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Transforming growth factor-beta-induced protein ig-h3 (Beta ig-h3) (Kerato-epithelin) (RGD-containing collagen-associated protein) (RGD-CAP)

 BGH3_HUMAN              Reviewed;         683 AA.
Q15582; D3DQB1; O14471; O14472; O14476; O43216; O43217; O43218;
O43219; Q53XM1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 187.
RecName: Full=Transforming growth factor-beta-induced protein ig-h3;
Short=Beta ig-h3;
AltName: Full=Kerato-epithelin;
AltName: Full=RGD-containing collagen-associated protein;
Short=RGD-CAP;
Flags: Precursor;
Name=TGFBI; Synonyms=BIGH3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1388724; DOI=10.1089/dna.1992.11.511;
Skonier J., Neubauer M., Madisen L., Bennett K., Plowman G.D.,
Purchio A.F.;
"cDNA cloning and sequence analysis of beta ig-h3, a novel gene
induced in a human adenocarcinoma cell line after treatment with
transforming growth factor-beta.";
DNA Cell Biol. 11:511-522(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CORNEAL DYSTROPHIES
CYS-124; HIS-124; GLN-555 AND TRP-555.
PubMed=9054935; DOI=10.1038/ng0397-247;
Munier F.L., Korvatska E., Djemai A., le Paslier D., Zografos L.,
Pescia G., Schorderet D.F.;
"Kerato-epithelin mutations in four 5q31-linked corneal dystrophies.";
Nat. Genet. 15:247-251(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-200.
NIEHS SNPs program;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 24-44, FUNCTION, INDUCTION, SUBCELLULAR LOCATION,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=8024701; DOI=10.1089/dna.1994.13.571;
Skonier J., Bennett K., Rothwell V., Kosowski S., Plowman G.,
Wallace P., Edelhoff S., Disteche C.M., Neubauer M., Marquardt H.,
Rodgers J., Purchio A.F.;
"Beta ig-h3: a transforming growth factor-beta-responsive gene
encoding a secreted protein that inhibits cell attachment in vitro and
suppresses the growth of CHO cells in nude mice.";
DNA Cell Biol. 13:571-584(1994).
[9]
PROTEIN SEQUENCE OF 43-53; 77-108; 173-178; 220-234; 337-349; 437-447
AND 470-485, MASS SPECTROMETRY, DISULFIDE BOND, TISSUE SPECIFICITY,
CHARACTERIZATION OF VARIANT CORNEAL DYSTROPHIES CYS-124, AND
CYSTEINYLATION AT CYS-65.
PubMed=27609313; DOI=10.1021/acs.biochem.6b00694;
Lukassen M.V., Scavenius C., Thoegersen I.B., Enghild J.J.;
"Disulfide bond pattern of transforming growth factor beta-induced
protein.";
Biochemistry 55:5610-5621(2016).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8077289; DOI=10.1002/jcp.1041600314;
Escribano J., Hernando N., Ghosh S., Crabb J., Coca-Prados M.;
"cDNA from human ocular ciliary epithelium homologous to beta ig-h3 is
preferentially expressed as an extracellular protein in the corneal
epithelium.";
J. Cell. Physiol. 160:511-521(1994).
[11]
REVIEW ON VARIANTS CORNEAL DYSTROPHIES.
PubMed=11501939; DOI=10.1007/s100380170041;
Fujiki K., Nakayasu K., Kanai A.;
"Corneal dystrophies in Japan.";
J. Hum. Genet. 46:431-435(2001).
[12]
GAMMA-CARBOXYGLUTAMATION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=18450759; DOI=10.1074/jbc.M708029200;
Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D.,
Galipeau J.;
"Periostin, a member of a novel family of vitamin K-dependent
proteins, is expressed by mesenchymal stromal cells.";
J. Biol. Chem. 283:17991-18001(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
SUBCELLULAR LOCATION, AND LACK OF GAMMA-CARBOXYGLUTAMATION.
PubMed=26273833; DOI=10.1371/journal.pone.0135374;
Annis D.S., Ma H., Balas D.M., Kumfer K.T., Sandbo N., Potts G.K.,
Coon J.J., Mosher D.F.;
"Absence of vitamin K-dependent gamma-carboxylation in human periostin
extracted from fibrotic lung or secreted from a cell line engineered
to optimize gamma-carboxylation.";
PLoS ONE 10:E0135374-E0135374(2015).
[15]
STRUCTURE BY NMR OF 502-634.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the FAS1 domain of human transforming growth
factor-beta induced protein IG-H3.";
Submitted (JAN-2006) to the PDB data bank.
[16]
VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; GLN-555 AND TRP-555.
PubMed=9463327; DOI=10.1086/301720;
Korvatska E., Munier F.L., Djemai A., Wang M.X., Frueh B.,
Chiou A.G.-Y., Uffer S., Ballestrazzi E., Braunstein R.E.,
Forster R.K., Culbertson W.W., Boman H., Zografos L., Schorderet D.F.;
"Mutation hot spots in 5q31-linked corneal dystrophies.";
Am. J. Hum. Genet. 62:320-324(1998).
[17]
VARIANT CDL3A THR-501.
PubMed=9497262; DOI=10.1086/301765;
Yamamoto S., Okada M., Tsujikawa M., Shimomura Y., Nishida K.,
Inoue Y., Watanabe H., Maeda N., Kurahashi H., Kinoshita S.,
Nakamura Y., Tano Y.;
"A kerato-epithelin (beta-ig-h3) mutation in lattice corneal dystrophy
type IIIA.";
Am. J. Hum. Genet. 62:719-722(1998).
[18]
VARIANT CDRB LEU-124.
PubMed=9780098; DOI=10.1016/S0002-9394(98)00135-4;
Okada M., Yamamoto S., Tsujikawa M., Watanabe H., Inoue Y., Maeda N.,
Shimomura Y., Nishida K., Quantock A.J., Kinoshita S., Tano Y.;
"Two distinct kerato-epithelin mutations in Reis-Bucklers corneal
dystrophy.";
Am. J. Ophthalmol. 126:535-542(1998).
[19]
VARIANT CDL1 ARG-527.
PubMed=9799082; DOI=10.1007/s004390050818;
Fujiki K., Hotta Y., Nakayasu K., Yokoyama T., Takano T.,
Yamaguchi T., Kanai A.;
"A new L527R mutation of the betaIGH3 gene in patients with lattice
corneal dystrophy with deep stromal opacities.";
Hum. Genet. 103:286-289(1998).
[20]
VARIANT CDRB PHE-540 DEL.
PubMed=10660331;
Rozzo C., Fossarello M., Galleri G., Sole G., Serru A., Orzalesi N.,
Serra A., Pirastu M.;
"A common beta ig-h3 gene mutation (delta F540) in a large cohort of
Sardinian Reis Buecklers' corneal dystrophy patients.";
Hum. Mutat. 12:215-216(1998).
[21]
VARIANTS CORNEAL DYSTROPHIES HIS-124; SER-124 AND TRP-555.
PubMed=10425035;
DOI=10.1002/(SICI)1098-1004(1999)14:2<126::AID-HUMU4>3.0.CO;2-W;
Stewart H.S., Ridgway A.E., Dixon M.J., Bonshek R.E., Parveen R.,
Black G.C.;
"Heterogeneity in granular corneal dystrophy: identification of three
causative mutations in the TGFBI (BIGH3) gene-lessons for corneal
amyloidogenesis.";
Hum. Mutat. 14:126-132(1999).
[22]
VARIANTS CDL HIS-622 AND ARG-626.
PubMed=10328397; DOI=10.1016/S0161-6420(99)00539-4;
Stewart H.S., Black G.C., Donnai D., Bonshek R.E., McCarthy J.,
Morgan S., Dixon M.J., Ridgway A.A.;
"A mutation within exon 14 of the TGFBI (BIGH3) gene on chromosome
5q31 causes an asymmetric, late-onset form of lattice corneal
dystrophy.";
Ophthalmology 106:964-970(1999).
[23]
VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; LEU-124; THR-501;
ARG-527; GLN-555 AND TRP-555, AND VARIANT SER-544.
PubMed=11024425; DOI=10.1016/S0002-9394(00)00571-7;
Mashima Y., Yamamoto S., Inoue Y., Yamada M., Konishi M., Watanabe H.,
Maeda N., Shimomura Y., Kinoshita S.;
"Association of autosomal dominantly inherited corneal dystrophies
with BIGH3 gene mutations in Japan.";
Am. J. Ophthalmol. 130:516-517(2000).
[24]
VARIANTS CORNEAL DYSTROPHIES LEU-124 AND 125-THR-GLU-126 DEL.
PubMed=10865320; DOI=10.1001/archopht.118.6.814;
Dighiero P., Drunat S., D'Hermies F., Renard G., Delpech M.,
Valleix S.;
"A novel variant of granular corneal dystrophy caused by association
of 2 mutations in the TGFBI gene-R124L and deltaT125-deltaE126.";
Arch. Ophthalmol. 118:814-818(2000).
[25]
VARIANT CDL1 PRO-518.
PubMed=10837380; DOI=10.1136/bjo.84.6.583;
Hirano K., Hotta Y., Fujiki K., Kanai A.;
"Corneal amyloidosis caused by Leu518Pro mutation of betaig-h3 gene.";
Br. J. Ophthalmol. 84:583-585(2000).
[26]
VARIANT CDL1 ARG-527.
PubMed=11413411; DOI=10.1097/00003226-200107000-00017;
Hirano K., Hotta Y., Nakamura M., Fujiki K., Kanai A., Yamamoto N.;
"Late-onset form of lattice corneal dystrophy caused by Leu527Arg
mutation of the TGFBI gene.";
Cornea 20:525-529(2001).
[27]
VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; LEU-124;
125-THR-GLU-126 DEL; THR-546; GLN-555; TRP-555 AND ARG-626.
PubMed=11297504; DOI=10.1016/S0161-6420(00)00662-X;
Dighiero P., Niel F., Ellies P., D'Hermies F., Savoldelli M.,
Renard G., Delpech M., Valleix S.;
"Histologic phenotype-genotype correlation of corneal dystrophies
associated with eight distinct mutations in the TGFBI gene.";
Ophthalmology 108:818-823(2001).
[28]
VARIANTS CORNEAL DYSTROPHIES CYS-124; HIS-124; SER-124; ARG-518;
ARG-538; PHE-540 DEL; TRP-555; LYS-622; ASP-623; ARG-626 AND PRO-626,
AND VARIANT ASP-631.
PubMed=11923233;
Munier F.L., Frueh B.E., Othenin-Girard P., Uffer S., Cousin P.,
Wang M.X., Heon E., Black G.C.M., Blasi M.A., Balestrazzi E.,
Lorenz B., Escoto R., Barraquer R., Hoeltzenbein M., Gloor B.,
Fossarello M., Singh A.D., Arsenijevic Y., Zografos L.,
Schorderet D.F.;
"BIGH3 mutation spectrum in corneal dystrophies.";
Invest. Ophthalmol. Vis. Sci. 43:949-954(2002).
[29]
VARIANT CDL1 ARG-569.
PubMed=14597039; DOI=10.1016/S0002-9394(03)00541-5;
Warren J.F., Abbott R.L., Yoon M.K., Crawford J.B., Spencer W.H.,
Margolis T.P.;
"A new mutation (Leu569Arg) within exon 13 of the TGFBI (BIGH3) gene
causes lattice corneal dystrophy type I.";
Am. J. Ophthalmol. 136:872-878(2003).
[30]
VARIANT GRANULAR CORNEAL DYSTROPHY HIS-123.
PubMed=12782158; DOI=10.1016/S0021-5155(03)00019-4;
Ha N.T., Cung le X., Chau H.M., Thanh T.K., Fujiki K., Murakami A.,
Kanai A.;
"A novel mutation of the TGFBI gene found in a Vietnamese family with
atypical granular corneal dystrophy.";
Jpn. J. Ophthalmol. 47:246-248(2003).
[31]
VARIANTS CDL1 ASP-546 AND GLN-551.
PubMed=15531312; DOI=10.1016/j.ajo.2004.06.021;
Aldave A.J., Gutmark J.G., Yellore V.S., Affeldt J.A., Meallet M.A.,
Udar N., Rao N.A., Small K.W., Klintworth G.K.;
"Lattice corneal dystrophy associated with the Ala546Asp and Pro551Gln
missense changes in the TGFBI gene.";
Am. J. Ophthalmol. 138:772-781(2004).
[32]
VARIANTS CDL1 CYS-124 AND ARG-626, VARIANT CDRB LEU-124, VARIANT CDGG1
TRP-555, VARIANTS LATTICE CORNEAL DYSTROPHY ASP-539; VAL-594 AND
624-VAL-VAL-625 DEL, AND VARIANT PHE-269.
PubMed=15623763; DOI=10.1167/iovs.04-0440;
Chakravarthi S.V.V.K., Kannabiran C., Sridhar M.S., Vemuganti G.K.;
"TGFBI gene mutations causing lattice and granular corneal dystrophies
in Indian patients.";
Invest. Ophthalmol. Vis. Sci. 46:121-125(2005).
[33]
VARIANT CDL3A SER-540.
PubMed=15790870; DOI=10.1167/iovs.04-1319;
Stix B., Leber M., Bingemer P., Gross C., Rueschoff J., Faendrich M.,
Schorderet D.F., Vorwerk C.K., Zacharias M., Roessner A., Roecken C.;
"Hereditary lattice corneal dystrophy is associated with corneal
amyloid deposits enclosing C-terminal fragments of keratoepithelin.";
Invest. Ophthalmol. Vis. Sci. 46:1133-1139(2005).
[34]
VARIANT CDL1 ASP-505.
PubMed=15838722; DOI=10.1007/s10384-004-0167-7;
Tian X., Fujiki K., Wang W., Murakami A., Xie P., Kanai A., Liu Z.;
"Novel mutation (V505D) of the TGFBI gene found in a Chinese family
with lattice corneal dystrophy, type I.";
Jpn. J. Ophthalmol. 49:84-88(2005).
[35]
VARIANTS EBMD ARG-509 AND SER-666.
PubMed=16652336; DOI=10.1002/humu.20331;
Boutboul S., Black G.C.M., Moore J.E., Sinton J., Menasche M.,
Munier F.L., Laroche L., Abitbol M., Schorderet D.F.;
"A subset of patients with epithelial basement membrane corneal
dystrophy have mutations in TGFBI/BIGH3.";
Hum. Mutat. 27:553-557(2006).
[36]
VARIANT CDL1 ARG-572.
PubMed=17013691; DOI=10.1007/s10384-006-0357-6;
Atchaneeyasakul L.-O., Appukuttan B., Pingsuthiwong S.,
Yenchitsomanus P.-T., Trinavarat A., Srisawat C.;
"A novel H572R mutation in the transforming growth factor-beta-induced
gene in a Thai family with lattice corneal dystrophy type I.";
Jpn. J. Ophthalmol. 50:403-408(2006).
[37]
VARIANT CDL1 HIS-572 DEL.
PubMed=16541014;
Aldave A.J., Rayner S.A., Kim B.T., Prechanond A., Yellore V.S.;
"Unilateral lattice corneal dystrophy associated with the novel
His572del mutation in the TGFBI gene.";
Mol. Vis. 12:142-146(2006).
[38]
VARIANT GRANULAR CORNEAL DYSTROPHY ILE-113.
PubMed=16636649;
Zenteno J.C., Ramirez-Miranda A., Santacruz-Valdes C.,
Suarez-Sanchez R.;
"Expanding the mutational spectrum in TGFBI-linked corneal
dystrophies: identification of a novel and unusual mutation
(Val113Ile) in a family with granular dystrophy.";
Mol. Vis. 12:331-335(2006).
-!- FUNCTION: Plays a role in cell adhesion (PubMed:8024701). May play
a role in cell-collagen interactions (By similarity).
{ECO:0000250|UniProtKB:O11780, ECO:0000269|PubMed:8024701}.
-!- SUBUNIT: Binds to type I, II, and IV collagens.
{ECO:0000250|UniProtKB:O11780}.
-!- INTERACTION:
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-10236573, EBI-10175124;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18450759,
ECO:0000269|PubMed:26273833, ECO:0000269|PubMed:8024701}.
Secreted, extracellular space, extracellular matrix
{ECO:0000269|PubMed:8077289}. Note=May be associated both with
microfibrils and with the cell surface (PubMed:8077289).
{ECO:0000269|PubMed:8077289}.
-!- TISSUE SPECIFICITY: Highly expressed in the corneal epithelium
(PubMed:27609313, PubMed:8077289). Expressed in heart, placenta,
lung, liver, skeletal muscle, kidney and pancreas
(PubMed:8077289). {ECO:0000269|PubMed:27609313,
ECO:0000269|PubMed:8077289}.
-!- INDUCTION: By TGF-beta (PubMed:1388724, PubMed:8024701).
{ECO:0000269|PubMed:1388724, ECO:0000269|PubMed:8024701}.
-!- PTM: Gamma-carboxylation is controversial. Gamma-
carboxyglutamated; gamma-carboxyglutamate residues are formed by
vitamin K dependent carboxylation; these residues may be required
for binding to calcium (PubMed:18450759). According to a more
recent report, does not contain vitamin K-dependent gamma-
carboxyglutamate residues (PubMed:26273833).
{ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}.
-!- PTM: The EMI domain contains 2 expected intradomain disulfide
bridges (Cys-49-Cys85 and Cys-84-Cys-97) and one unusual
interdomain disulfide bridge to the second FAS1 domain (Cys-74-
Cys-339). This arrangement violates the predicted disulfide bridge
pattern of an EMI domain. {ECO:0000305|PubMed:27609313}.
-!- DISEASE: Corneal dystrophy, epithelial basement membrane (EBMD)
[MIM:121820]: A bilateral anterior corneal dystrophy characterized
by grayish epithelial fingerprint lines, geographic map-like
lines, and dots (or microcysts) on slit-lamp examination.
Pathologic studies show abnormal, redundant basement membrane and
intraepithelial lacunae filled with cellular debris.
{ECO:0000269|PubMed:16652336}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Corneal dystrophy, Groenouw type 1 (CDGG1) [MIM:121900]:
A rare form of stromal corneal dystrophy characterized by multiple
small deposits in the superficial central corneal stroma, and
progressive visual impairment. {ECO:0000269|PubMed:15623763}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Corneal dystrophy, lattice type 1 (CDL1) [MIM:122200]: A
form of lattice corneal dystrophy, a class of inherited stromal
amyloidoses characterized by pathognomonic branching lattice
figures in the cornea. CDL1 is characterized by progressive visual
impairment, and the presence of delicate, double-contoured,
interdigitating, elongated deposits that form a reticular pattern
in the corneal stroma. Systemic amyloidosis is absent. Recurrent
corneal ulceration sometimes occurs. {ECO:0000269|PubMed:10837380,
ECO:0000269|PubMed:11413411, ECO:0000269|PubMed:14597039,
ECO:0000269|PubMed:15531312, ECO:0000269|PubMed:15623763,
ECO:0000269|PubMed:15838722, ECO:0000269|PubMed:16541014,
ECO:0000269|PubMed:17013691, ECO:0000269|PubMed:9799082}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Corneal dystrophy, Thiel-Behnke type (CDTB) [MIM:602082]:
A bilateral disorder of the cornea characterized by progressive
honeycomb-like, subepithelial corneal opacities with recurrent
erosions. Note=The disease is caused by mutations affecting the
gene represented in this entry.
-!- DISEASE: Corneal dystrophy, Reis-Bucklers type (CDRB)
[MIM:608470]: A bilateral disorder of the cornea characterized by
intermittent attacks of ocular irritation, recurrent painful
corneal erosions starting in childhood, corneal opacities in a
geographic pattern at the level of the Bowman layer, and a
progressive decrease of visual acuity. The lesions are primarily
in Bowman membrane with secondary involvement of the epithelium
and superficial part of the stroma. Bowman membrane is almost
completely replaced by pathologic materials including disoriented
collagen fibrils. {ECO:0000269|PubMed:10660331,
ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:9780098}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Corneal dystrophy, lattice type 3A (CDL3A) [MIM:608471]:
A form of lattice corneal dystrophy, a class of inherited stromal
amyloidoses characterized by pathognomonic branching lattice
figures in the cornea. CDL3A is characterized by decreased visual
acuity, and the presence of thick, ropy branching lattice lines
and accumulations of amyloid deposits in the corneal stroma.
Systemic amyloidosis is absent. CDL3A clinically resembles to
lattice corneal dystrophy type 3, but differs in that its age of
onset is 70 to 90 years. It has an autosomal dominant inheritance
pattern. {ECO:0000269|PubMed:15790870,
ECO:0000269|PubMed:9497262}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Corneal dystrophy, Avellino type (CDA) [MIM:607541]: A
corneal disease resulting in reduced visual acuity and
characterized by gray, crumb-like granular deposits in the
anterior third of the stroma in each corneal button. Fusiform
amyloid deposits, histochemically and morphologically identical to
those of lattice corneal dystrophy, are found in the deeper
stroma. Additional features include recurrent corneal erosions,
and glare and decreased night vision. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tgfbi/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TGFBIID42539ch5q31.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M77349; AAA61163.1; -; mRNA.
EMBL; AF035626; AAB88695.1; -; Genomic_DNA.
EMBL; AF035627; AAB88698.1; -; Genomic_DNA.
EMBL; AF035628; AAB88696.1; -; Genomic_DNA.
EMBL; AF035629; AAB88697.1; -; Genomic_DNA.
EMBL; AY149344; AAN10294.1; -; Genomic_DNA.
EMBL; BT009820; AAP88822.1; -; mRNA.
EMBL; AC004503; AAC08449.1; -; Genomic_DNA.
EMBL; AC005219; AAC24944.1; -; Genomic_DNA.
EMBL; CH471062; EAW62199.1; -; Genomic_DNA.
EMBL; CH471062; EAW62200.1; -; Genomic_DNA.
EMBL; BC000097; AAH00097.1; -; mRNA.
EMBL; BC004972; AAH04972.1; -; mRNA.
CCDS; CCDS47266.1; -.
PIR; I52996; I52996.
RefSeq; NP_000349.1; NM_000358.2.
UniGene; Hs.369397; -.
PDB; 1X3B; NMR; -; A=502-634.
PDB; 2LTB; NMR; -; A=502-634.
PDB; 2LTC; NMR; -; A=502-634.
PDB; 2VXP; X-ray; 2.50 A; A/B=502-633.
PDB; 5NV6; X-ray; 2.93 A; A/B=1-683.
PDBsum; 1X3B; -.
PDBsum; 2LTB; -.
PDBsum; 2LTC; -.
PDBsum; 2VXP; -.
PDBsum; 5NV6; -.
ProteinModelPortal; Q15582; -.
SMR; Q15582; -.
BioGrid; 112903; 2.
CORUM; Q15582; -.
IntAct; Q15582; 4.
MINT; MINT-122359; -.
STRING; 9606.ENSP00000416330; -.
iPTMnet; Q15582; -.
PhosphoSitePlus; Q15582; -.
BioMuta; TGFBI; -.
DMDM; 2498193; -.
EPD; Q15582; -.
MaxQB; Q15582; -.
PaxDb; Q15582; -.
PeptideAtlas; Q15582; -.
PRIDE; Q15582; -.
DNASU; 7045; -.
Ensembl; ENST00000442011; ENSP00000416330; ENSG00000120708.
GeneID; 7045; -.
KEGG; hsa:7045; -.
UCSC; uc003lbf.5; human.
CTD; 7045; -.
DisGeNET; 7045; -.
EuPathDB; HostDB:ENSG00000120708.16; -.
GeneCards; TGFBI; -.
HGNC; HGNC:11771; TGFBI.
HPA; HPA008612; -.
HPA; HPA017019; -.
MalaCards; TGFBI; -.
MIM; 121820; phenotype.
MIM; 121900; phenotype.
MIM; 122200; phenotype.
MIM; 601692; gene.
MIM; 602082; phenotype.
MIM; 607541; phenotype.
MIM; 608470; phenotype.
MIM; 608471; phenotype.
neXtProt; NX_Q15582; -.
OpenTargets; ENSG00000120708; -.
Orphanet; 98962; Granular corneal dystrophy type I.
Orphanet; 98963; Granular corneal dystrophy type II.
Orphanet; 98964; Lattice corneal dystrophy type I.
Orphanet; 98956; Microcystic corneal dystrophy.
Orphanet; 98961; Reis-Bucklers corneal dystrophy.
Orphanet; 98960; Thiel-Behnke corneal dystrophy.
PharmGKB; PA36484; -.
eggNOG; KOG1437; Eukaryota.
eggNOG; COG2335; LUCA.
GeneTree; ENSGT00530000063860; -.
HOVERGEN; HBG000715; -.
InParanoid; Q15582; -.
KO; K19519; -.
OMA; KHGMALT; -.
OrthoDB; EOG091G020T; -.
PhylomeDB; Q15582; -.
TreeFam; TF316269; -.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; Q15582; -.
ChiTaRS; TGFBI; human.
EvolutionaryTrace; Q15582; -.
GeneWiki; TGFBI; -.
GenomeRNAi; 7045; -.
PRO; PR:Q15582; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000120708; -.
CleanEx; HS_TGFBI; -.
ExpressionAtlas; Q15582; baseline and differential.
Genevisible; Q15582; HS.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
GO; GO:0005518; F:collagen binding; IPI:BHF-UCL.
GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; TAS:ProtInc.
GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
GO; GO:0007162; P:negative regulation of cell adhesion; TAS:ProtInc.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
Gene3D; 2.30.180.10; -; 4.
InterPro; IPR011489; EMI_domain.
InterPro; IPR036378; FAS1_dom_sf.
InterPro; IPR000782; FAS1_domain.
InterPro; IPR032954; TGFBI.
InterPro; IPR016666; TGFBI/POSTN.
PANTHER; PTHR10900:SF82; PTHR10900:SF82; 1.
Pfam; PF02469; Fasciclin; 4.
PIRSF; PIRSF016553; BIGH3_OSF2; 1.
SMART; SM00554; FAS1; 4.
SUPFAM; SSF82153; SSF82153; 4.
PROSITE; PS51041; EMI; 1.
PROSITE; PS50213; FAS1; 4.
1: Evidence at protein level;
3D-structure; Amyloid; Amyloidosis; Cell adhesion; Complete proteome;
Corneal dystrophy; Direct protein sequencing; Disease mutation;
Disulfide bond; Extracellular matrix; Gamma-carboxyglutamic acid;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Sensory transduction; Signal; Vision.
SIGNAL 1 23 {ECO:0000269|PubMed:8024701}.
CHAIN 24 683 Transforming growth factor-beta-induced
protein ig-h3.
/FTId=PRO_0000008769.
DOMAIN 45 99 EMI. {ECO:0000255|PROSITE-
ProRule:PRU00384}.
DOMAIN 103 236 FAS1 1. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 240 371 FAS1 2. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 375 498 FAS1 3. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 502 632 FAS1 4. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
MOTIF 642 644 Cell attachment site. {ECO:0000255}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 65 65 S-cysteinyl cysteine.
{ECO:0000269|PubMed:27609313}.
DISULFID 49 85 {ECO:0000269|PubMed:27609313}.
DISULFID 74 339 {ECO:0000269|PubMed:27609313}.
DISULFID 84 97 {ECO:0000269|PubMed:27609313}.
DISULFID 214 317 {ECO:0000269|PubMed:27609313}.
DISULFID 473 478 {ECO:0000269|PubMed:27609313}.
VARIANT 113 113 V -> I (in granular corneal dystrophy;
unclassified form; with centrifuge
pattern of opacities; dbSNP:rs757933370).
{ECO:0000269|PubMed:16636649}.
/FTId=VAR_031531.
VARIANT 123 123 D -> H (in granular corneal dystrophy;
unclassified form; Hanoi;
dbSNP:rs541270955).
{ECO:0000269|PubMed:12782158}.
/FTId=VAR_031532.
VARIANT 124 124 R -> C (in CDL1; cysteinylated; no effect
on the disulfide bond pattern;
dbSNP:rs121909210).
{ECO:0000269|PubMed:11024425,
ECO:0000269|PubMed:11297504,
ECO:0000269|PubMed:11923233,
ECO:0000269|PubMed:15623763,
ECO:0000269|PubMed:27609313,
ECO:0000269|PubMed:9054935,
ECO:0000269|PubMed:9463327}.
/FTId=VAR_077904.
VARIANT 124 124 R -> H (in CDA; most common mutation in
Japanese; dbSNP:rs121909211).
{ECO:0000269|PubMed:10425035,
ECO:0000269|PubMed:11024425,
ECO:0000269|PubMed:11297504,
ECO:0000269|PubMed:11923233,
ECO:0000269|PubMed:9054935,
ECO:0000269|PubMed:9463327}.
/FTId=VAR_005077.
VARIANT 124 124 R -> L (in CDRB; dbSNP:rs121909211).
{ECO:0000269|PubMed:10865320,
ECO:0000269|PubMed:11024425,
ECO:0000269|PubMed:11297504,
ECO:0000269|PubMed:15623763,
ECO:0000269|PubMed:9780098}.
/FTId=VAR_005078.
VARIANT 124 124 R -> S (in CDGG1; late-onset; mild ocular
irritation and reduction in visual
acuity; dbSNP:rs121909210).
{ECO:0000269|PubMed:10425035,
ECO:0000269|PubMed:11923233}.
/FTId=VAR_012444.
VARIANT 125 126 Missing (associated with Leu-124 in
atypical granular dystrophy; French
granular variant).
{ECO:0000269|PubMed:10865320,
ECO:0000269|PubMed:11297504}.
/FTId=VAR_012445.
VARIANT 200 200 I -> F (in dbSNP:rs45455404).
{ECO:0000269|Ref.3}.
/FTId=VAR_014335.
VARIANT 269 269 L -> F (in dbSNP:rs199852470).
{ECO:0000269|PubMed:15623763}.
/FTId=VAR_031533.
VARIANT 496 496 R -> G (in dbSNP:rs10057190).
/FTId=VAR_031534.
VARIANT 501 501 P -> T (in CDL3A; dbSNP:rs121909212).
{ECO:0000269|PubMed:11024425,
ECO:0000269|PubMed:9497262}.
/FTId=VAR_005079.
VARIANT 505 505 V -> D (in CDL1).
{ECO:0000269|PubMed:15838722}.
/FTId=VAR_031535.
VARIANT 509 509 L -> R (in EBMD; dbSNP:rs121909216).
{ECO:0000269|PubMed:16652336}.
/FTId=VAR_031536.
VARIANT 518 518 L -> P (in CDL1).
{ECO:0000269|PubMed:10837380}.
/FTId=VAR_012446.
VARIANT 518 518 L -> R (in CDL1; severe phenotype;
delayed age of onset).
{ECO:0000269|PubMed:11923233}.
/FTId=VAR_018484.
VARIANT 527 527 L -> R (in CDL1; late-onset; found also
in sporadic cases).
{ECO:0000269|PubMed:11024425,
ECO:0000269|PubMed:11413411,
ECO:0000269|PubMed:9799082}.
/FTId=VAR_005080.
VARIANT 538 538 T -> R (in CDL1; delayed age of onset).
{ECO:0000269|PubMed:11923233}.
/FTId=VAR_018485.
VARIANT 539 539 V -> D (in lattice corneal dystrophy;
unclassified form).
{ECO:0000269|PubMed:15623763}.
/FTId=VAR_031537.
VARIANT 540 540 F -> S (in CDL3A; dbSNP:rs121909214).
{ECO:0000269|PubMed:15790870}.
/FTId=VAR_031538.
VARIANT 540 540 Missing (in CDRB).
{ECO:0000269|PubMed:10660331,
ECO:0000269|PubMed:11923233}.
/FTId=VAR_005081.
VARIANT 544 544 N -> S (found in lattice corneal
dystrophy; unclassified form; late-onset;
dbSNP:rs777288957).
{ECO:0000269|PubMed:11024425}.
/FTId=VAR_012447.
VARIANT 546 546 A -> D (in CDL1; associated with Q-551;
dbSNP:rs267607109).
{ECO:0000269|PubMed:15531312}.
/FTId=VAR_031539.
VARIANT 546 546 A -> T (in CDL3A).
{ECO:0000269|PubMed:11297504}.
/FTId=VAR_012448.
VARIANT 551 551 P -> Q (in CDL1; associated with D-546;
dbSNP:rs267607110).
{ECO:0000269|PubMed:15531312}.
/FTId=VAR_031540.
VARIANT 555 555 R -> Q (in CDTB; originally thought to
cause CDRB; dbSNP:rs121909209).
{ECO:0000269|PubMed:11024425,
ECO:0000269|PubMed:11297504,
ECO:0000269|PubMed:9054935,
ECO:0000269|PubMed:9463327}.
/FTId=VAR_005082.
VARIANT 555 555 R -> W (in CDGG1; common mutation in
Europe and United States; rare in Japan;
dbSNP:rs121909208).
{ECO:0000269|PubMed:10425035,
ECO:0000269|PubMed:11024425,
ECO:0000269|PubMed:11297504,
ECO:0000269|PubMed:11923233,
ECO:0000269|PubMed:15623763,
ECO:0000269|PubMed:9054935,
ECO:0000269|PubMed:9463327}.
/FTId=VAR_005083.
VARIANT 569 569 L -> R (in CDL1).
{ECO:0000269|PubMed:14597039}.
/FTId=VAR_031541.
VARIANT 572 572 H -> R (in CDL1; late-onset).
{ECO:0000269|PubMed:17013691}.
/FTId=VAR_031543.
VARIANT 572 572 Missing (in CDL1; late-onset and
unilateral phenotype).
{ECO:0000269|PubMed:16541014}.
/FTId=VAR_031542.
VARIANT 594 594 G -> V (in lattice corneal dystrophy;
unclassified form).
{ECO:0000269|PubMed:15623763}.
/FTId=VAR_031544.
VARIANT 622 622 N -> H (in asymmetric lattice corneal
dystrophy).
{ECO:0000269|PubMed:10328397}.
/FTId=VAR_012449.
VARIANT 622 622 N -> K (in CDL3A).
{ECO:0000269|PubMed:11923233}.
/FTId=VAR_018486.
VARIANT 623 623 G -> D (in CDL1; delayed age of onset;
dbSNP:rs121909215).
{ECO:0000269|PubMed:11923233}.
/FTId=VAR_018487.
VARIANT 624 625 Missing (in lattice corneal dystrophy;
unclassified form).
{ECO:0000269|PubMed:15623763}.
/FTId=VAR_031545.
VARIANT 626 626 H -> P (in CDL1).
{ECO:0000269|PubMed:11923233}.
/FTId=VAR_018488.
VARIANT 626 626 H -> R (in CDL1; delayed age of onset).
{ECO:0000269|PubMed:10328397,
ECO:0000269|PubMed:11297504,
ECO:0000269|PubMed:11923233,
ECO:0000269|PubMed:15623763}.
/FTId=VAR_012450.
VARIANT 631 631 V -> D (found in lattice corneal
dystrophy; unclassified form).
{ECO:0000269|PubMed:11923233}.
/FTId=VAR_018489.
VARIANT 666 666 R -> S (in EBMD; unknown pathological
significance; dbSNP:rs121909217).
{ECO:0000269|PubMed:16652336}.
/FTId=VAR_031546.
STRAND 48 54 {ECO:0000244|PDB:5NV6}.
STRAND 60 62 {ECO:0000244|PDB:5NV6}.
STRAND 71 73 {ECO:0000244|PDB:5NV6}.
STRAND 76 84 {ECO:0000244|PDB:5NV6}.
STRAND 94 96 {ECO:0000244|PDB:5NV6}.
HELIX 106 113 {ECO:0000244|PDB:5NV6}.
HELIX 116 124 {ECO:0000244|PDB:5NV6}.
HELIX 128 133 {ECO:0000244|PDB:5NV6}.
STRAND 134 136 {ECO:0000244|PDB:5NV6}.
STRAND 138 143 {ECO:0000244|PDB:5NV6}.
HELIX 145 149 {ECO:0000244|PDB:5NV6}.
HELIX 153 161 {ECO:0000244|PDB:5NV6}.
TURN 163 165 {ECO:0000244|PDB:5NV6}.
HELIX 166 173 {ECO:0000244|PDB:5NV6}.
STRAND 175 178 {ECO:0000244|PDB:5NV6}.
HELIX 182 185 {ECO:0000244|PDB:5NV6}.
TURN 186 188 {ECO:0000244|PDB:5NV6}.
STRAND 202 204 {ECO:0000244|PDB:5NV6}.
STRAND 210 212 {ECO:0000244|PDB:5NV6}.
STRAND 215 223 {ECO:0000244|PDB:5NV6}.
STRAND 225 234 {ECO:0000244|PDB:5NV6}.
HELIX 243 249 {ECO:0000244|PDB:5NV6}.
HELIX 251 253 {ECO:0000244|PDB:5NV6}.
HELIX 254 263 {ECO:0000244|PDB:5NV6}.
HELIX 266 270 {ECO:0000244|PDB:5NV6}.
STRAND 275 280 {ECO:0000244|PDB:5NV6}.
HELIX 282 287 {ECO:0000244|PDB:5NV6}.
HELIX 290 298 {ECO:0000244|PDB:5NV6}.
HELIX 300 308 {ECO:0000244|PDB:5NV6}.
STRAND 310 314 {ECO:0000244|PDB:5NV6}.
HELIX 318 320 {ECO:0000244|PDB:5NV6}.
STRAND 325 332 {ECO:0000244|PDB:5NV6}.
STRAND 334 340 {ECO:0000244|PDB:5NV6}.
STRAND 343 346 {ECO:0000244|PDB:5NV6}.
STRAND 352 359 {ECO:0000244|PDB:5NV6}.
STRAND 362 369 {ECO:0000244|PDB:5NV6}.
TURN 374 376 {ECO:0000244|PDB:5NV6}.
TURN 379 385 {ECO:0000244|PDB:5NV6}.
HELIX 389 397 {ECO:0000244|PDB:5NV6}.
HELIX 402 405 {ECO:0000244|PDB:5NV6}.
STRAND 410 415 {ECO:0000244|PDB:5NV6}.
HELIX 417 420 {ECO:0000244|PDB:5NV6}.
HELIX 429 436 {ECO:0000244|PDB:5NV6}.
STRAND 439 442 {ECO:0000244|PDB:5NV6}.
HELIX 446 448 {ECO:0000244|PDB:5NV6}.
STRAND 454 460 {ECO:0000244|PDB:5NV6}.
STRAND 462 467 {ECO:0000244|PDB:5NV6}.
STRAND 472 474 {ECO:0000244|PDB:5NV6}.
STRAND 477 479 {ECO:0000244|PDB:5NV6}.
STRAND 490 496 {ECO:0000244|PDB:5NV6}.
HELIX 505 509 {ECO:0000244|PDB:2VXP}.
HELIX 513 515 {ECO:0000244|PDB:5NV6}.
HELIX 516 525 {ECO:0000244|PDB:2VXP}.
HELIX 528 532 {ECO:0000244|PDB:2VXP}.
STRAND 533 535 {ECO:0000244|PDB:1X3B}.
STRAND 537 542 {ECO:0000244|PDB:2VXP}.
HELIX 544 549 {ECO:0000244|PDB:2VXP}.
HELIX 552 559 {ECO:0000244|PDB:2VXP}.
HELIX 562 571 {ECO:0000244|PDB:2VXP}.
STRAND 572 576 {ECO:0000244|PDB:2VXP}.
HELIX 580 582 {ECO:0000244|PDB:5NV6}.
STRAND 587 591 {ECO:0000244|PDB:2VXP}.
STRAND 594 602 {ECO:0000244|PDB:2VXP}.
STRAND 605 610 {ECO:0000244|PDB:2VXP}.
STRAND 614 620 {ECO:0000244|PDB:2VXP}.
STRAND 623 630 {ECO:0000244|PDB:2VXP}.
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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