ID BGH3_HUMAN Reviewed; 683 AA. AC Q15582; D3DQB1; O14471; O14472; O14476; O43216; O43217; O43218; O43219; AC Q53XM1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 223. DE RecName: Full=Transforming growth factor-beta-induced protein ig-h3; DE Short=Beta ig-h3; DE AltName: Full=Kerato-epithelin; DE AltName: Full=RGD-containing collagen-associated protein; DE Short=RGD-CAP; DE Flags: Precursor; GN Name=TGFBI; Synonyms=BIGH3; 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]. RX PubMed=1388724; DOI=10.1089/dna.1992.11.511; RA Skonier J., Neubauer M., Madisen L., Bennett K., Plowman G.D., RA Purchio A.F.; RT "cDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in RT a human adenocarcinoma cell line after treatment with transforming growth RT factor-beta."; RL DNA Cell Biol. 11:511-522(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CORNEAL DYSTROPHIES RP CYS-124; HIS-124; GLN-555 AND TRP-555. RX PubMed=9054935; DOI=10.1038/ng0397-247; RA Munier F.L., Korvatska E., Djemai A., le Paslier D., Zografos L., RA Pescia G., Schorderet D.F.; RT "Kerato-epithelin mutations in four 5q31-linked corneal dystrophies."; RL Nat. Genet. 15:247-251(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-200. RG NIEHS SNPs program; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 24-44, FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=8024701; DOI=10.1089/dna.1994.13.571; RA Skonier J., Bennett K., Rothwell V., Kosowski S., Plowman G., Wallace P., RA Edelhoff S., Disteche C.M., Neubauer M., Marquardt H., Rodgers J., RA Purchio A.F.; RT "Beta ig-h3: a transforming growth factor-beta-responsive gene encoding a RT secreted protein that inhibits cell attachment in vitro and suppresses the RT growth of CHO cells in nude mice."; RL DNA Cell Biol. 13:571-584(1994). RN [9] RP PROTEIN SEQUENCE OF 43-53; 77-108; 173-178; 220-234; 337-349; 437-447 AND RP 470-485, MASS SPECTROMETRY, DISULFIDE BOND, TISSUE SPECIFICITY, RP CHARACTERIZATION OF VARIANT CORNEAL DYSTROPHIES CYS-124, AND CYSTEINYLATION RP AT CYS-65. RX PubMed=27609313; DOI=10.1021/acs.biochem.6b00694; RA Lukassen M.V., Scavenius C., Thoegersen I.B., Enghild J.J.; RT "Disulfide bond pattern of transforming growth factor beta-induced RT protein."; RL Biochemistry 55:5610-5621(2016). RN [10] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=8077289; DOI=10.1002/jcp.1041600314; RA Escribano J., Hernando N., Ghosh S., Crabb J., Coca-Prados M.; RT "cDNA from human ocular ciliary epithelium homologous to beta ig-h3 is RT preferentially expressed as an extracellular protein in the corneal RT epithelium."; RL J. Cell. Physiol. 160:511-521(1994). RN [11] RP REVIEW ON VARIANTS CORNEAL DYSTROPHIES. RX PubMed=11501939; DOI=10.1007/s100380170041; RA Fujiki K., Nakayasu K., Kanai A.; RT "Corneal dystrophies in Japan."; RL J. Hum. Genet. 46:431-435(2001). RN [12] RP GAMMA-CARBOXYGLUTAMATION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=18450759; DOI=10.1074/jbc.m708029200; RA Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D., Galipeau J.; RT "Periostin, a member of a novel family of vitamin K-dependent proteins, is RT expressed by mesenchymal stromal cells."; RL J. Biol. Chem. 283:17991-18001(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP SUBCELLULAR LOCATION, AND LACK OF GAMMA-CARBOXYGLUTAMATION. RX PubMed=26273833; DOI=10.1371/journal.pone.0135374; RA Annis D.S., Ma H., Balas D.M., Kumfer K.T., Sandbo N., Potts G.K., RA Coon J.J., Mosher D.F.; RT "Absence of vitamin K-dependent gamma-carboxylation in human periostin RT extracted from fibrotic lung or secreted from a cell line engineered to RT optimize gamma-carboxylation."; RL PLoS ONE 10:E0135374-E0135374(2015). RN [15] RP STRUCTURE BY NMR OF 502-634. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the FAS1 domain of human transforming growth factor- RT beta induced protein IG-H3."; RL Submitted (JAN-2006) to the PDB data bank. RN [16] RP VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; GLN-555 AND TRP-555. RX PubMed=9463327; DOI=10.1086/301720; RA Korvatska E., Munier F.L., Djemai A., Wang M.X., Frueh B., Chiou A.G.-Y., RA Uffer S., Ballestrazzi E., Braunstein R.E., Forster R.K., Culbertson W.W., RA Boman H., Zografos L., Schorderet D.F.; RT "Mutation hot spots in 5q31-linked corneal dystrophies."; RL Am. J. Hum. Genet. 62:320-324(1998). RN [17] RP VARIANT CDL3A THR-501. RX PubMed=9497262; DOI=10.1086/301765; RA Yamamoto S., Okada M., Tsujikawa M., Shimomura Y., Nishida K., Inoue Y., RA Watanabe H., Maeda N., Kurahashi H., Kinoshita S., Nakamura Y., Tano Y.; RT "A kerato-epithelin (beta-ig-h3) mutation in lattice corneal dystrophy type RT IIIA."; RL Am. J. Hum. Genet. 62:719-722(1998). RN [18] RP VARIANT CDRB LEU-124. RX PubMed=9780098; DOI=10.1016/s0002-9394(98)00135-4; RA Okada M., Yamamoto S., Tsujikawa M., Watanabe H., Inoue Y., Maeda N., RA Shimomura Y., Nishida K., Quantock A.J., Kinoshita S., Tano Y.; RT "Two distinct kerato-epithelin mutations in Reis-Bucklers corneal RT dystrophy."; RL Am. J. Ophthalmol. 126:535-542(1998). RN [19] RP VARIANT CDL1 ARG-527. RX PubMed=9799082; DOI=10.1007/s004390050818; RA Fujiki K., Hotta Y., Nakayasu K., Yokoyama T., Takano T., Yamaguchi T., RA Kanai A.; RT "A new L527R mutation of the betaIGH3 gene in patients with lattice corneal RT dystrophy with deep stromal opacities."; RL Hum. Genet. 103:286-289(1998). RN [20] RP VARIANT CDRB PHE-540 DEL. RX PubMed=10660331; RA Rozzo C., Fossarello M., Galleri G., Sole G., Serru A., Orzalesi N., RA Serra A., Pirastu M.; RT "A common beta ig-h3 gene mutation (delta F540) in a large cohort of RT Sardinian Reis Buecklers' corneal dystrophy patients."; RL Hum. Mutat. 12:215-216(1998). RN [21] RP VARIANTS CORNEAL DYSTROPHIES HIS-124; SER-124 AND TRP-555. RX PubMed=10425035; RX DOI=10.1002/(sici)1098-1004(1999)14:2<126::aid-humu4>3.0.co;2-w; RA Stewart H.S., Ridgway A.E., Dixon M.J., Bonshek R.E., Parveen R., RA Black G.C.; RT "Heterogeneity in granular corneal dystrophy: identification of three RT causative mutations in the TGFBI (BIGH3) gene-lessons for corneal RT amyloidogenesis."; RL Hum. Mutat. 14:126-132(1999). RN [22] RP VARIANTS CDL HIS-622 AND ARG-626. RX PubMed=10328397; DOI=10.1016/s0161-6420(99)00539-4; RA Stewart H.S., Black G.C., Donnai D., Bonshek R.E., McCarthy J., Morgan S., RA Dixon M.J., Ridgway A.A.; RT "A mutation within exon 14 of the TGFBI (BIGH3) gene on chromosome 5q31 RT causes an asymmetric, late-onset form of lattice corneal dystrophy."; RL Ophthalmology 106:964-970(1999). RN [23] RP VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; LEU-124; THR-501; ARG-527; RP GLN-555 AND TRP-555, AND VARIANT SER-544. RX PubMed=11024425; DOI=10.1016/s0002-9394(00)00571-7; RA Mashima Y., Yamamoto S., Inoue Y., Yamada M., Konishi M., Watanabe H., RA Maeda N., Shimomura Y., Kinoshita S.; RT "Association of autosomal dominantly inherited corneal dystrophies with RT BIGH3 gene mutations in Japan."; RL Am. J. Ophthalmol. 130:516-517(2000). RN [24] RP VARIANTS CORNEAL DYSTROPHIES LEU-124 AND 125-THR-GLU-126 DEL. RX PubMed=10865320; DOI=10.1001/archopht.118.6.814; RA Dighiero P., Drunat S., D'Hermies F., Renard G., Delpech M., Valleix S.; RT "A novel variant of granular corneal dystrophy caused by association of 2 RT mutations in the TGFBI gene-R124L and deltaT125-deltaE126."; RL Arch. Ophthalmol. 118:814-818(2000). RN [25] RP VARIANT CDL1 PRO-518. RX PubMed=10837380; DOI=10.1136/bjo.84.6.583; RA Hirano K., Hotta Y., Fujiki K., Kanai A.; RT "Corneal amyloidosis caused by Leu518Pro mutation of betaig-h3 gene."; RL Br. J. Ophthalmol. 84:583-585(2000). RN [26] RP VARIANT CDL1 ARG-527. RX PubMed=11413411; DOI=10.1097/00003226-200107000-00017; RA Hirano K., Hotta Y., Nakamura M., Fujiki K., Kanai A., Yamamoto N.; RT "Late-onset form of lattice corneal dystrophy caused by Leu527Arg mutation RT of the TGFBI gene."; RL Cornea 20:525-529(2001). RN [27] RP VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; LEU-124; 125-THR-GLU-126 RP DEL; THR-546; GLN-555; TRP-555 AND ARG-626. RX PubMed=11297504; DOI=10.1016/s0161-6420(00)00662-x; RA Dighiero P., Niel F., Ellies P., D'Hermies F., Savoldelli M., Renard G., RA Delpech M., Valleix S.; RT "Histologic phenotype-genotype correlation of corneal dystrophies RT associated with eight distinct mutations in the TGFBI gene."; RL Ophthalmology 108:818-823(2001). RN [28] RP VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; SER-124; ARG-518; ARG-538; RP PHE-540 DEL; TRP-555; LYS-622; ASP-623; ARG-626 AND PRO-626, AND VARIANT RP ASP-631. RX PubMed=11923233; RA Munier F.L., Frueh B.E., Othenin-Girard P., Uffer S., Cousin P., Wang M.X., RA Heon E., Black G.C.M., Blasi M.A., Balestrazzi E., Lorenz B., Escoto R., RA Barraquer R., Hoeltzenbein M., Gloor B., Fossarello M., Singh A.D., RA Arsenijevic Y., Zografos L., Schorderet D.F.; RT "BIGH3 mutation spectrum in corneal dystrophies."; RL Invest. Ophthalmol. Vis. Sci. 43:949-954(2002). RN [29] RP VARIANT CDL1 ARG-569. RX PubMed=14597039; DOI=10.1016/s0002-9394(03)00541-5; RA Warren J.F., Abbott R.L., Yoon M.K., Crawford J.B., Spencer W.H., RA Margolis T.P.; RT "A new mutation (Leu569Arg) within exon 13 of the TGFBI (BIGH3) gene causes RT lattice corneal dystrophy type I."; RL Am. J. Ophthalmol. 136:872-878(2003). RN [30] RP VARIANT GRANULAR CORNEAL DYSTROPHY HIS-123. RX PubMed=12782158; DOI=10.1016/s0021-5155(03)00019-4; RA Ha N.T., Cung le X., Chau H.M., Thanh T.K., Fujiki K., Murakami A., RA Kanai A.; RT "A novel mutation of the TGFBI gene found in a Vietnamese family with RT atypical granular corneal dystrophy."; RL Jpn. J. Ophthalmol. 47:246-248(2003). RN [31] RP VARIANTS CDL1 ASP-546 AND GLN-551. RX PubMed=15531312; DOI=10.1016/j.ajo.2004.06.021; RA Aldave A.J., Gutmark J.G., Yellore V.S., Affeldt J.A., Meallet M.A., RA Udar N., Rao N.A., Small K.W., Klintworth G.K.; RT "Lattice corneal dystrophy associated with the Ala546Asp and Pro551Gln RT missense changes in the TGFBI gene."; RL Am. J. Ophthalmol. 138:772-781(2004). RN [32] RP VARIANTS CDL1 CYS-124 AND ARG-626, VARIANT CDRB LEU-124, VARIANT CDGG1 RP TRP-555, VARIANTS LATTICE CORNEAL DYSTROPHY ASP-539; VAL-594 AND RP 624-VAL-VAL-625 DEL, AND VARIANT PHE-269. RX PubMed=15623763; DOI=10.1167/iovs.04-0440; RA Chakravarthi S.V.V.K., Kannabiran C., Sridhar M.S., Vemuganti G.K.; RT "TGFBI gene mutations causing lattice and granular corneal dystrophies in RT Indian patients."; RL Invest. Ophthalmol. Vis. Sci. 46:121-125(2005). RN [33] RP VARIANT CDL3A SER-540. RX PubMed=15790870; DOI=10.1167/iovs.04-1319; RA Stix B., Leber M., Bingemer P., Gross C., Rueschoff J., Faendrich M., RA Schorderet D.F., Vorwerk C.K., Zacharias M., Roessner A., Roecken C.; RT "Hereditary lattice corneal dystrophy is associated with corneal amyloid RT deposits enclosing C-terminal fragments of keratoepithelin."; RL Invest. Ophthalmol. Vis. Sci. 46:1133-1139(2005). RN [34] RP VARIANT CDL1 ASP-505. RX PubMed=15838722; DOI=10.1007/s10384-004-0167-7; RA Tian X., Fujiki K., Wang W., Murakami A., Xie P., Kanai A., Liu Z.; RT "Novel mutation (V505D) of the TGFBI gene found in a Chinese family with RT lattice corneal dystrophy, type I."; RL Jpn. J. Ophthalmol. 49:84-88(2005). RN [35] RP VARIANTS EBMD ARG-509 AND SER-666. RX PubMed=16652336; DOI=10.1002/humu.20331; RA Boutboul S., Black G.C.M., Moore J.E., Sinton J., Menasche M., Munier F.L., RA Laroche L., Abitbol M., Schorderet D.F.; RT "A subset of patients with epithelial basement membrane corneal dystrophy RT have mutations in TGFBI/BIGH3."; RL Hum. Mutat. 27:553-557(2006). RN [36] RP VARIANT CDL1 ARG-572. RX PubMed=17013691; DOI=10.1007/s10384-006-0357-6; RA Atchaneeyasakul L.-O., Appukuttan B., Pingsuthiwong S., RA Yenchitsomanus P.-T., Trinavarat A., Srisawat C.; RT "A novel H572R mutation in the transforming growth factor-beta-induced gene RT in a Thai family with lattice corneal dystrophy type I."; RL Jpn. J. Ophthalmol. 50:403-408(2006). RN [37] RP VARIANT CDL1 HIS-572 DEL. RX PubMed=16541014; RA Aldave A.J., Rayner S.A., Kim B.T., Prechanond A., Yellore V.S.; RT "Unilateral lattice corneal dystrophy associated with the novel His572del RT mutation in the TGFBI gene."; RL Mol. Vis. 12:142-146(2006). RN [38] RP VARIANT GRANULAR CORNEAL DYSTROPHY ILE-113. RX PubMed=16636649; RA Zenteno J.C., Ramirez-Miranda A., Santacruz-Valdes C., Suarez-Sanchez R.; RT "Expanding the mutational spectrum in TGFBI-linked corneal dystrophies: RT identification of a novel and unusual mutation (Val113Ile) in a family with RT granular dystrophy."; RL Mol. Vis. 12:331-335(2006). CC -!- FUNCTION: Plays a role in cell adhesion (PubMed:8024701). May play a CC role in cell-collagen interactions (By similarity). CC {ECO:0000250|UniProtKB:O11780, ECO:0000269|PubMed:8024701}. CC -!- SUBUNIT: Binds to type I, II, and IV collagens. CC {ECO:0000250|UniProtKB:O11780}. CC -!- INTERACTION: CC Q15582; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-10236573, EBI-10175124; CC Q15582; P05107: ITGB2; NbExp=2; IntAct=EBI-10236573, EBI-300173; CC Q15582; Q15063: POSTN; NbExp=7; IntAct=EBI-10236573, EBI-7067070; CC Q15582; P25815: S100P; NbExp=3; IntAct=EBI-10236573, EBI-743700; CC Q15582; Q15582: TGFBI; NbExp=5; IntAct=EBI-10236573, EBI-10236573; CC Q15582; A0A0G2K692: Postn; Xeno; NbExp=5; IntAct=EBI-10236573, EBI-25473213; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18450759, CC ECO:0000269|PubMed:26273833, ECO:0000269|PubMed:8024701}. Secreted, CC extracellular space, extracellular matrix {ECO:0000269|PubMed:8077289}. CC Note=May be associated both with microfibrils and with the cell surface CC (PubMed:8077289). {ECO:0000269|PubMed:8077289}. CC -!- TISSUE SPECIFICITY: Highly expressed in the corneal epithelium CC (PubMed:27609313, PubMed:8077289). Expressed in heart, placenta, lung, CC liver, skeletal muscle, kidney and pancreas (PubMed:8077289). CC {ECO:0000269|PubMed:27609313, ECO:0000269|PubMed:8077289}. CC -!- INDUCTION: By TGF-beta (PubMed:1388724, PubMed:8024701). CC {ECO:0000269|PubMed:1388724, ECO:0000269|PubMed:8024701}. CC -!- PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated; CC gamma-carboxyglutamate residues are formed by vitamin K dependent CC carboxylation; these residues may be required for binding to calcium CC (PubMed:18450759). According to a more recent report, does not contain CC vitamin K-dependent gamma-carboxyglutamate residues (PubMed:26273833). CC {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}. CC -!- PTM: The EMI domain contains 2 expected intradomain disulfide bridges CC (Cys-49-Cys85 and Cys-84-Cys-97) and one unusual interdomain disulfide CC bridge to the second FAS1 domain (Cys-74-Cys-339). This arrangement CC violates the predicted disulfide bridge pattern of an EMI domain. CC {ECO:0000305|PubMed:27609313}. CC -!- DISEASE: Corneal dystrophy, epithelial basement membrane (EBMD) CC [MIM:121820]: A bilateral anterior corneal dystrophy characterized by CC grayish epithelial fingerprint lines, geographic map-like lines, and CC dots (or microcysts) on slit-lamp examination. Pathologic studies show CC abnormal, redundant basement membrane and intraepithelial lacunae CC filled with cellular debris. {ECO:0000269|PubMed:16652336}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Corneal dystrophy, Groenouw type 1 (CDGG1) [MIM:121900]: A CC rare form of stromal corneal dystrophy characterized by multiple small CC deposits in the superficial central corneal stroma, and progressive CC visual impairment. {ECO:0000269|PubMed:15623763}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Corneal dystrophy, lattice type 1 (CDL1) [MIM:122200]: A form CC of lattice corneal dystrophy, a class of inherited stromal amyloidoses CC characterized by pathognomonic branching lattice figures in the cornea. CC CDL1 is characterized by progressive visual impairment, and the CC presence of delicate, double-contoured, interdigitating, elongated CC deposits that form a reticular pattern in the corneal stroma. Systemic CC amyloidosis is absent. Recurrent corneal ulceration sometimes occurs. CC {ECO:0000269|PubMed:10837380, ECO:0000269|PubMed:11413411, CC ECO:0000269|PubMed:14597039, ECO:0000269|PubMed:15531312, CC ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:15838722, CC ECO:0000269|PubMed:16541014, ECO:0000269|PubMed:17013691, CC ECO:0000269|PubMed:9799082}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Corneal dystrophy, Thiel-Behnke type (CDTB) [MIM:602082]: A CC bilateral disorder of the cornea characterized by progressive CC honeycomb-like, subepithelial corneal opacities with recurrent CC erosions. Note=The disease is caused by variants affecting the gene CC represented in this entry. CC -!- DISEASE: Corneal dystrophy, Reis-Bucklers type (CDRB) [MIM:608470]: A CC bilateral disorder of the cornea characterized by intermittent attacks CC of ocular irritation, recurrent painful corneal erosions starting in CC childhood, corneal opacities in a geographic pattern at the level of CC the Bowman layer, and a progressive decrease of visual acuity. The CC lesions are primarily in Bowman membrane with secondary involvement of CC the epithelium and superficial part of the stroma. Bowman membrane is CC almost completely replaced by pathologic materials including CC disoriented collagen fibrils. {ECO:0000269|PubMed:10660331, CC ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:9780098}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Corneal dystrophy, lattice type 3A (CDL3A) [MIM:608471]: A CC form of lattice corneal dystrophy, a class of inherited stromal CC amyloidoses characterized by pathognomonic branching lattice figures in CC the cornea. CDL3A is characterized by decreased visual acuity, and the CC presence of thick, ropy branching lattice lines and accumulations of CC amyloid deposits in the corneal stroma. Systemic amyloidosis is absent. CC CDL3A clinically resembles to lattice corneal dystrophy type 3, but CC differs in that its age of onset is 70 to 90 years. It has an autosomal CC dominant inheritance pattern. {ECO:0000269|PubMed:15790870, CC ECO:0000269|PubMed:9497262}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Corneal dystrophy, Avellino type (CDA) [MIM:607541]: A corneal CC disease resulting in reduced visual acuity and characterized by gray, CC crumb-like granular deposits in the anterior third of the stroma in CC each corneal button. Fusiform amyloid deposits, histochemically and CC morphologically identical to those of lattice corneal dystrophy, are CC found in the deeper stroma. Additional features include recurrent CC corneal erosions, and glare and decreased night vision. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/tgfbi/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42539/TGFBI"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M77349; AAA61163.1; -; mRNA. DR EMBL; AF035626; AAB88695.1; -; Genomic_DNA. DR EMBL; AF035627; AAB88698.1; -; Genomic_DNA. DR EMBL; AF035628; AAB88696.1; -; Genomic_DNA. DR EMBL; AF035629; AAB88697.1; -; Genomic_DNA. DR EMBL; AY149344; AAN10294.1; -; Genomic_DNA. DR EMBL; BT009820; AAP88822.1; -; mRNA. DR EMBL; AC004503; AAC08449.1; -; Genomic_DNA. DR EMBL; AC005219; AAC24944.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62199.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62200.1; -; Genomic_DNA. DR EMBL; BC000097; AAH00097.1; -; mRNA. DR EMBL; BC004972; AAH04972.1; -; mRNA. DR CCDS; CCDS47266.1; -. DR PIR; I52996; I52996. DR RefSeq; NP_000349.1; NM_000358.2. DR PDB; 1X3B; NMR; -; A=502-634. DR PDB; 2LTB; NMR; -; A=502-634. DR PDB; 2LTC; NMR; -; A=502-634. DR PDB; 2VXP; X-ray; 2.50 A; A/B=502-633. DR PDB; 5NV6; X-ray; 2.93 A; A/B=1-683. DR PDB; 7AS7; X-ray; 2.65 A; A=45-632. DR PDB; 7ASC; X-ray; 4.80 A; A/B=45-633. DR PDB; 7ASG; X-ray; 2.00 A; A=45-632. DR PDB; 8HGA; NMR; -; A/B/C/D=611-633. DR PDB; 8HIA; EM; 4.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=611-633. DR PDBsum; 1X3B; -. DR PDBsum; 2LTB; -. DR PDBsum; 2LTC; -. DR PDBsum; 2VXP; -. DR PDBsum; 5NV6; -. DR PDBsum; 7AS7; -. DR PDBsum; 7ASC; -. DR PDBsum; 7ASG; -. DR PDBsum; 8HGA; -. DR PDBsum; 8HIA; -. DR AlphaFoldDB; Q15582; -. DR EMDB; EMD-34813; -. DR SMR; Q15582; -. DR BioGRID; 112903; 14. DR CORUM; Q15582; -. DR IntAct; Q15582; 13. DR MINT; Q15582; -. DR STRING; 9606.ENSP00000416330; -. DR ChEMBL; CHEMBL4295829; -. DR GlyGen; Q15582; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q15582; -. DR PhosphoSitePlus; Q15582; -. DR BioMuta; TGFBI; -. DR DMDM; 2498193; -. DR EPD; Q15582; -. DR jPOST; Q15582; -. DR MassIVE; Q15582; -. DR MaxQB; Q15582; -. DR PaxDb; 9606-ENSP00000416330; -. DR PeptideAtlas; Q15582; -. DR ProteomicsDB; 60645; -. DR Pumba; Q15582; -. DR Antibodypedia; 1982; 478 antibodies from 40 providers. DR DNASU; 7045; -. DR Ensembl; ENST00000442011.7; ENSP00000416330.2; ENSG00000120708.17. DR GeneID; 7045; -. DR KEGG; hsa:7045; -. DR MANE-Select; ENST00000442011.7; ENSP00000416330.2; NM_000358.3; NP_000349.1. DR UCSC; uc003lbf.5; human. DR AGR; HGNC:11771; -. DR CTD; 7045; -. DR DisGeNET; 7045; -. DR GeneCards; TGFBI; -. DR HGNC; HGNC:11771; TGFBI. DR HPA; ENSG00000120708; Tissue enhanced (choroid plexus, placenta). DR MalaCards; TGFBI; -. DR MIM; 121820; phenotype. DR MIM; 121900; phenotype. DR MIM; 122200; phenotype. DR MIM; 601692; gene. DR MIM; 602082; phenotype. DR MIM; 607541; phenotype. DR MIM; 608470; phenotype. DR MIM; 608471; phenotype. DR neXtProt; NX_Q15582; -. DR OpenTargets; ENSG00000120708; -. DR Orphanet; 98956; Epithelial basement membrane dystrophy. DR Orphanet; 98962; Granular corneal dystrophy type I. DR Orphanet; 98963; Granular corneal dystrophy type II. DR Orphanet; 98964; Lattice corneal dystrophy type I. DR Orphanet; 98961; Reis-Buecklers corneal dystrophy. DR Orphanet; 98960; Thiel-Behnke corneal dystrophy. DR PharmGKB; PA36484; -. DR VEuPathDB; HostDB:ENSG00000120708; -. DR eggNOG; KOG1437; Eukaryota. DR GeneTree; ENSGT00530000063860; -. DR HOGENOM; CLU_017611_1_0_1; -. DR InParanoid; Q15582; -. DR OMA; NSMERYT; -. DR OrthoDB; 523796at2759; -. DR PhylomeDB; Q15582; -. DR TreeFam; TF316269; -. DR PathwayCommons; Q15582; -. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SignaLink; Q15582; -. DR SIGNOR; Q15582; -. DR BioGRID-ORCS; 7045; 8 hits in 1156 CRISPR screens. DR ChiTaRS; TGFBI; human. DR EvolutionaryTrace; Q15582; -. DR GeneWiki; TGFBI; -. DR GenomeRNAi; 7045; -. DR Pharos; Q15582; Tbio. DR PRO; PR:Q15582; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q15582; Protein. DR Bgee; ENSG00000120708; Expressed in amniotic fluid and 198 other cell types or tissues. DR ExpressionAtlas; Q15582; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL. DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central. DR GO; GO:0005518; F:collagen binding; IPI:BHF-UCL. DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005178; F:integrin binding; TAS:ProtInc. DR GO; GO:0001525; P:angiogenesis; IEP:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central. DR GO; GO:0008283; P:cell population proliferation; TAS:ProtInc. DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0051179; P:localization; IMP:DisProt. DR GO; GO:0007162; P:negative regulation of cell adhesion; TAS:ProtInc. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR Gene3D; 2.30.180.10; FAS1 domain; 4. DR InterPro; IPR011489; EMI_domain. DR InterPro; IPR036378; FAS1_dom_sf. DR InterPro; IPR000782; FAS1_domain. DR InterPro; IPR016666; TGFBI/POSTN. DR PANTHER; PTHR10900; PERIOSTIN-RELATED; 1. DR PANTHER; PTHR10900:SF82; TRANSFORMING GROWTH FACTOR-BETA-INDUCED PROTEIN IG-H3; 1. DR Pfam; PF02469; Fasciclin; 4. DR PIRSF; PIRSF016553; BIGH3_OSF2; 1. DR SMART; SM00554; FAS1; 4. DR SUPFAM; SSF82153; FAS1 domain; 4. DR PROSITE; PS51041; EMI; 1. DR PROSITE; PS50213; FAS1; 4. DR Genevisible; Q15582; HS. PE 1: Evidence at protein level; KW 3D-structure; Amyloid; Amyloidosis; Cell adhesion; Corneal dystrophy; KW Direct protein sequencing; Disease variant; Disulfide bond; KW Extracellular matrix; Gamma-carboxyglutamic acid; Phosphoprotein; KW Reference proteome; Repeat; Secreted; Sensory transduction; Signal; Vision. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:8024701" FT CHAIN 24..683 FT /note="Transforming growth factor-beta-induced protein ig- FT h3" FT /id="PRO_0000008769" FT DOMAIN 45..99 FT /note="EMI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384" FT DOMAIN 103..236 FT /note="FAS1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 240..371 FT /note="FAS1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 375..498 FT /note="FAS1 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 502..632 FT /note="FAS1 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT MOTIF 642..644 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 65 FT /note="S-cysteinyl cysteine" FT /evidence="ECO:0000269|PubMed:27609313" FT DISULFID 49..85 FT /evidence="ECO:0000269|PubMed:27609313" FT DISULFID 74..339 FT /evidence="ECO:0000269|PubMed:27609313" FT DISULFID 84..97 FT /evidence="ECO:0000269|PubMed:27609313" FT DISULFID 214..317 FT /evidence="ECO:0000269|PubMed:27609313" FT DISULFID 473..478 FT /evidence="ECO:0000269|PubMed:27609313" FT VARIANT 113 FT /note="V -> I (in granular corneal dystrophy; unclassified FT form; with centrifuge pattern of opacities; FT dbSNP:rs757933370)" FT /evidence="ECO:0000269|PubMed:16636649" FT /id="VAR_031531" FT VARIANT 123 FT /note="D -> H (in granular corneal dystrophy; unclassified FT form; Hanoi; dbSNP:rs541270955)" FT /evidence="ECO:0000269|PubMed:12782158" FT /id="VAR_031532" FT VARIANT 124 FT /note="R -> C (in CDL1; cysteinylated; no effect on the FT disulfide bond pattern; dbSNP:rs121909210)" FT /evidence="ECO:0000269|PubMed:11024425, FT ECO:0000269|PubMed:11297504, ECO:0000269|PubMed:11923233, FT ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:27609313, FT ECO:0000269|PubMed:9054935, ECO:0000269|PubMed:9463327" FT /id="VAR_077904" FT VARIANT 124 FT /note="R -> H (in CDA; most common mutation in Japanese; FT dbSNP:rs121909211)" FT /evidence="ECO:0000269|PubMed:10425035, FT ECO:0000269|PubMed:11024425, ECO:0000269|PubMed:11297504, FT ECO:0000269|PubMed:11923233, ECO:0000269|PubMed:9054935, FT ECO:0000269|PubMed:9463327" FT /id="VAR_005077" FT VARIANT 124 FT /note="R -> L (in CDRB; dbSNP:rs121909211)" FT /evidence="ECO:0000269|PubMed:10865320, FT ECO:0000269|PubMed:11024425, ECO:0000269|PubMed:11297504, FT ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:9780098" FT /id="VAR_005078" FT VARIANT 124 FT /note="R -> S (in CDGG1; late-onset; mild ocular irritation FT and reduction in visual acuity; dbSNP:rs121909210)" FT /evidence="ECO:0000269|PubMed:10425035, FT ECO:0000269|PubMed:11923233" FT /id="VAR_012444" FT VARIANT 125..126 FT /note="Missing (associated in cis with L-124 in atypical FT granular dystrophy; French granular variant)" FT /evidence="ECO:0000269|PubMed:10865320, FT ECO:0000269|PubMed:11297504" FT /id="VAR_012445" FT VARIANT 200 FT /note="I -> F (in dbSNP:rs45455404)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_014335" FT VARIANT 269 FT /note="L -> F (in dbSNP:rs199852470)" FT /evidence="ECO:0000269|PubMed:15623763" FT /id="VAR_031533" FT VARIANT 496 FT /note="R -> G (in dbSNP:rs10057190)" FT /id="VAR_031534" FT VARIANT 501 FT /note="P -> T (in CDL3A; dbSNP:rs121909212)" FT /evidence="ECO:0000269|PubMed:11024425, FT ECO:0000269|PubMed:9497262" FT /id="VAR_005079" FT VARIANT 505 FT /note="V -> D (in CDL1)" FT /evidence="ECO:0000269|PubMed:15838722" FT /id="VAR_031535" FT VARIANT 509 FT /note="L -> R (in EBMD; dbSNP:rs121909216)" FT /evidence="ECO:0000269|PubMed:16652336" FT /id="VAR_031536" FT VARIANT 518 FT /note="L -> P (in CDL1)" FT /evidence="ECO:0000269|PubMed:10837380" FT /id="VAR_012446" FT VARIANT 518 FT /note="L -> R (in CDL1; severe phenotype; delayed age of FT onset)" FT /evidence="ECO:0000269|PubMed:11923233" FT /id="VAR_018484" FT VARIANT 527 FT /note="L -> R (in CDL1; late-onset; found also in sporadic FT cases; dbSNP:rs1050842080)" FT /evidence="ECO:0000269|PubMed:11024425, FT ECO:0000269|PubMed:11413411, ECO:0000269|PubMed:9799082" FT /id="VAR_005080" FT VARIANT 538 FT /note="T -> R (in CDL1; delayed age of onset)" FT /evidence="ECO:0000269|PubMed:11923233" FT /id="VAR_018485" FT VARIANT 539 FT /note="V -> D (in lattice corneal dystrophy; unclassified FT form; dbSNP:rs1382893670)" FT /evidence="ECO:0000269|PubMed:15623763" FT /id="VAR_031537" FT VARIANT 540 FT /note="F -> S (in CDL3A; dbSNP:rs121909214)" FT /evidence="ECO:0000269|PubMed:15790870" FT /id="VAR_031538" FT VARIANT 540 FT /note="Missing (in CDRB)" FT /evidence="ECO:0000269|PubMed:10660331, FT ECO:0000269|PubMed:11923233" FT /id="VAR_005081" FT VARIANT 544 FT /note="N -> S (found in lattice corneal dystrophy; FT unclassified form; late-onset; dbSNP:rs777288957)" FT /evidence="ECO:0000269|PubMed:11024425" FT /id="VAR_012447" FT VARIANT 546 FT /note="A -> D (in CDL1; associated in cis with Q-551; FT dbSNP:rs267607109)" FT /evidence="ECO:0000269|PubMed:15531312" FT /id="VAR_031539" FT VARIANT 546 FT /note="A -> T (in CDL3A)" FT /evidence="ECO:0000269|PubMed:11297504" FT /id="VAR_012448" FT VARIANT 551 FT /note="P -> Q (in CDL1; associated in cis with D-546; FT dbSNP:rs267607110)" FT /evidence="ECO:0000269|PubMed:15531312" FT /id="VAR_031540" FT VARIANT 555 FT /note="R -> Q (in CDTB; originally thought to cause CDRB; FT dbSNP:rs121909209)" FT /evidence="ECO:0000269|PubMed:11024425, FT ECO:0000269|PubMed:11297504, ECO:0000269|PubMed:9054935, FT ECO:0000269|PubMed:9463327" FT /id="VAR_005082" FT VARIANT 555 FT /note="R -> W (in CDGG1; common mutation in Europe and FT United States; rare in Japan; dbSNP:rs121909208)" FT /evidence="ECO:0000269|PubMed:10425035, FT ECO:0000269|PubMed:11024425, ECO:0000269|PubMed:11297504, FT ECO:0000269|PubMed:11923233, ECO:0000269|PubMed:15623763, FT ECO:0000269|PubMed:9054935, ECO:0000269|PubMed:9463327" FT /id="VAR_005083" FT VARIANT 569 FT /note="L -> R (in CDL1)" FT /evidence="ECO:0000269|PubMed:14597039" FT /id="VAR_031541" FT VARIANT 572 FT /note="H -> R (in CDL1; late-onset)" FT /evidence="ECO:0000269|PubMed:17013691" FT /id="VAR_031543" FT VARIANT 572 FT /note="Missing (in CDL1; late-onset and unilateral FT phenotype)" FT /evidence="ECO:0000269|PubMed:16541014" FT /id="VAR_031542" FT VARIANT 594 FT /note="G -> V (in lattice corneal dystrophy; unclassified FT form)" FT /evidence="ECO:0000269|PubMed:15623763" FT /id="VAR_031544" FT VARIANT 622 FT /note="N -> H (in asymmetric lattice corneal dystrophy)" FT /evidence="ECO:0000269|PubMed:10328397" FT /id="VAR_012449" FT VARIANT 622 FT /note="N -> K (in CDL3A)" FT /evidence="ECO:0000269|PubMed:11923233" FT /id="VAR_018486" FT VARIANT 623 FT /note="G -> D (in CDL1; delayed age of onset; FT dbSNP:rs121909215)" FT /evidence="ECO:0000269|PubMed:11923233" FT /id="VAR_018487" FT VARIANT 624..625 FT /note="Missing (in lattice corneal dystrophy; unclassified FT form)" FT /evidence="ECO:0000269|PubMed:15623763" FT /id="VAR_031545" FT VARIANT 626 FT /note="H -> P (in CDL1)" FT /evidence="ECO:0000269|PubMed:11923233" FT /id="VAR_018488" FT VARIANT 626 FT /note="H -> R (in CDL1; delayed age of onset; FT dbSNP:rs1052006472)" FT /evidence="ECO:0000269|PubMed:10328397, FT ECO:0000269|PubMed:11297504, ECO:0000269|PubMed:11923233, FT ECO:0000269|PubMed:15623763" FT /id="VAR_012450" FT VARIANT 631 FT /note="V -> D (found in lattice corneal dystrophy; FT unclassified form)" FT /evidence="ECO:0000269|PubMed:11923233" FT /id="VAR_018489" FT VARIANT 666 FT /note="R -> S (in EBMD; uncertain significance; FT dbSNP:rs121909217)" FT /evidence="ECO:0000269|PubMed:16652336" FT /id="VAR_031546" FT STRAND 48..57 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 76..84 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 106..112 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 116..125 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 128..133 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 145..149 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 153..160 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 163..173 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:7ASG" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:5NV6" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 215..224 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 227..234 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 243..249 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 254..263 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 266..270 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:7AS7" FT STRAND 275..280 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 282..286 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 290..297 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 300..308 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 311..314 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 325..328 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 334..340 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 343..346 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 352..359 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 362..369 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 379..383 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 389..397 FT /evidence="ECO:0007829|PDB:7ASG" FT TURN 398..400 FT /evidence="ECO:0007829|PDB:7AS7" FT HELIX 402..405 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 410..415 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 417..420 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 429..436 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 454..457 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 462..467 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 477..485 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 490..496 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 505..510 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 516..524 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 530..532 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 533..535 FT /evidence="ECO:0007829|PDB:1X3B" FT STRAND 537..542 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 544..549 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 552..555 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 562..571 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 573..576 FT /evidence="ECO:0007829|PDB:7ASG" FT HELIX 580..582 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 587..591 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 594..602 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 605..608 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 614..620 FT /evidence="ECO:0007829|PDB:7ASG" FT STRAND 623..630 FT /evidence="ECO:0007829|PDB:7ASG" SQ SEQUENCE 683 AA; 74681 MW; 40FDC8A71EBB3D00 CRC64; MALFVRLLAL ALALALGPAA TLAGPAKSPY QLVLQHSRLR GRQHGPNVCA VQKVIGTNRK YFTNCKQWYQ RKICGKSTVI SYECCPGYEK VPGEKGCPAA LPLSNLYETL GVVGSTTTQL YTDRTEKLRP EMEGPGSFTI FAPSNEAWAS LPAEVLDSLV SNVNIELLNA LRYHMVGRRV LTDELKHGMT LTSMYQNSNI QIHHYPNGIV TVNCARLLKA DHHATNGVVH LIDKVISTIT NNIQQIIEIE DTFETLRAAV AASGLNTMLE GNGQYTLLAP TNEAFEKIPS ETLNRILGDP EALRDLLNNH ILKSAMCAEA IVAGLSVETL EGTTLEVGCS GDMLTINGKA IISNKDILAT NGVIHYIDEL LIPDSAKTLF ELAAESDVST AIDLFRQAGL GNHLSGSERL TLLAPLNSVF KDGTPPIDAH TRNLLRNHII KDQLASKYLY HGQTLETLGG KKLRVFVYRN SLCIENSCIA AHDKRGRYGT LFTMDRVLTP PMGTVMDVLK GDNRFSMLVA AIQSAGLTET LNREGVYTVF APTNEAFRAL PPRERSRLLG DAKELANILK YHIGDEILVS GGIGALVRLK SLQGDKLEVS LKNNVVSVNK EPVAEPDIMA TNGVVHVITN VLQPPANRPQ ERGDELADSA LEIFKQASAF SRASQRSVRL APVYQKLLER MKH //