BGH3_HUMAN
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 03-AUG-2022, entry version 214.
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 -!- 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="http://atlasgeneticsoncology.org/Genes/TGFBIID42539ch5q31.html";
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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 PDBsum; 1X3B; -.
DR PDBsum; 2LTB; -.
DR PDBsum; 2LTC; -.
DR PDBsum; 2VXP; -.
DR PDBsum; 5NV6; -.
DR PDBsum; 7AS7; -.
DR PDBsum; 7ASC; -.
DR PDBsum; 7ASG; -.
DR AlphaFoldDB; Q15582; -.
DR SMR; Q15582; -.
DR BioGRID; 112903; 10.
DR CORUM; Q15582; -.
DR IntAct; Q15582; 12.
DR MINT; Q15582; -.
DR STRING; 9606.ENSP00000416330; -.
DR ChEMBL; CHEMBL4295829; -.
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; Q15582; -.
DR PeptideAtlas; Q15582; -.
DR PRIDE; Q15582; -.
DR ProteomicsDB; 60645; -.
DR Antibodypedia; 1982; 419 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 CTD; 7045; -.
DR DisGeNET; 7045; -.
DR GeneCards; TGFBI; -.
DR HGNC; HGNC:11771; TGFBI.
DR HPA; ENSG00000120708; Tissue enhanced (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; LHQVDRP; -.
DR OrthoDB; 926852at2759; -.
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 1078 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 196 other tissues.
DR ExpressionAtlas; Q15582; baseline and differential.
DR Genevisible; Q15582; HS.
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: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; -; 4.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR032954; TGFBI.
DR InterPro; IPR016666; TGFBI/POSTN.
DR PANTHER; PTHR10900:SF82; PTHR10900:SF82; 1.
DR Pfam; PF02469; Fasciclin; 4.
DR PIRSF; PIRSF016553; BIGH3_OSF2; 1.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF82153; SSF82153; 4.
DR PROSITE; PS51041; EMI; 1.
DR PROSITE; PS50213; FAS1; 4.
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 with Leu-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 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 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; unknown pathological 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
