| IED ID | IndEnz0002015825 |
| Enzyme Type ID | protease015825 |
| Protein Name |
Beta-nerve growth factor Beta-NGF |
| Gene Name | Ngf Ngfb |
| 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 | MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG |
| Enzyme Length | 241 |
| Uniprot Accession Number | P01139 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 171; /note="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol); via amide nitrogen and carbonyl oxygen"; /evidence="ECO:0000269|PubMed:26144237, ECO:0007744|PDB:4XPJ"; BINDING 171; /note="a 1-acyl-sn-glycero-3-phospho-L-serine; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:22649032, ECO:0007744|PDB:4EAX"; BINDING 173; /note="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol); via amide nitrogen and carbonyl oxygen"; /evidence="ECO:0000269|PubMed:26144237, ECO:0007744|PDB:4XPJ"; BINDING 209; /note="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol); shared with dimeric partner"; /evidence="ECO:0000269|PubMed:26144237, ECO:0007744|PDB:4XPJ"; BINDING 209; /note="a 1-acyl-sn-glycero-3-phospho-L-serine; shared with dimeric partner"; /evidence="ECO:0000269|PubMed:22649032, ECO:0007744|PDB:4EAX" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems (PubMed:20036257). Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (PubMed:22649032). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse (PubMed:22155786). In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro) (PubMed:20036257). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI (By similarity). Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer (PubMed:22649032, PubMed:26144237). The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form (PubMed:22649032). {ECO:0000250|UniProtKB:P01138, ECO:0000269|PubMed:20036257, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (9); Binding site (5); Chain (1); Disulfide bond (3); Erroneous initiation (5); Glycosylation (2); Helix (1); Mutagenesis (4); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Endosome;Glycoprotein;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain. {ECO:0000269|PubMed:23785138}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1284621}. Endosome lumen {ECO:0000269|PubMed:20036257}. Note=ProNGF is endocytosed after binding to the cell surface receptor formed by SORT1 and NGFR. {ECO:0000269|PubMed:20036257}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:20036257 |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (7) |
| Cross Reference PDB | 1BET; 1BTG; 1SGF; 3IJ2; 4EAX; 4XPJ; 5LSD; 6FFY; |
| Mapped Pubmed ID | 10217270; 10357900; 10362258; 10412058; 10491653; 10545116; 10613847; 10651992; 10677035; 10712647; 10719890; 10888742; 10985348; 11147812; 11161617; 11316775; 11556531; 11731234; 11731452; 11784080; 11877426; 12056835; 12367511; 12473665; 12485622; 1302014; 1336558; 1347284; 1370487; 1376319; 1412798; 14514757; 14623868; 14651951; 14706643; 14736860; 1496419; 14973275; 14976160; 15010204; 15067320; 15093680; 1531670; 15376326; 1547729; 15548667; 15604101; 15625712; 15894570; 16039798; 16141072; 1617222; 16298082; 16319926; 1633105; 1639217; 16516892; 16602821; 1665041; 16729028; 1673105; 16762005; 16953113; 1705364; 17079272; 17093052; 17101855; 17417650; 17488777; 17553423; 17594942; 17653039; 17724343; 17881125; 18006062; 18052984; 18087045; 18162309; 18230652; 18323418; 18329889; 18349525; 18367547; 18498735; 18635195; 18657279; 18709654; 18725298; 18774569; 19029245; 19036963; 19170059; 19193386; 19319189; 19334503; 19342646; 19357131; 19376199; 19444944; 19515925; 1970802; 19728147; 19755105; 19816194; 19844589; 19893045; 20018664; 20032263; 20045424; 20075049; 20350782; 20360245; 20449688; 20507613; 20572009; 20680101; 20696380; 20736176; 21040701; 21048026; 21085186; 21145972; 21151121; 21165786; 21267068; 2133552; 21339331; 21385399; 21529369; 21541365; 21677750; 21816277; 21818348; 22031887; 22098391; 22168511; 22187379; 22318233; 22503986; 22520925; 22621370; 22682244; 22700375; 22808101; 22903500; 22906231; 22999926; 23015435; 23091165; 23100411; 23224557; 23322532; 23426701; 23462468; 23466052; 23538417; 23538529; 23562608; 23623989; 23633509; 2369898; 23825664; 23831350; 23934089; 23989259; 24006456; 24040063; 24139045; 24154525; 24173031; 24265601; 24270184; 24338202; 24438745; 24574008; 24631295; 24733831; 24752460; 24760869; 24811380; 24937592; 24952961; 25049196; 25088915; 25211588; 25231981; 25286822; 25397406; 25410786; 2542863; 25460199; 25496838; 25542970; 25647301; 25650182; 25734767; 26066836; 26347141; 26418744; 26631553; 26683342; 2676841; 27076121; 27306411; 27342083; 2740343; 27424144; 27437725; 27493098; 27568565; 27655914; 27825441; 27997532; 28079757; 28083536; 28232789; 28416686; 28453662; 28542147; 28706241; 28919207; 2897103; 28973166; 2906326; 29166838; 29241539; 29253516; 29381137; 29523844; 29584618; 29589323; 29615468; 29875237; 29975347; 30037926; 3036794; 30430919; 30524266; 30612733; 30934765; 30977543; 31196952; 31578352; 31685654; 31996225; 32579702; 32669337; 32892421; 33307981; 34639085; 34851661; 3871525; 6200835; 7508936; 7523515; 7530767; 7556925; 7608209; 7686585; 7750647; 7751941; 7824161; 7830881; 7852636; 7854358; 7890684; 7963523; 8050673; 8083730; 8090729; 8114702; 8117293; 8137419; 8144363; 8163557; 8163724; 8189222; 8223273; 8288218; 8294906; 8395451; 8404042; 8449508; 8452817; 8586974; 8589528; 8660976; 8764654; 8816255; 8861722; 8907554; 8924216; 925010; 9295375; 9331334; 9457670; 9480761; 9514521; 9640332; 9895316; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,077 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |