQGVCLPNYE ATCWLWGDPH
YHSFDGRKFD FQGTCNYVLA TTGCPGVSTQ GLTPFTVTTK NQNRGNPAVS YVRVVTVAAL
GTNISIHKDE IGKVRVNGVL TALPVSVADG RISVTQGASK ALLVADFGLQ VSYDWNWRVD
VTLPSSYHGA VCGLCGNMDR NPNNDQVFPN GTLAPSIPIW GGSWRAPGWD PLCWDECRGS
CPTCPEDRLE QYEGPGFCGP LAPGTGGPFT TCHAHVPPES FFKGCVLDVC MGGGDRDILC
KALASYVAAC QAAGVVIEDW RAQVGCEITC PENSHYEVCG SPCPASCPSP APLTTPAVCE
GPCVEGCQCD AGFVLSADRC VPLNNGCGCW ANGTYHEAGS EFWADGTCSQ WCRCGPGGGS
LVCTPASCGL GEVCGLLPSG QHGCQPVSTA ECQAWGDPHY VTLDGHRFNF QGTCEYLLSA
PCHGPPLGAE NFTVTVANEH RGSQAVSYTR SVTLQIYNHS LTLSARWPRK LQVDGVFVTL
PFQLDSLLHA HLSGADVVVT TTSGLSLAFD GDSFVRLRVP AAYAGSLCGL CGNYNQDPAD
DLKAVGGKPA GWQVGGAQGC GECVSKPCPS PCTPEQQESF GGPDACGVIS ATDGPLAPCH
GLVPPAQYFQ GCLLDACQVQ GHPGGLCPAV ATYVAACQAA GAQLREWRRP DFCPFQCPAH
SHYELCGDSC PGSCPSLSAP EGCESACREG CVCDAGFVLS GDTCVPVGQC GCLHDDRYYP
LGQTFYPGPG CDSLCRCREG GEVSCEPSSC GPHETCRPSG GSLGCVAVGS TTCQASGDPH
YTTFDGRRFD FMGTCVYVLA QTCGTRPGLH RFAVLQENVA WGNGRVSVTR VITVQVANFT
LRLEQRQWKV TVNGVDMKLP VVLANGQIRA SQHGSDVVIE TDFGLRVAYD LVYYVRVTVP
GNYYQLMCGL CGNYNGDPKD DFQKPNGSQA GNANEFGNSW EEVVPDSPCL PPPTCPPGSE
GCIPSEECPP ELEKKYQKEE FCGLLSSPTG PLSSCHKLVD PQGPLKDCIF DLCLGGGNLS
ILCSNIHAYV SACQAAGGQV EPWRNETFCP MECPQNSHYE LCADTCSLGC SALSAPLQCP
DGCAEGCQCD SGFLYNGQAC VPIQQCGCYH NGAYYEPEQT VLIDNCRQQC TCHVGKVVVC
QEHSCKPGQV CQPSGGILSC VNKDPCHGVT CRPQETCKEQ GGQGVCLPNY EATCWLWGDP
HYHSFDGRKF DFQGTCNYVL ATTGCPGVST QGLTPFTVTT KNQNRGNPAV SYVRVVTVAA
LGTNISIHKD EIGKVRVNGV LTALPVSVAD GRISVTQGAS KALLVADFGL QVSYDWNWRV
DVTLPSSYHG AVCGLCGNMD RNPNNDQVFP NGTLAPSIPI WGGSWRAPGW DPLCWDECRG
SCPTCPEDRL EQYEGPGFCG PLAPGTGGPF TTCHAHVPPE SFFKGCVLDV CMGGGDRDIL
CKALASYVAA CQAAGVVIED WRAQVGCEIT CPENSHYEVC GPPCPASCPS PAPLTTPAVC
EGPCVEGCQC DAGFVLSADR CVPLNNGCGC WANGTYHEAG SEFWADGTCS QWCRCGPGGG
SLVCTPASCG LGEVCGLLPS GQHGCQPVST AECQAWGDPH YVTLDGHRFD FQGTCEYLLS
APCHGPPLGA ENFTVTVANE HRGSQAVSYT RSVTLQIYNH SLTLSARWPR KLQVDGVFVT
LPFQLDSLLH AHLSGADVVV TTTSGLSLAF DGDSFVRLRV PAAYAGSLCG LCGNYNQDPA
DDLKAVGGKP AGWQVGGAQG CGECVSKPCP SPCTPEQQES FGGPDACGVI SATDGPLAPC
HGLVPPAQYF QGCLLDACQV QGHPGGLCPA VATYVAACQA AGAQLREWRR PDFCPFQCPA
HSHYELCGDS CPGSCPSLSA PEGCESACRE GCVCDAGFVL SGDTCVPVGQ CGCLHDDRYY
PLGQTFYPGP GCDSLCRCRE GGEVSCEPSS CGPHETCRPS GGSLGCVAVG STTCQASGDP
HYTTFDGHRF DFMGTCVYVL AQTCGTRPGL HRFAVLQENV AWGNGRVSVT RVITVQVANF
TLRLEQRQWK VTVNGVDMKL PVVLANGQIR ASQHGSDVVI ETDFGLRVAY DLVYYVRVTV
PGNYYQLMCG LCGNYNGDPK DDFQKPNGSQ AGNANEFGNS WEEVVPDSPC LPPPTCPPGS
AGCIPSDKCP PELEKKYQKE EFCGLLSSPT GPLSSCHKLV DPQGPLKDCI FDLCLGGGNL
SILCSNIHAY VSACQAAGGH VEPWRNETFC PMECPQNSHY ELCADTCSLG CSALSAPLQC
PDGCAEGCQC DSGFLYNGQA CVPIQQCGCY HNGVYYEPEQ TVLIDNCRQQ CTCHVGKVVV
CQEHSCKPGQ VCQPSGGILS CVTKDPCHGV TCRPQETCKE QGGQGVCLPN YEATCWLWGD
PHYHSFDGRK FDFQGTCNYV LATTGCPGVS TQGLTPFTVT TKNQNRGNPA VSYVRVVTVA
ALGTNISIHK DEIGKVRVNG VLTALPVSVA DGRISVAQGA SKALLVADFG LQVSYDWNWR
VDVTLPSSYH GAVCGLCGNM DRNPNNDQVF PNGTLAPSIP IWGGSWRAPG WDPLCWDECR
GSCPTCPEDR LEQYEGPGFC GPLSSGTGGP FTTCHAHVPP ESFFKGCVLD VCMGGGDRDI
LCKALASYVA ACQAAGVVIE DWRAQVGCEI TCPENSHYEV CGPPCPASCP SPAPLTTPAV
CEGPCVEGCQ CDAGFVLSAD RCVPLNNGCG CWANGTYHEA GSEFWADGTC SQWCRCGPGG
GSLVCTPASC GLGEVCGLLP SGQHGCQPVS TAECQAWGDP HYVTLDGHRF DFQGTCEYLL
SAPCHGPPLG AENFTVTVAN EHRGSQAVSY TRSVTLQIYN HSLTLSARWP RKLQVDGVFV
ALPFQLDSLL HAHLSGADVV VTTTSGLSLA FDGDSFVRLR VPAAYAASLC GLCGNYNQDP
ADDLKAVGGK PAGWQVGGAQ GCGECVSKPC PSPCTPEQQE SFGGPDACGV ISATDGPLAP
CHGLVPPAQY FQGCLLDACQ VQGHPGGLCP AVATYVAACQ AAGAQLGEWR RPDFCPLQCP
AHSHYELCGD SCPVSCPSLS APEGCESACR EGCVCDAGFV LSGDTCVPVG QCGCLHDGRY
YPLGEVFYPG PECERRCECG PGGHVTCQEG AACGPHEECR LEDGVQACHA TGCGRCLANG
GIHYITLDGR VYDLHGSCSY VLAQVCHPKP GDEDFSIVLE KNAAGDLQRL LVTVAGQVVS
LAQGQQVTVD GEAVALPVAV GRVRVTAEGR NMVLQTTKGL RLLFDGDAHL LMSIPSPFRG
RLCGLCGNFN GNWSDDFVLP NGSAASSVET FGAAWRAPGS SKGCGEGCGP QGCPVCLAEE
TAPYESNEAC GQLRNPQGPF ATCQAVLSPS EYFRQCVYDL CAQKGDKAFL CRSLAAYTAA
CQAAGVAVKP WRTDSFCPLH CPAHSHYSIC TRTCQGSCAA LSGLTGCTTR CFEGCECDDR
FLLSQGVCIP VQDCGCTHNG RYLPVNSSLL TSDCSERCSC SSSSGLTCQA AGCPPGRVCE
VKAEARNCWA TRGLCVLSVG ANLTTFDGAR GATTSPGVYE LSSRCPGLQN TIPWYRVVAE
VQICHGKTEA VGQVHIFFQD GMVTLTPNKG VWVNGLRVDL PAEKLASVSV SRTPDGSLLV
RQKAGVQVWL GANGKVAVIV SNDHAGKLCG ACGNFDGDQT NDWHDSQEKP AMEKWRAQDF
SPCYG
