ID LTBP3_HUMAN Reviewed; 1303 AA. AC Q9NS15; O15107; Q96HB9; Q9H7K2; Q9UFN4; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 4. DT 02-OCT-2024, entry version 196. DE RecName: Full=Latent-transforming growth factor beta-binding protein 3; DE Short=LTBP-3; DE Flags: Precursor; GN Name=LTBP3; 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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=12154076; DOI=10.1242/jcs.115.17.3457; RA Penttinen C., Saharinen J., Weikkolainen K., Hyytiainen M., Keski-Oja J.; RT "Secretion of human latent TGF-beta-binding protein-3 (LTBP-3) is dependent RT on co-expression of TGF-beta."; RL J. Cell Sci. 115:3457-3468(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Spleen; RA Ohara O., Nagase T., Kikuno R., Okumura K.; RT "The nucleotide sequence of a long cDNA clone isolated from human spleen."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 394-573. RC TISSUE=Liver; RX PubMed=9620332; DOI=10.1002/hep.510270619; RA Michel K., Roth S., Trautwein C., Gong W., Flemming P., Gressner A.M.; RT "Analysis of the expression pattern of the latent transforming growth RT factor beta binding protein isoforms in normal and diseased human liver RT reveals a new splice variant missing the proteinase-sensitive hinge RT region."; RL Hepatology 27:1592-1599(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 514-1303 (ISOFORM 2). RC TISSUE=Colon; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1303. RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP INTERACTION WITH TGFB1. 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 proteins, RT LTBPs, creates a hydrophobic interaction surface for binding of small RT latent TGF-beta."; RL Mol. Biol. Cell 11:2691-2704(2000). RN [7] 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 [8] RP REVIEW. RX PubMed=11104663; DOI=10.1042/bj3520601; 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 [9] RP SUBCELLULAR LOCATION. RX PubMed=16157329; DOI=10.1016/j.yexcr.2005.08.008; RA Koli K., Hyytieainen M., Ryynanen M.J., Keski-Oja J.; RT "Sequential deposition of latent TGF-beta binding proteins (LTBPs) during RT formation of the extracellular matrix in human lung fibroblasts."; RL Exp. Cell Res. 310:370-382(2005). RN [10] RP INTERACTION WITH EFEMP2. RX PubMed=27339457; DOI=10.1016/j.matbio.2016.06.003; RA Sasaki T., Hanisch F.G., Deutzmann R., Sakai L.Y., Sakuma T., Miyamoto T., RA Yamamoto T., Hannappel E., Chu M.L., Lanig H., von der Mark K.; RT "Functional consequence of fibulin-4 missense mutations associated with RT vascular and skeletal abnormalities and cutis laxa."; RL Matrix Biol. 56:132-149(2016). RN [11] RP INVOLVEMENT IN DASS. RX PubMed=19344874; DOI=10.1016/j.ajhg.2009.03.007; RA Noor A., Windpassinger C., Vitcu I., Orlic M., Rafiq M.A., Khalid M., RA Malik M.N., Ayub M., Alman B., Vincent J.B.; RT "Oligodontia is caused by mutation in LTBP3, the gene encoding latent TGF- RT beta binding protein 3."; RL Am. J. Hum. Genet. 84:519-523(2009). RN [12] RP INVOLVEMENT IN GPHYSD3, VARIANT GPHYSD3 CYS-696, AND CHARACTERIZATION OF RP VARIANT GPHYSD3 CYS-696. RX PubMed=27068007; DOI=10.1136/jmedgenet-2015-103647; RA McInerney-Leo A.M., Le Goff C., Leo P.J., Kenna T.J., Keith P., RA Harris J.E., Steer R., Bole-Feysot C., Nitschke P., Kielty C., Brown M.A., RA Zankl A., Duncan E.L., Cormier-Daire V.; RT "Mutations in LTBP3 cause acromicric dysplasia and geleophysic dysplasia."; RL J. Med. Genet. 53:457-464(2016). CC -!- FUNCTION: Key regulator of transforming growth factor beta (TGFB1, CC TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in CC a latent state during storage in extracellular space. Associates CC specifically via disulfide bonds with the Latency-associated peptide CC (LAP), which is the regulatory chain of TGF-beta, and regulates CC integrin-dependent activation of TGF-beta. CC {ECO:0000303|PubMed:10743502, ECO:0000303|PubMed:11104663}. CC -!- SUBUNIT: Forms part of the large latent transforming growth factor beta CC precursor complex; removal is essential for activation of complex. CC Interacts with EFEMP2 (PubMed:27339457). {ECO:0000269|PubMed:10930463, CC ECO:0000269|PubMed:27339457}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12154076}. Secreted, CC extracellular space, extracellular matrix CC {ECO:0000269|PubMed:16157329}. Note=Secretion occurs after coexpression CC with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 CC propeptide. {ECO:0000269|PubMed:12154076}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NS15-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NS15-2; Sequence=VSP_009241; CC -!- TISSUE SPECIFICITY: Isoform 2: Expressed prominently in heart, skeletal CC muscle, prostate, testis, small intestine and ovary (PubMed:12154076). CC Isoform 1: Strongly expressed in pancreas and liver (PubMed:12154076). CC {ECO:0000269|PubMed:12154076}. CC -!- PTM: Contains hydroxylated asparagine residues. CC {ECO:0000250|UniProtKB:Q14766}. CC -!- PTM: Two intrachain disulfide bonds from the TB3 domain are rearranged CC upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, CC anchoring it to the extracellular matrix. CC {ECO:0000250|UniProtKB:Q14766}. CC -!- DISEASE: Dental anomalies and short stature (DASS) [MIM:601216]: A CC disorder characterized by hypoplastic amelogenesis imperfecta, CC significant short stature, brachyolmia-like anomalies including CC platyspondyly with short pedicles, narrow intervertebral and CC interpedicular distances, rectangular-shaped vertebrae with posterior CC scalloping and herniation of the nuclei, and broad femoral necks. CC Dental anomalies include widely spaced, small, yellow teeth, CC oligodontia, and severely reduced to absent enamel. CC {ECO:0000269|PubMed:19344874}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Geleophysic dysplasia 3 (GPHYSD3) [MIM:617809]: A form of CC geleophysic dysplasia, a rare skeletal disease characterized by severe CC short stature, short hands and feet, and joint limitations. Radiologic CC features include delayed bone age, cone-shaped epiphyses, shortened CC long tubular bones, and ovoid vertebral bodies. Affected individuals CC have characteristic facial features including a 'happy' face with full CC cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin CC upper lip. Other distinctive features include skin thickening, CC progressive cardiac valvular thickening often leading to an early CC death, toe walking, tracheal stenosis, respiratory insufficiency, and CC lysosomal-like storage vacuoles in various tissues. GPHYSD3 inheritance CC is autosomal dominant. {ECO:0000269|PubMed:27068007}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15767.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF135960; AAF62352.3; -; mRNA. DR EMBL; AK024477; BAB15767.1; ALT_INIT; mRNA. DR EMBL; AF011407; AAB64201.1; -; mRNA. DR EMBL; BC008761; AAH08761.2; -; mRNA. DR EMBL; AL117551; CAB55988.1; -; mRNA. DR CCDS; CCDS44647.1; -. [Q9NS15-1] DR CCDS; CCDS8103.1; -. [Q9NS15-2] DR PIR; T17298; T17298. DR RefSeq; NP_001123616.1; NM_001130144.2. [Q9NS15-1] DR RefSeq; NP_001157738.1; NM_001164266.1. DR RefSeq; NP_066548.2; NM_021070.4. [Q9NS15-2] DR AlphaFoldDB; Q9NS15; -. DR BioGRID; 110232; 50. DR IntAct; Q9NS15; 20. DR MINT; Q9NS15; -. DR STRING; 9606.ENSP00000301873; -. DR GlyCosmos; Q9NS15; 9 sites, 2 glycans. DR GlyGen; Q9NS15; 23 sites, 4 O-linked glycans (17 sites). DR iPTMnet; Q9NS15; -. DR PhosphoSitePlus; Q9NS15; -. DR BioMuta; LTBP3; -. DR DMDM; 116242623; -. DR jPOST; Q9NS15; -. DR MassIVE; Q9NS15; -. DR PaxDb; 9606-ENSP00000301873; -. DR PeptideAtlas; Q9NS15; -. DR ProteomicsDB; 82461; -. [Q9NS15-1] DR ProteomicsDB; 82462; -. [Q9NS15-2] DR Antibodypedia; 70903; 13 antibodies from 10 providers. DR DNASU; 4054; -. DR Ensembl; ENST00000301873.11; ENSP00000301873.5; ENSG00000168056.18. [Q9NS15-1] DR Ensembl; ENST00000322147.8; ENSP00000326647.4; ENSG00000168056.18. [Q9NS15-2] DR GeneID; 4054; -. DR KEGG; hsa:4054; -. DR MANE-Select; ENST00000301873.11; ENSP00000301873.5; NM_001130144.3; NP_001123616.1. DR UCSC; uc001oei.4; human. [Q9NS15-1] DR AGR; HGNC:6716; -. DR CTD; 4054; -. DR DisGeNET; 4054; -. DR GeneCards; LTBP3; -. DR GeneReviews; LTBP3; -. DR HGNC; HGNC:6716; LTBP3. DR HPA; ENSG00000168056; Low tissue specificity. DR MalaCards; LTBP3; -. DR MIM; 601216; phenotype. DR MIM; 602090; gene. DR MIM; 617809; phenotype. DR neXtProt; NX_Q9NS15; -. DR OpenTargets; ENSG00000168056; -. DR Orphanet; 969; Acromicric dysplasia. DR Orphanet; 2899; Brachyolmia-amelogenesis imperfecta syndrome. DR Orphanet; 2623; Geleophysic dysplasia. DR PharmGKB; PA30479; -. DR VEuPathDB; HostDB:ENSG00000168056; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00940000160285; -. DR InParanoid; Q9NS15; -. DR OMA; CRDSCHH; -. DR OrthoDB; 354414at2759; -. DR PhylomeDB; Q9NS15; -. DR TreeFam; TF317514; -. DR PathwayCommons; Q9NS15; -. DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres. DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. DR SignaLink; Q9NS15; -. DR BioGRID-ORCS; 4054; 83 hits in 1157 CRISPR screens. DR ChiTaRS; LTBP3; human. DR GeneWiki; LTBP3; -. DR GenomeRNAi; 4054; -. DR Pharos; Q9NS15; Tbio. DR PRO; PR:Q9NS15; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9NS15; protein. DR Bgee; ENSG00000168056; Expressed in descending thoracic aorta and 191 other cell types or tissues. DR ExpressionAtlas; Q9NS15; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl. DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl. DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0060430; P:lung saccule development; IEA:Ensembl. DR GO; GO:0030502; P:negative regulation of bone mineralization; IEA:Ensembl. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl. DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; IMP:UniProtKB. DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; IMP:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB. DR CDD; cd00054; EGF_CA; 11. DR Gene3D; 2.10.25.10; Laminin; 15. DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4. DR InterPro; IPR026823; cEGF. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR051145; GAS-SHBG-PROS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR049883; NOTCH1_EGF-like. DR InterPro; IPR017878; TB_dom. DR InterPro; IPR036773; TB_dom_sf. DR PANTHER; PTHR24040:SF13; FIBROPELLIN-1; 1. DR PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF12662; cEGF; 1. DR Pfam; PF07645; EGF_CA; 10. DR Pfam; PF12661; hEGF; 2. DR Pfam; PF00683; TB; 4. DR SMART; SM00181; EGF; 15. DR SMART; SM00179; EGF_CA; 14. DR SUPFAM; SSF57196; EGF/Laminin; 4. DR SUPFAM; SSF57184; Growth factor receptor domain; 4. DR SUPFAM; SSF57581; TB module/8-cys domain; 4. DR PROSITE; PS00010; ASX_HYDROXYL; 11. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 8. DR PROSITE; PS50026; EGF_3; 13. DR PROSITE; PS01187; EGF_CA; 12. DR PROSITE; PS51364; TB; 4. PE 1: Evidence at protein level; KW Alternative splicing; Amelogenesis imperfecta; Disease variant; KW Disulfide bond; Dwarfism; EGF-like domain; Extracellular matrix; KW Glycoprotein; Growth factor binding; Proteomics identification; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..43 FT /evidence="ECO:0000255" FT CHAIN 44..1303 FT /note="Latent-transforming growth factor beta-binding FT protein 3" FT /id="PRO_0000007646" FT DOMAIN 109..141 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 277..331 FT /note="TB 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DOMAIN 355..395 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 403..455 FT /note="TB 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DOMAIN 574..615 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 616..659 FT /note="EGF-like 4; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 660..702 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 744..784 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 785..825 FT /note="EGF-like 7; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 826..865 FT /note="EGF-like 8; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 866..908 FT /note="EGF-like 9; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 917..971 FT /note="TB 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DOMAIN 993..1035 FT /note="EGF-like 10; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1036..1076 FT /note="EGF-like 11; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1082..1122 FT /note="EGF-like 12; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1136..1186 FT /note="TB 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DOMAIN 1254..1298 FT /note="EGF-like 13; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 247..282 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 478..552 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1188..1219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 487..501 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 517..534 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 89 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 349 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 845 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 936 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1275 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 113..123 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 117..129 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 131..140 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 279..303 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 289..316 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 304..319 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 359..370 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 365..379 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 381..394 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 405..428 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 415..440 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 429..443 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 430..455 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 578..590 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 585..599 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 601..614 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 620..632 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 625..641 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 664..676 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 670..685 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 687..701 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 748..759 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 754..768 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 770..783 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 789..800 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 795..809 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 811..824 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 830..841 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 836..850 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 852..864 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 870..883 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 877..892 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 894..907 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 919..942 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 929..954 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 929 FT /note="Interchain (with C-33 in TGFB1); in linked form" FT /evidence="ECO:0000250|UniProtKB:Q14766" FT DISULFID 943..959 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 944..971 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 954 FT /note="Interchain (with C-33 in TGFB1); in linked form" FT /evidence="ECO:0000250|UniProtKB:Q14766" FT DISULFID 997..1010 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1005..1019 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1021..1034 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1040..1051 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1046..1060 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1062..1075 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1086..1097 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1092..1106 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1108..1121 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1138..1162 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 1148..1174 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 1163..1177 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 1164..1186 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DISULFID 1258..1273 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 1268..1282 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT VAR_SEQ 1082..1128 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009241" FT VARIANT 696 FT /note="S -> C (in GPHYSD3; uncertain significance; no FT effect on TGF-beta secretion; dbSNP:rs1554974135)" FT /evidence="ECO:0000269|PubMed:27068007" FT /id="VAR_080565" FT CONFLICT 35 FT /note="Missing (in Ref. 2; BAB15767)" FT /evidence="ECO:0000305" FT CONFLICT 477 FT /note="D -> H (in Ref. 3; AAB64201)" FT /evidence="ECO:0000305" SQ SEQUENCE 1303 AA; 139359 MW; 3BC6B1EE19198414 CRC64; MPGPRGAAGG LAPEMRGAGA AGLLALLLLL LLLLLGLGGR VEGGPAGERG AGGGGALARE RFKVVFAPVI CKRTCLKGQC RDSCQQGSNM TLIGENGHST DTLTGSGFRV VVCPLPCMNG GQCSSRNQCL CPPDFTGRFC QVPAGGAGGG TGGSGPGLSR TGALSTGALP PLAPEGDSVA SKHAIYAVQV IADPPGPGEG PPAQHAAFLV PLGPGQISAE VQAPPPVVNV RVHHPPEASV QVHRIESSNA ESAAPSQHLL PHPKPSHPRP PTQKPLGRCF QDTLPKQPCG SNPLPGLTKQ EDCCGSIGTA WGQSKCHKCP QLQYTGVQKP GPVRGEVGAD CPQGYKRLNS THCQDINECA MPGVCRHGDC LNNPGSYRCV CPPGHSLGPS RTQCIADKPE EKSLCFRLVS PEHQCQHPLT TRLTRQLCCC SVGKAWGARC QRCPTDGTAA FKEICPAGKG YHILTSHQTL TIQGESDFSL FLHPDGPPKP QQLPESPSQA PPPEDTEEER GVTTDSPVSE ERSVQQSHPT ATTTPARPYP ELISRPSPPT MRWFLPDLPP SRSAVEIAPT QVTETDECRL NQNICGHGEC VPGPPDYSCH CNPGYRSHPQ HRYCVDVNEC EAEPCGPGRG ICMNTGGSYN CHCNRGYRLH VGAGGRSCVD LNECAKPHLC GDGGFCINFP GHYKCNCYPG YRLKASRPPV CEDIDECRDP SSCPDGKCEN KPGSFKCIAC QPGYRSQGGG ACRDVNECAE GSPCSPGWCE NLPGSFRCTC AQGYAPAPDG RSCLDVDECE AGDVCDNGIC SNTPGSFQCQ CLSGYHLSRD RSHCEDIDEC DFPAACIGGD CINTNGSYRC LCPQGHRLVG GRKCQDIDEC SQDPSLCLPH GACKNLQGSY VCVCDEGFTP TQDQHGCEEV EQPHHKKECY LNFDDTVFCD SVLATNVTQQ ECCCSLGAGW GDHCEIYPCP VYSSAEFHSL CPDGKGYTQD NNIVNYGIPA HRDIDECMLF GSEICKEGKC VNTQPGYECY CKQGFYYDGN LLECVDVDEC LDESNCRNGV CENTRGGYRC ACTPPAEYSP AQRQCLSPEE MDVDECQDPA ACRPGRCVNL PGSYRCECRP PWVPGPSGRD CQLPESPAER APERRDVCWS QRGEDGMCAG PLAGPALTFD DCCCRQGRGW GAQCRPCPPR GAGSHCPTSQ SESNSFWDTS PLLLGKPPRD EDSSEEDSDE CRCVSGRCVP RPGGAVCECP GGFQLDASRA RCVDIDECRE LNQRGLLCKS ERCVNTSGSF RCVCKAGFAR SRPHGACVPQ RRR //