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Associates non-covalently with TGF-beta-3 and regulates its activation via interaction with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-3 (By similarity). Interaction with integrins results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-3 (By similarity)"}],"commentType":"FUNCTION","molecule":"Latency-associated peptide"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01137"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P04202"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P17125"}],"value":"Transforming growth factor beta-3: Multifunctional protein that regulates embryogenesis and cell differentiation and is required in various processes such as secondary palate development (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains remain non-covalently linked rendering TGF-beta-3 inactive during storage in extracellular matrix (By similarity). At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1 and LRRC32/GARP that control activation of TGF-beta-3 and maintain it in a latent state during storage in extracellular milieus (By similarity). TGF-beta-3 is released from LAP by integrins: integrin-binding results in distortion of the LAP chain and subsequent release of the active TGF-beta-3 (By similarity). Once activated following release of LAP, TGF-beta-3 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01137"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P04202"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P17125"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8819159"}],"value":"Interacts with ASPN (PubMed:8819159). Latency-associated peptide: Homodimer; disulfide-linked. Latency-associated peptide: Interacts with Transforming growth factor beta-3 (TGF-beta-3) chain; interaction is non-covalent and maintains (TGF-beta-3) in a latent state (By similarity). Latency-associated peptide: Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-3 and promote epithelial fusion during palate development (By similarity). Latency-associated peptide: Interacts (via cell attachment site) with integrins, leading to release of the active TGF-beta-3 (By similarity). Transforming growth factor beta-3: Homodimer; disulfide-linked (PubMed:8819159). Transforming growth factor beta-3: Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P10600","intActId":"EBI-1033020"},"interactantTwo":{"uniProtKBAccession":"P10600","geneName":"TGFB3","intActId":"EBI-1033020"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P10600","intActId":"EBI-1033020"},"interactantTwo":{"uniProtKBAccession":"P37173","geneName":"TGFBR2","intActId":"EBI-296151"},"numberOfExperiments":8,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Latency-associated peptide","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01137"}],"value":"Secreted, extracellular space, extracellular matrix","id":"SL-0111"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Transforming growth factor beta-3","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01137"}],"value":"Secreted","id":"SL-0243"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P10600-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P10600-2"],"sequenceIds":["VSP_056285"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P01137"}],"value":"Transforming growth factor beta-3 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26797129"}],"value":"Methylated at Gln-293 by N6AMT1"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Arrhythmogenic right ventricular dysplasia, familial, 1","diseaseAccession":"DI-01549","acronym":"ARVD1","description":"A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias.","diseaseCrossReference":{"database":"MIM","id":"107970"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15639475"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Loeys-Dietz syndrome 5","diseaseAccession":"DI-03991","acronym":"LDS5","description":"A form of Loeys-Dietz syndrome, a syndrome with widespread systemic involvement characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. 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