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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
 
 
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