| IED ID | IndEnz0002013668 |
| Enzyme Type ID | protease013668 |
| Protein Name |
Transforming growth factor beta-2 proprotein Cleaved into: Latency-associated peptide LAP ; Transforming growth factor beta-2 TGF-beta-2 |
| Gene Name | Tgfb2 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MHYCVLSTFLLLHLVPVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPDEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPSHLPSENAIPPTFYRPYFRIVRFDVSTMEKNASNLVKAEFRVFRLQNPKARVAEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVQEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYASGDQKTIKSTRKKTSGKTPHLLLMLLPSYRLESQQSSRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHTKVLSLYNTINPEASASPCCVSQDLEPLTILYYIGNTPKIEQLSNMIVKSCKCS |
| Enzyme Length | 414 |
| Uniprot Accession Number | P27090 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Transforming growth factor beta-2 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-2 and regulates its activation via interaction with 'milieu molecules', such as LTBP1 and LRRC32/GARP, that control activation of TGF-beta-2. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: Transforming growth factor beta-2: Multifunctional protein that regulates various processes such as angiogenesis and heart 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-2 (TGF-beta-2) chains remain non-covalently linked rendering TGF-beta-2 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-2 and maintain it in a latent state during storage in extracellular milieus (By similarity). Once activated following release of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202, ECO:0000250|UniProtKB:P61812}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (10); Chain (2); Disulfide bond (5); Glycosylation (3); Helix (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | 3D-structure;Cleavage on pair of basic residues;Disulfide bond;Extracellular matrix;Glycoprotein;Growth factor;Mitogen;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted {ECO:0000250|UniProtKB:P01137}. |
| Modified Residue | |
| Post Translational Modification | PTM: Transforming growth factor beta-2 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-2 (TGF-beta-2) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-2 inactive. {ECO:0000250|UniProtKB:P01137}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5TX2; 5TX6; |
| Mapped Pubmed ID | 10030593; 10349630; 10433821; 10446266; 10521784; 10588868; 10848613; 10976050; 10984614; 11084649; 11092979; 11106407; 11109025; 11159184; 11180952; 11390347; 11404017; 11526486; 11675471; 11677049; 11784073; 11829488; 11830573; 11850179; 11854453; 11857453; 11882017; 11934857; 11960699; 11984523; 12091349; 12114535; 12141444; 12142029; 12192060; 12217325; 12220125; 12381922; 12393102; 12466851; 12478370; 12588999; 12617806; 12666199; 12666204; 12773577; 12805272; 12815630; 12838410; 1284245; 1373953; 1375903; 14550911; 14701881; 14707111; 15031101; 15226263; 15248063; 15294963; 15305298; 15342483; 1543915; 15478122; 15528466; 15531369; 15582152; 15615879; 15630473; 15724248; 15744664; 1577201; 15911702; 15923624; 15929941; 15963767; 16026545; 16026622; 16141072; 16192636; 16257223; 16282338; 16314491; 1638993; 16466398; 16598383; 16602821; 16632597; 16702235; 1672660; 16741229; 1676977; 16787918; 16879310; 16887829; 16919269; 1707784; 17141511; 1723948; 17272814; 17303760; 17350578; 17391645; 17418116; 17460765; 17519332; 17526730; 17559664; 17634193; 1764993; 17673674; 17767158; 17804598; 17881772; 17997227; 18038450; 18159948; 18213583; 18287057; 18317401; 18358466; 18498095; 18498113; 18508041; 18723448; 18790002; 1879607; 18796538; 18804458; 18854036; 18941179; 18945958; 19084512; 19109099; 19123128; 19141644; 19161227; 19164472; 19304887; 19403103; 19449303; 19465598; 19509472; 1955457; 19587023; 1970330; 19705113; 19757385; 19846762; 19864318; 19906978; 19965872; 20007998; 2015789; 20184861; 20200502; 20230754; 20299672; 20300191; 20346356; 2040369; 20421479; 20427645; 20501701; 20530870; 20565961; 20603020; 20633555; 20858897; 20875417; 20890042; 20970343; 21087928; 21181942; 21266196; 21300867; 21352545; 21356372; 21436291; 21512031; 21533152; 21593251; 21597012; 21780244; 21880664; 21909369; 21959449; 21967974; 21983003; 21984612; 22130515; 22186728; 22235033; 2226202; 22326956; 22331429; 22437311; 22485132; 22560297; 22573381; 22674610; 22682244; 22696295; 22739237; 22772368; 22847922; 22899851; 22995554; 23041440; 23193168; 23303681; 23319608; 23342175; 23525041; 23560082; 23584732; 23603491; 2375595; 23824573; 23946447; 24006456; 2401212; 24045946; 24131868; 24157418; 24161934; 24278323; 24279395; 24356956; 24449835; 24472616; 24474796; 24550112; 24623077; 24680892; 24741061; 24760528; 2481605; 24831012; 24859004; 24895296; 24906856; 24917498; 24952961; 24990151; 24996922; 25053429; 25082703; 25249460; 25274628; 25318679; 25332192; 25336743; 25382630; 25428587; 25448845; 25450421; 25467979; 25520397; 25575930; 25715398; 25766329; 25963716; 26100917; 26120030; 26284554; 26315405; 26324903; 26457758; 26458493; 26472242; 26607280; 26799667; 26837596; 26878215; 26930384; 26952977; 27056911; 27180663; 27215389; 27224923; 27348588; 27358050; 27377816; 27465829; 27605619; 27771509; 27913639; 27922003; 27939132; 28009292; 28159809; 28228478; 28329690; 28538179; 28558017; 28568893; 28621467; 28640846; 28675425; 28700594; 28771943; 28807903; 28809397; 28945200; 29031500; 29038307; 29416028; 29438518; 29540665; 29593116; 29618843; 29686677; 29689292; 29743238; 29853617; 29869452; 29945868; 30201295; 30228991; 30598510; 30659114; 30731284; 30922407; 31028279; 31118233; 31311865; 31399471; 31719045; 32001436; 32219603; 3226728; 32655758; 32794350; 32938678; 33147210; 33227706; 33510480; 33798452; 33846290; 34622152; 34830390; 7485998; 7493021; 7574296; 7601910; 7627810; 7687212; 7774812; 7813789; 7819129; 7819439; 7842167; 7883868; 8002998; 8050368; 8075820; 8119140; 8125201; 8148154; 8164195; 8206089; 8358866; 8530024; 8541216; 8565825; 8726224; 8916368; 9010342; 9169087; 9177772; 9184209; 9203584; 9217007; 9427478; 9525700; 9768360; 9839358; 9921650; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,589 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |