Full text data of FCGBP
FCGBP
[Confidence: low (only semi-automatic identification from reviews)]
IgGFc-binding protein (Fcgamma-binding protein antigen; FcgammaBP; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
IgGFc-binding protein (Fcgamma-binding protein antigen; FcgammaBP; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y6R7
ID FCGBP_HUMAN Reviewed; 5405 AA.
AC Q9Y6R7; O95784;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 3.
DT 22-JAN-2014, entry version 96.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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.,
RA Yoshida T., 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
RT human normal thyroid tissue, thyroid adenomas and thyroid
RT carcinomas.";
RL J. Endocrinol. 174:517-524(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3719, AND MASS
RP SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., 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;
RP ASN-2138 AND ASN-2518, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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, AND MASS
RP SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein 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
RT reveal that their main component, the Muc2 mucin, is strongly bound to
RT the Fcgbp 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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: May be involved in the maintenance of the mucosal
CC structure as a gel-like component of the mucosa.
CC -!- SUBUNIT: Interacts with the Fc portion of IgG and with MUC2.
CC -!- SUBCELLULAR LOCATION: Secreted (Probable).
CC -!- TISSUE SPECIFICITY: Mainly expressed in placenta and colon
CC epithelium. Expressed in thyroid, and down-regulated in thyroid
CC carcinomas. Present in serum, with higher levels in patients with
CC various autoimmune diseases (at protein level).
CC -!- DOMAIN: The N-terminal IgGFc-binding region is primate-specific.
CC -!- SIMILARITY: Contains 12 TIL (trypsin inhibitory-like) domains.
CC -!- SIMILARITY: Contains 13 VWFD domains.
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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 RefSeq; XP_005259422.1; XM_005259365.1.
DR UniGene; Hs.111732; -.
DR ProteinModelPortal; Q9Y6R7; -.
DR IntAct; Q9Y6R7; 2.
DR PhosphoSite; Q9Y6R7; -.
DR DMDM; 224471888; -.
DR PaxDb; Q9Y6R7; -.
DR PRIDE; Q9Y6R7; -.
DR Ensembl; ENST00000221347; ENSP00000221347; ENSG00000090920.
DR GeneID; 8857; -.
DR KEGG; hsa:8857; -.
DR UCSC; uc002omp.4; human.
DR CTD; 8857; -.
DR GeneCards; GC19M040353; -.
DR H-InvDB; HIX0040147; -.
DR HGNC; HGNC:13572; FCGBP.
DR HPA; HPA003517; -.
DR HPA; HPA003564; -.
DR neXtProt; NX_Q9Y6R7; -.
DR PharmGKB; PA28059; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000112559; -.
DR InParanoid; Q9Y6R7; -.
DR OMA; SSCHKLV; -.
DR OrthoDB; EOG7SJD3N; -.
DR PhylomeDB; Q9Y6R7; -.
DR GeneWiki; FCGBP; -.
DR GenomeRNAi; 8857; -.
DR NextBio; 33257; -.
DR PRO; PR:Q9Y6R7; -.
DR Bgee; Q9Y6R7; -.
DR CleanEx; HS_FCGBP; -.
DR Genevestigator; Q9Y6R7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR025615; TILa_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_C.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF08742; C8; 12.
DR Pfam; PF01826; TIL; 12.
DR Pfam; PF12714; TILa; 11.
DR Pfam; PF00094; VWD; 13.
DR SMART; SM00832; C8; 12.
DR SMART; SM00274; FOLN; 9.
DR SMART; SM00214; VWC; 4.
DR SMART; SM00216; VWD; 13.
DR SUPFAM; SSF57567; SSF57567; 12.
DR PROSITE; PS51233; VWFD; 13.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 5405 IgGFc-binding protein.
FT /FTId=PRO_0000256698.
FT DOMAIN 471 690 VWFD 1.
FT DOMAIN 745 799 TIL 1.
FT DOMAIN 863 1081 VWFD 2.
FT DOMAIN 1136 1189 TIL 2.
FT DOMAIN 1251 1477 VWFD 3.
FT DOMAIN 1532 1585 TIL 3.
FT DOMAIN 1672 1895 VWFD 4.
FT DOMAIN 1950 2007 TIL 4.
FT DOMAIN 2071 2282 VWFD 5.
FT DOMAIN 2337 2390 TIL 5.
FT DOMAIN 2452 2678 VWFD 6.
FT DOMAIN 2733 2786 TIL 6.
FT DOMAIN 2873 3096 VWFD 7.
FT DOMAIN 3151 3208 TIL 7.
FT DOMAIN 3272 3483 VWFD 8.
FT DOMAIN 3538 3591 TIL 8.
FT DOMAIN 3653 3879 VWFD 9.
FT DOMAIN 3934 3987 TIL 9.
FT DOMAIN 4074 4297 VWFD 10.
FT DOMAIN 4352 4409 TIL 10.
FT DOMAIN 4473 4684 VWFD 11.
FT DOMAIN 4739 4792 TIL 11.
FT DOMAIN 4855 5066 VWFD 12.
FT DOMAIN 5121 5174 TIL 12.
FT DOMAIN 5234 5405 VWFD 13.
FT REGION 24 450 IgGFc-binding.
FT COMPBIAS 741 847 Cys-rich.
FT COMPBIAS 1132 1235 Cys-rich.
FT COMPBIAS 1528 1656 Cys-rich.
FT COMPBIAS 2333 2436 Cys-rich.
FT COMPBIAS 2729 2857 Cys-rich.
FT COMPBIAS 3534 3637 Cys-rich.
FT COMPBIAS 3930 4058 Cys-rich.
FT COMPBIAS 5117 5219 Cys-rich.
FT CARBOHYD 75 75 N-linked (GlcNAc...).
FT CARBOHYD 91 91 N-linked (GlcNAc...).
FT CARBOHYD 1317 1317 N-linked (GlcNAc...) (complex).
FT CARBOHYD 1743 1743 N-linked (GlcNAc...).
FT CARBOHYD 2138 2138 N-linked (GlcNAc...).
FT CARBOHYD 2518 2518 N-linked (GlcNAc...).
FT CARBOHYD 3719 3719 N-linked (GlcNAc...).
FT CARBOHYD 4145 4145 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 4540 4540 N-linked (GlcNAc...) (Potential).
FT DISULFID 494 502 By similarity.
FT DISULFID 886 894 By similarity.
FT DISULFID 1274 1282 By similarity.
FT DISULFID 1695 1704 By similarity.
FT DISULFID 2094 2102 By similarity.
FT DISULFID 2475 2483 By similarity.
FT DISULFID 2896 2905 By similarity.
FT DISULFID 3295 3303 By similarity.
FT DISULFID 3676 3684 By similarity.
FT DISULFID 4097 4106 By similarity.
FT DISULFID 4496 4504 By similarity.
FT DISULFID 4878 4886 By similarity.
FT VARIANT 732 732 V -> A (in dbSNP:rs34181317).
FT /FTId=VAR_054490.
FT VARIANT 770 770 N -> S (in dbSNP:rs34939346).
FT /FTId=VAR_054491.
FT VARIANT 929 929 G -> R (in dbSNP:rs35338934).
FT /FTId=VAR_054492.
FT VARIANT 971 971 V -> M (in dbSNP:rs35922811).
FT /FTId=VAR_054493.
FT VARIANT 1019 1019 G -> R (in dbSNP:rs34254649).
FT /FTId=VAR_054494.
FT VARIANT 1340 1340 V -> L (in dbSNP:rs11083543).
FT /FTId=VAR_028903.
FT VARIANT 1436 1436 P -> L (in dbSNP:rs36106401).
FT /FTId=VAR_054495.
FT VARIANT 1445 1445 H -> D (in dbSNP:rs2909229).
FT /FTId=VAR_054496.
FT VARIANT 1524 1524 T -> N (in dbSNP:rs34938990).
FT /FTId=VAR_054497.
FT VARIANT 1616 1616 G -> V (in dbSNP:rs7248839).
FT /FTId=VAR_028904.
FT VARIANT 1617 1617 M -> V (in dbSNP:rs7249743).
FT /FTId=VAR_028905.
FT VARIANT 2089 2089 N -> D (in dbSNP:rs885723).
FT /FTId=VAR_028906.
FT VARIANT 2646 2646 E -> D (in dbSNP:rs2542320).
FT /FTId=VAR_028907.
FT VARIANT 2647 2647 E -> K (in dbSNP:rs2542319).
FT /FTId=VAR_028908.
FT VARIANT 2793 2793 A -> V (in dbSNP:rs2542316).
FT /FTId=VAR_028909.
FT VARIANT 2814 2814 V -> A (in dbSNP:rs3746009).
FT /FTId=VAR_028910.
FT VARIANT 3264 3264 G -> S (in dbSNP:rs6508919).
FT /FTId=VAR_028911.
FT VARIANT 3920 3920 H -> Q (in dbSNP:rs2542318).
FT /FTId=VAR_028912.
FT VARIANT 4015 4015 V -> A (in dbSNP:rs3746009).
FT /FTId=VAR_028913.
FT VARIANT 4095 4095 G -> D (in dbSNP:rs1975181).
FT /FTId=VAR_028914.
FT VARIANT 4465 4465 G -> S (in dbSNP:rs6508919).
FT /FTId=VAR_028915.
FT VARIANT 4906 4906 D -> H (in dbSNP:rs3746013).
FT /FTId=VAR_028916.
FT VARIANT 5017 5017 A -> V (in dbSNP:rs741143).
FT /FTId=VAR_054498.
FT CONFLICT 1961 1961 S -> P (in Ref. 1; BAA19526).
FT CONFLICT 2719 2719 Q -> H (in Ref. 1; BAA19526).
FT CONFLICT 2842 2842 N -> T (in Ref. 1; BAA19526).
FT CONFLICT 2976 2976 T -> A (in Ref. 1; BAA19526).
FT CONFLICT 3117 3117 R -> H (in Ref. 1; BAA19526).
FT CONFLICT 3668 3668 H -> R (in Ref. 1; BAA19526).
FT CONFLICT 3841 3841 A -> E (in Ref. 1; BAA19526).
FT CONFLICT 3847 3848 DK -> EE (in Ref. 1; BAA19526).
FT CONFLICT 4043 4043 T -> N (in Ref. 1; BAA19526).
FT CONFLICT 4284 4284 S -> A (in Ref. 1; BAA19526).
FT CONFLICT 4318 4318 R -> H (in Ref. 1; BAA19526).
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
//
ID FCGBP_HUMAN Reviewed; 5405 AA.
AC Q9Y6R7; O95784;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 3.
DT 22-JAN-2014, entry version 96.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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.,
RA Yoshida T., 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
RT human normal thyroid tissue, thyroid adenomas and thyroid
RT carcinomas.";
RL J. Endocrinol. 174:517-524(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3719, AND MASS
RP SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., 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;
RP ASN-2138 AND ASN-2518, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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, AND MASS
RP SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein 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
RT reveal that their main component, the Muc2 mucin, is strongly bound to
RT the Fcgbp 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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: May be involved in the maintenance of the mucosal
CC structure as a gel-like component of the mucosa.
CC -!- SUBUNIT: Interacts with the Fc portion of IgG and with MUC2.
CC -!- SUBCELLULAR LOCATION: Secreted (Probable).
CC -!- TISSUE SPECIFICITY: Mainly expressed in placenta and colon
CC epithelium. Expressed in thyroid, and down-regulated in thyroid
CC carcinomas. Present in serum, with higher levels in patients with
CC various autoimmune diseases (at protein level).
CC -!- DOMAIN: The N-terminal IgGFc-binding region is primate-specific.
CC -!- SIMILARITY: Contains 12 TIL (trypsin inhibitory-like) domains.
CC -!- SIMILARITY: Contains 13 VWFD domains.
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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 RefSeq; XP_005259422.1; XM_005259365.1.
DR UniGene; Hs.111732; -.
DR ProteinModelPortal; Q9Y6R7; -.
DR IntAct; Q9Y6R7; 2.
DR PhosphoSite; Q9Y6R7; -.
DR DMDM; 224471888; -.
DR PaxDb; Q9Y6R7; -.
DR PRIDE; Q9Y6R7; -.
DR Ensembl; ENST00000221347; ENSP00000221347; ENSG00000090920.
DR GeneID; 8857; -.
DR KEGG; hsa:8857; -.
DR UCSC; uc002omp.4; human.
DR CTD; 8857; -.
DR GeneCards; GC19M040353; -.
DR H-InvDB; HIX0040147; -.
DR HGNC; HGNC:13572; FCGBP.
DR HPA; HPA003517; -.
DR HPA; HPA003564; -.
DR neXtProt; NX_Q9Y6R7; -.
DR PharmGKB; PA28059; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000112559; -.
DR InParanoid; Q9Y6R7; -.
DR OMA; SSCHKLV; -.
DR OrthoDB; EOG7SJD3N; -.
DR PhylomeDB; Q9Y6R7; -.
DR GeneWiki; FCGBP; -.
DR GenomeRNAi; 8857; -.
DR NextBio; 33257; -.
DR PRO; PR:Q9Y6R7; -.
DR Bgee; Q9Y6R7; -.
DR CleanEx; HS_FCGBP; -.
DR Genevestigator; Q9Y6R7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR025615; TILa_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_C.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF08742; C8; 12.
DR Pfam; PF01826; TIL; 12.
DR Pfam; PF12714; TILa; 11.
DR Pfam; PF00094; VWD; 13.
DR SMART; SM00832; C8; 12.
DR SMART; SM00274; FOLN; 9.
DR SMART; SM00214; VWC; 4.
DR SMART; SM00216; VWD; 13.
DR SUPFAM; SSF57567; SSF57567; 12.
DR PROSITE; PS51233; VWFD; 13.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 5405 IgGFc-binding protein.
FT /FTId=PRO_0000256698.
FT DOMAIN 471 690 VWFD 1.
FT DOMAIN 745 799 TIL 1.
FT DOMAIN 863 1081 VWFD 2.
FT DOMAIN 1136 1189 TIL 2.
FT DOMAIN 1251 1477 VWFD 3.
FT DOMAIN 1532 1585 TIL 3.
FT DOMAIN 1672 1895 VWFD 4.
FT DOMAIN 1950 2007 TIL 4.
FT DOMAIN 2071 2282 VWFD 5.
FT DOMAIN 2337 2390 TIL 5.
FT DOMAIN 2452 2678 VWFD 6.
FT DOMAIN 2733 2786 TIL 6.
FT DOMAIN 2873 3096 VWFD 7.
FT DOMAIN 3151 3208 TIL 7.
FT DOMAIN 3272 3483 VWFD 8.
FT DOMAIN 3538 3591 TIL 8.
FT DOMAIN 3653 3879 VWFD 9.
FT DOMAIN 3934 3987 TIL 9.
FT DOMAIN 4074 4297 VWFD 10.
FT DOMAIN 4352 4409 TIL 10.
FT DOMAIN 4473 4684 VWFD 11.
FT DOMAIN 4739 4792 TIL 11.
FT DOMAIN 4855 5066 VWFD 12.
FT DOMAIN 5121 5174 TIL 12.
FT DOMAIN 5234 5405 VWFD 13.
FT REGION 24 450 IgGFc-binding.
FT COMPBIAS 741 847 Cys-rich.
FT COMPBIAS 1132 1235 Cys-rich.
FT COMPBIAS 1528 1656 Cys-rich.
FT COMPBIAS 2333 2436 Cys-rich.
FT COMPBIAS 2729 2857 Cys-rich.
FT COMPBIAS 3534 3637 Cys-rich.
FT COMPBIAS 3930 4058 Cys-rich.
FT COMPBIAS 5117 5219 Cys-rich.
FT CARBOHYD 75 75 N-linked (GlcNAc...).
FT CARBOHYD 91 91 N-linked (GlcNAc...).
FT CARBOHYD 1317 1317 N-linked (GlcNAc...) (complex).
FT CARBOHYD 1743 1743 N-linked (GlcNAc...).
FT CARBOHYD 2138 2138 N-linked (GlcNAc...).
FT CARBOHYD 2518 2518 N-linked (GlcNAc...).
FT CARBOHYD 3719 3719 N-linked (GlcNAc...).
FT CARBOHYD 4145 4145 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 4540 4540 N-linked (GlcNAc...) (Potential).
FT DISULFID 494 502 By similarity.
FT DISULFID 886 894 By similarity.
FT DISULFID 1274 1282 By similarity.
FT DISULFID 1695 1704 By similarity.
FT DISULFID 2094 2102 By similarity.
FT DISULFID 2475 2483 By similarity.
FT DISULFID 2896 2905 By similarity.
FT DISULFID 3295 3303 By similarity.
FT DISULFID 3676 3684 By similarity.
FT DISULFID 4097 4106 By similarity.
FT DISULFID 4496 4504 By similarity.
FT DISULFID 4878 4886 By similarity.
FT VARIANT 732 732 V -> A (in dbSNP:rs34181317).
FT /FTId=VAR_054490.
FT VARIANT 770 770 N -> S (in dbSNP:rs34939346).
FT /FTId=VAR_054491.
FT VARIANT 929 929 G -> R (in dbSNP:rs35338934).
FT /FTId=VAR_054492.
FT VARIANT 971 971 V -> M (in dbSNP:rs35922811).
FT /FTId=VAR_054493.
FT VARIANT 1019 1019 G -> R (in dbSNP:rs34254649).
FT /FTId=VAR_054494.
FT VARIANT 1340 1340 V -> L (in dbSNP:rs11083543).
FT /FTId=VAR_028903.
FT VARIANT 1436 1436 P -> L (in dbSNP:rs36106401).
FT /FTId=VAR_054495.
FT VARIANT 1445 1445 H -> D (in dbSNP:rs2909229).
FT /FTId=VAR_054496.
FT VARIANT 1524 1524 T -> N (in dbSNP:rs34938990).
FT /FTId=VAR_054497.
FT VARIANT 1616 1616 G -> V (in dbSNP:rs7248839).
FT /FTId=VAR_028904.
FT VARIANT 1617 1617 M -> V (in dbSNP:rs7249743).
FT /FTId=VAR_028905.
FT VARIANT 2089 2089 N -> D (in dbSNP:rs885723).
FT /FTId=VAR_028906.
FT VARIANT 2646 2646 E -> D (in dbSNP:rs2542320).
FT /FTId=VAR_028907.
FT VARIANT 2647 2647 E -> K (in dbSNP:rs2542319).
FT /FTId=VAR_028908.
FT VARIANT 2793 2793 A -> V (in dbSNP:rs2542316).
FT /FTId=VAR_028909.
FT VARIANT 2814 2814 V -> A (in dbSNP:rs3746009).
FT /FTId=VAR_028910.
FT VARIANT 3264 3264 G -> S (in dbSNP:rs6508919).
FT /FTId=VAR_028911.
FT VARIANT 3920 3920 H -> Q (in dbSNP:rs2542318).
FT /FTId=VAR_028912.
FT VARIANT 4015 4015 V -> A (in dbSNP:rs3746009).
FT /FTId=VAR_028913.
FT VARIANT 4095 4095 G -> D (in dbSNP:rs1975181).
FT /FTId=VAR_028914.
FT VARIANT 4465 4465 G -> S (in dbSNP:rs6508919).
FT /FTId=VAR_028915.
FT VARIANT 4906 4906 D -> H (in dbSNP:rs3746013).
FT /FTId=VAR_028916.
FT VARIANT 5017 5017 A -> V (in dbSNP:rs741143).
FT /FTId=VAR_054498.
FT CONFLICT 1961 1961 S -> P (in Ref. 1; BAA19526).
FT CONFLICT 2719 2719 Q -> H (in Ref. 1; BAA19526).
FT CONFLICT 2842 2842 N -> T (in Ref. 1; BAA19526).
FT CONFLICT 2976 2976 T -> A (in Ref. 1; BAA19526).
FT CONFLICT 3117 3117 R -> H (in Ref. 1; BAA19526).
FT CONFLICT 3668 3668 H -> R (in Ref. 1; BAA19526).
FT CONFLICT 3841 3841 A -> E (in Ref. 1; BAA19526).
FT CONFLICT 3847 3848 DK -> EE (in Ref. 1; BAA19526).
FT CONFLICT 4043 4043 T -> N (in Ref. 1; BAA19526).
FT CONFLICT 4284 4284 S -> A (in Ref. 1; BAA19526).
FT CONFLICT 4318 4318 R -> H (in Ref. 1; BAA19526).
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
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