GenomeNet

Database: UniProt
Entry: Q14767
LinkDB: Q14767
Original site: Q14767 
ID   LTBP2_HUMAN             Reviewed;        1821 AA.
AC   Q14767; Q99907; Q9NS51;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   29-OCT-2014, entry version 137.
DE   RecName: Full=Latent-transforming growth factor beta-binding protein 2;
DE            Short=LTBP-2;
DE   Flags: Precursor;
GN   Name=LTBP2; Synonyms=C14orf141, LTBP3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Foreskin fibroblast;
RX   PubMed=7798248;
RA   Moren A., Olofsson A., Stenman G., Sahlin P., Kanzaki T.,
RA   Claesson-Welsh L., ten Dijke P., Miyazono K., Heldin C.;
RT   "Identification and characterization of LTBP-2, a novel latent
RT   transforming growth factor-beta-binding protein.";
RL   J. Biol. Chem. 269:32469-32478(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8697098; DOI=10.1016/1357-2725(95)00167-0;
RA   Bashir M.M., Han M.-D., Abrams W.R., Tucker T., Ma R.-I., Gibson M.,
RA   Ritty T., Mecham R., Rosenbloom J.;
RT   "Analysis of the human gene encoding latent transforming growth
RT   factor-beta-binding protein-2.";
RL   Int. J. Biochem. Cell Biol. 28:531-542(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [4]
RP   LACK OF INTERACTION WITH TGFB1, AND MUTAGENESIS OF 1449-ASP-LEU-1450.
RX   PubMed=10930463; DOI=10.1091/mbc.11.8.2691;
RA   Saharinen J., Keski-Oja J.;
RT   "Specific sequence motif of 8-Cys repeats of TGF-beta binding
RT   proteins, LTBPs, creates a hydrophobic interaction surface for binding
RT   of small latent TGF-beta.";
RL   Mol. Biol. Cell 11:2691-2704(2000).
RN   [5]
RP   REVIEW.
RX   PubMed=10743502; DOI=10.1016/S1359-6101(99)00010-6;
RA   Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.;
RT   "Latent transforming growth factor-beta binding proteins (LTBPs) --
RT   structural extracellular matrix proteins for targeting TGF-beta
RT   action.";
RL   Cytokine Growth Factor Rev. 10:99-117(1999).
RN   [6]
RP   REVIEW.
RX   PubMed=11104663; DOI=10.1042/0264-6021:3520601;
RA   Oklu R., Hesketh R.;
RT   "The latent transforming growth factor beta binding protein (LTBP)
RT   family.";
RL   Biochem. J. 352:601-610(2000).
RN   [7]
RP   INVOLVEMENT IN GLC3D.
RX   PubMed=19361779; DOI=10.1016/j.ajhg.2009.03.017;
RA   Ali M., McKibbin M., Booth A., Parry D.A., Jain P., Riazuddin S.A.,
RA   Hejtmancik J.F., Khan S.N., Firasat S., Shires M., Gilmour D.F.,
RA   Towns K., Murphy A.L., Azmanov D., Tournev I., Cherninkova S.,
RA   Jafri H., Raashid Y., Toomes C., Craig J., Mackey D.A.,
RA   Kalaydjieva L., Riazuddin S., Inglehearn C.F.;
RT   "Null mutations in LTBP2 cause primary congenital glaucoma.";
RL   Am. J. Hum. Genet. 84:664-671(2009).
RN   [8]
RP   INVOLVEMENT IN MSPKA.
RX   PubMed=20617341; DOI=10.1007/s00439-010-0858-8;
RA   Kumar A., Duvvari M.R., Prabhakaran V.C., Shetty J.S., Murthy G.J.,
RA   Blanton S.H.;
RT   "A homozygous mutation in LTBP2 causes isolated microspherophakia.";
RL   Hum. Genet. 128:365-371(2010).
RN   [9]
RP   HEPARIN-BINDING REGIONS, AND INTERACTION WITH SDC4.
RX   PubMed=20382221; DOI=10.1016/j.matbio.2010.03.005;
RA   Parsi M.K., Adams J.R., Whitelock J., Gibson M.A.;
RT   "LTBP-2 has multiple heparin/heparan sulfate binding sites.";
RL   Matrix Biol. 29:393-401(2010).
RN   [10]
RP   VARIANT WMS3 MET-1177.
RX   PubMed=22539340; DOI=10.1002/humu.22105;
RA   Haji-Seyed-Javadi R., Jelodari-Mamaghani S., Paylakhi S.H.,
RA   Yazdani S., Nilforushan N., Fan J.B., Klotzle B., Mahmoudi M.J.,
RA   Ebrahimian M.J., Chelich N., Taghiabadi E., Kamyab K., Boileau C.,
RA   Paisan-Ruiz C., Ronaghi M., Elahi E.;
RT   "LTBP2 mutations cause Weill-Marchesani and Weill-Marchesani-like
RT   syndrome and affect disruptions in the extracellular matrix.";
RL   Hum. Mutat. 33:1182-1187(2012).
CC   -!- FUNCTION: May play an integral structural role in elastic-fiber
CC       architectural organization and/or assembly.
CC   -!- SUBUNIT: Forms part of the large latent transforming growth factor
CC       beta precursor complex; removal is essential for activation of
CC       complex. Interacts with SDC4. {ECO:0000269|PubMed:20382221}.
CC   -!- INTERACTION:
CC       Q9UBX5:FBLN5; NbExp=2; IntAct=EBI-1546118, EBI-947897;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Localized in
CC       nuchal ligament and aorta to the fibrillin-containing,
CC       microfibrillar component of elastic fibers. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in lung, weakly expressed in heart,
CC       placenta, liver and skeletal muscle.
CC   -!- DOMAIN: Associates covalently with small latent TGF-beta complex
CC       via Repeat B and Repeat C. {ECO:0000250}.
CC   -!- PTM: Contains hydroxylated asparagine residues. {ECO:0000250}.
CC   -!- DISEASE: Glaucoma 3, primary congenital, D (GLC3D) [MIM:613086]:
CC       An autosomal recessive form of primary congenital glaucoma (PCG).
CC       PCG is characterized by marked increase of intraocular pressure at
CC       birth or early childhood, large ocular globes (buphthalmos) and
CC       corneal edema. It results from developmental defects of the
CC       trabecular meshwork and anterior chamber angle of the eye that
CC       prevent adequate drainage of aqueous humor.
CC       {ECO:0000269|PubMed:19361779}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Microspherophakia and/or megalocornea, with ectopia
CC       lentis and with or without secondary glaucoma (MSPKA)
CC       [MIM:251750]: A rare disease characterized by smaller and more
CC       spherical lenses than normal bilaterally, an increased
CC       anteroposterior thickness of the lens, and highly myopic eyes.
CC       Lens dislocation or subluxation may occur, leading to defective
CC       accommodation. {ECO:0000269|PubMed:20617341}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Weill-Marchesani syndrome 3 (WMS3) [MIM:614819]: A rare
CC       connective tissue disorder characterized by short stature,
CC       brachydactyly, joint stiffness, and eye abnormalities including
CC       microspherophakia, ectopia lentis, severe myopia and glaucoma.
CC       {ECO:0000269|PubMed:22539340}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 20 EGF-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 4 TB (TGF-beta binding) domains.
CC       {ECO:0000305}.
CC   -!- CAUTION: PubMed:7798248 reported that a complex is formed with
CC       TGFB1. PubMed:10930463 has shown that there is no association with
CC       TGFB1. {ECO:0000305}.
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DR   EMBL; Z37976; CAA86030.1; -; mRNA.
DR   EMBL; S82451; AAB37459.1; -; mRNA.
DR   EMBL; AC013451; AAF87081.1; -; Genomic_DNA.
DR   CCDS; CCDS9831.1; -.
DR   PIR; A55494; A55494.
DR   RefSeq; NP_000419.1; NM_000428.2.
DR   UniGene; Hs.512776; -.
DR   UniGene; Hs.597522; -.
DR   ProteinModelPortal; Q14767; -.
DR   SMR; Q14767; 171-221, 403-428, 552-736, 856-1624, 1735-1819.
DR   IntAct; Q14767; 3.
DR   MINT; MINT-2806977; -.
DR   STRING; 9606.ENSP00000261978; -.
DR   PhosphoSite; Q14767; -.
DR   DMDM; 296439311; -.
DR   PaxDb; Q14767; -.
DR   PRIDE; Q14767; -.
DR   Ensembl; ENST00000261978; ENSP00000261978; ENSG00000119681.
DR   GeneID; 4053; -.
DR   KEGG; hsa:4053; -.
DR   UCSC; uc001xqa.3; human.
DR   CTD; 4053; -.
DR   GeneCards; GC14M074965; -.
DR   GeneReviews; LTBP2; -.
DR   HGNC; HGNC:6715; LTBP2.
DR   HPA; HPA003415; -.
DR   MIM; 251750; phenotype.
DR   MIM; 602091; gene.
DR   MIM; 613086; phenotype.
DR   MIM; 614819; phenotype.
DR   neXtProt; NX_Q14767; -.
DR   Orphanet; 98976; Congenital glaucoma.
DR   Orphanet; 238763; Glaucoma secondary to spherophakia/ectopia lentis and megalocornea.
DR   Orphanet; 3449; Weill-Marchesani syndrome.
DR   PharmGKB; PA164741922; -.
DR   eggNOG; NOG318792; -.
DR   GeneTree; ENSGT00760000118806; -.
DR   HOGENOM; HOG000293153; -.
DR   HOVERGEN; HBG052370; -.
DR   InParanoid; Q14767; -.
DR   KO; K08023; -.
DR   OMA; YFCQIPC; -.
DR   OrthoDB; EOG7FR7FP; -.
DR   PhylomeDB; Q14767; -.
DR   Reactome; REACT_150331; Molecules associated with elastic fibres.
DR   ChiTaRS; LTBP2; human.
DR   GeneWiki; LTBP2; -.
DR   GenomeRNAi; 4053; -.
DR   NextBio; 15880; -.
DR   PRO; PR:Q14767; -.
DR   Bgee; Q14767; -.
DR   CleanEx; HS_LTBP2; -.
DR   CleanEx; HS_LTBP3; -.
DR   ExpressionAtlas; Q14767; baseline and differential.
DR   Genevestigator; Q14767; -.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:ProtInc.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0009306; P:protein secretion; TAS:ProtInc.
DR   GO; GO:0006605; P:protein targeting; TAS:ProtInc.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc.
DR   Gene3D; 3.90.290.10; -; 5.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_N_dom.
DR   InterPro; IPR017878; TB_dom.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 17.
DR   Pfam; PF00683; TB; 4.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 16.
DR   SUPFAM; SSF57184; SSF57184; 5.
DR   SUPFAM; SSF57581; SSF57581; 5.
DR   PROSITE; PS00010; ASX_HYDROXYL; 13.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 11.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS01187; EGF_CA; 16.
DR   PROSITE; PS51364; TB; 4.
PE   1: Evidence at protein level;
KW   Complete proteome; Disease mutation; Disulfide bond; Dwarfism;
KW   EGF-like domain; Glaucoma; Glycoprotein; Growth factor binding;
KW   Heparin-binding; Hydroxylation; Polymorphism; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36   1821       Latent-transforming growth factor beta-
FT                                binding protein 2.
FT                                /FTId=PRO_0000007643.
FT   DOMAIN      187    219       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      396    428       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      552    604       TB 1.
FT   DOMAIN      622    662       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      672    724       TB 2.
FT   DOMAIN      844    886       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      887    929       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      930    969       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      970   1009       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1010   1050       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1051   1092       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1093   1134       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1135   1175       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1176   1217       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1218   1258       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1259   1302       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1303   1344       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1345   1387       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1411   1463       TB 3.
FT   DOMAIN     1485   1527       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1528   1567       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1584   1636       TB 4.
FT   DOMAIN     1733   1773       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1774   1818       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION       94    115       Heparin-binding.
FT   REGION      232    249       Heparin-binding.
FT   REGION      344    354       Heparin-binding.
FT   MOTIF       375    377       Cell attachment site. {ECO:0000255}.
FT   COMPBIAS    856   1372       Cys-rich.
FT   CARBOHYD    181    181       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    343    343       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    616    616       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    811    811       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1170   1170       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1309   1309       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1430   1430       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1568   1568       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    191    201       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    195    207       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    209    218       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    400    410       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    404    416       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    418    427       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    626    637       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    632    646       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    648    661       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    848    861       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    856    870       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    872    885       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    891    902       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    896    911       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    913    928       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    934    945       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    940    954       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    956    968       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    974    985       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    980    994       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    997   1008       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1014   1025       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1020   1034       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1036   1049       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1055   1066       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1061   1075       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1078   1091       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1097   1108       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1103   1117       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1120   1133       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1139   1151       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1146   1160       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1162   1174       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1180   1192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1186   1201       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1203   1216       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1222   1233       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1228   1242       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1244   1257       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1263   1276       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1271   1285       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1289   1301       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1307   1319       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1313   1328       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1330   1343       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1349   1361       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1356   1370       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1372   1386       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1489   1502       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1497   1511       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1513   1526       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1532   1542       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1537   1551       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1553   1566       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1737   1748       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1743   1757       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1759   1772       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1778   1793       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1788   1802       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1804   1817       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VARIANT      37     37       R -> M (in dbSNP:rs934996).
FT                                /FTId=VAR_059270.
FT   VARIANT     319    319       P -> Q (in dbSNP:rs2304707).
FT                                /FTId=VAR_055752.
FT   VARIANT     591    591       P -> S (in dbSNP:rs2196862).
FT                                /FTId=VAR_060337.
FT   VARIANT    1177   1177       V -> M (in WMS3).
FT                                {ECO:0000269|PubMed:22539340}.
FT                                /FTId=VAR_068647.
FT   MUTAGEN    1449   1450       DL->EIFP: Gain-of-function. Forms a
FT                                complex with TGFB1.
FT                                {ECO:0000269|PubMed:10930463}.
FT   CONFLICT    897    897       K -> Q (in Ref. 1; CAA86030).
FT                                {ECO:0000305}.
FT   CONFLICT   1443   1443       S -> T (in Ref. 1; CAA86030).
FT                                {ECO:0000305}.
FT   CONFLICT   1615   1615       E -> K (in Ref. 1; CAA86030).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1821 AA;  195052 MW;  3D6952B39885E1A6 CRC64;
     MRPRTKARSP GRALRNPWRG FLPLTLALFV GAGHAQRDPV GRYEPAGGDA NRLRRPGGSY
     PAAAAAKVYS LFREQDAPVA GLQPVERAQP GWGSPRRPTE AEARRPSRAQ QSRRVQPPAQ
     TRRSTPLGQQ QPAPRTRAAP ALPRLGTPQR SGAAPPTPPR GRLTGRNVCG GQCCPGWTTA
     NSTNHCIKPV CEPPCQNRGS CSRPQLCVCR SGFRGARCEE VIPDEEFDPQ NSRLAPRRWA
     ERSPNLRRSS AAGEGTLARA QPPAPQSPPA PQSPPAGTLS GLSQTHPSQQ HVGLSRTVRL
     HPTATASSQL SSNALPPGPG LEQRDGTQQA VPLEHPSSPW GLNLTEKIKK IKIVFTPTIC
     KQTCARGHCA NSCERGDTTT LYSQGGHGHD PKSGFRIYFC QIPCLNGGRC IGRDECWCPA
     NSTGKFCHLP IPQPDREPPG RGSRPRALLE APLKQSTFTL PLSNQLASVN PSLVKVHIHH
     PPEASVQIHQ VAQVRGGVEE ALVENSVETR PPPWLPASPG HSLWDSNNIP ARSGEPPRPL
     PPAAPRPRGL LGRCYLNTVN GQCANPLLEL TTQEDCCGSV GAFWGVTLCA PCPPRPASPV
     IENGQLECPQ GYKRLNLTHC QDINECLTLG LCKDAECVNT RGSYLCTCRP GLMLDPSRSR
     CVSDKAISML QGLCYRSLGP GTCTLPLAQR ITKQICCCSR VGKAWGSECE KCPLPGTEAF
     REICPAGHGY TYASSDIRLS MRKAEEEELA RPPREQGQRS SGALPGPAER QPLRVVTDTW
     LEAGTIPDKG DSQAGQVTTS VTHAPAWVTG NATTPPMPEQ GIAEIQEEQV TPSTDVLVTL
     STPGIDRCAA GATNVCGPGT CVNLPDGYRC VCSPGYQLHP SQAYCTDDNE CLRDPCKGKG
     RCINRVGSYS CFCYPGYTLA TSGATQECQD INECEQPGVC SGGQCTNTEG SYHCECDQGY
     IMVRKGHCQD INECRHPGTC PDGRCVNSPG SYTCLACEEG YRGQSGSCVD VNECLTPGVC
     AHGKCTNLEG SFRCSCEQGY EVTSDEKGCQ DVDECASRAS CPTGLCLNTE GSFACSACEN
     GYWVNEDGTA CEDLDECAFP GVCPSGVCTN TAGSFSCKDC DGGYRPSPLG DSCEDVDECE
     DPQSSCLGGE CKNTVGSYQC LCPQGFQLAN GTVCEDVNEC MGEEHCAPHG ECLNSHGSFF
     CLCAPGFVSA EGGTSCQDVD ECATTDPCVG GHCVNTEGSF NCLCETGFQP SPESGECVDI
     DECEDYGDPV CGTWKCENSP GSYRCVLGCQ PGFHMAPNGD CIDIDECAND TMCGSHGFCD
     NTDGSFRCLC DQGFEISPSG WDCVDVNECE LMLAVCGAAL CENVEGSFLC LCASDLEEYD
     AQEGHCRPRG AGGQSMSEAP TGDHAPAPTR MDCYSGQKGH APCSSVLGRN TTQAECCCTQ
     GASWGDACDL CPSEDSAEFS EICPSGKGYI PVEGAWTFGQ TMYTDADECV IFGPGLCPNG
     RCLNTVPGYV CLCNPGFHYD ASHKKCEDHD ECQDLACENG ECVNTEGSFH CFCSPPLTLD
     LSQQRCMNST SSTEDLPDHD IHMDICWKKV TNDVCSEPLR GHRTTYTECC CQDGEAWSQQ
     CALCPPRSSE VYAQLCNVAR IEAEREAGVH FRPGYEYGPG PDDLHYSIYG PDGAPFYNYL
     GPEDTVPEPA FPNTAGHSAD RTPILESPLQ PSELQPHYVA SHPEPPAGFE GLQAEECGIL
     NGCENGRCVR VREGYTCDCF EGFQLDAAHM ACVDVNECDD LNGPAVLCVH GYCENTEGSY
     RCHCSPGYVA EAGPPHCTAK E
//
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