NGF_MOUSE
ID NGF_MOUSE Reviewed; 241 AA.
AC P01139; Q63864; Q6LDB7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Beta-nerve growth factor;
DE Short=Beta-NGF;
DE Flags: Precursor;
GN Name=Ngf; Synonyms=Ngfb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Submandibular gland;
RX PubMed=6336309; DOI=10.1038/302538a0;
RA Scott J., Selby M.J., Urdea M.S., Quiroga M., Bell G.I., Rutter W.J.;
RT "Isolation and nucleotide sequence of a cDNA encoding the precursor of
RT mouse nerve growth factor.";
RL Nature 302:538-540(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6688123; DOI=10.1038/303821a0;
RA Ullrich A., Gray A., Berman C., Dull T.J.;
RT "Human beta-nerve growth factor gene sequence highly homologous to that of
RT mouse.";
RL Nature 303:821-825(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6327169; DOI=10.1101/sqb.1983.048.01.048;
RA Ullrich A., Gray A., Berman C., Coussens L., Dull T.J.;
RT "Sequence homology of human and mouse beta-NGF subunit genes.";
RL Cold Spring Harb. Symp. Quant. Biol. 48:435-442(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Submandibular gland;
RX PubMed=3670305; DOI=10.1128/mcb.7.9.3057-3064.1987;
RA Selby M.J., Edwards R., Sharp F., Rutter W.J.;
RT "Mouse nerve growth factor gene: structure and expression.";
RL Mol. Cell. Biol. 7:3057-3064(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=1284621; DOI=10.1016/0197-0186(92)90155-k;
RA Yamamoto T., Yamakuni T., Okabe N., Amano T.;
RT "Production and secretion of nerve growth factor by clonal striated muscle
RT cell line, G8-1.";
RL Neurochem. Int. 21:251-258(1992).
RN [6]
RP PROTEIN SEQUENCE OF 122-239.
RX PubMed=4566923; DOI=10.1021/bi00725a018;
RA Angeletti R.H., Hermodson M.A., Bradshaw R.A.;
RT "Amino acid sequences of mouse 2.5S nerve growth factor. II. Isolation and
RT characterization of the thermolytic and peptic peptides and the complete
RT covalent structure.";
RL Biochemistry 12:100-115(1973).
RN [7]
RP FUNCTION, AND INTERACTION WITH SORCS2 AND NGFR.
RX PubMed=22155786; DOI=10.1126/scisignal.2002060;
RA Deinhardt K., Kim T., Spellman D.S., Mains R.E., Eipper B.A., Neubert T.A.,
RA Chao M.V., Hempstead B.L.;
RT "Neuronal growth cone retraction relies on proneurotrophin receptor
RT signaling through Rac.";
RL Sci. Signal. 4:RA82-RA82(2011).
RN [8]
RP INDUCTION.
RX PubMed=23785138; DOI=10.1523/jneurosci.2757-12.2013;
RA Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F.,
RA Sassone-Corsi P., Ptacek L.J., Akassoglou K.;
RT "p75 neurotrophin receptor is a clock gene that regulates oscillatory
RT components of circadian and metabolic networks.";
RL J. Neurosci. 33:10221-10234(2013).
RN [9]
RP INTERACTION WITH SORCS2.
RX PubMed=24908487; DOI=10.1016/j.neuron.2014.04.022;
RA Glerup S., Olsen D., Vaegter C.B., Gustafsen C., Sjoegaard S.S., Hermey G.,
RA Kjolby M., Molgaard S., Ulrichsen M., Boggild S., Skeldal S.,
RA Fjorback A.N., Nyengaard J.R., Jacobsen J., Bender D., Bjarkam C.R.,
RA Soerensen E.S., Fuechtbauer E.M., Eichele G., Madsen P., Willnow T.E.,
RA Petersen C.M., Nykjaer A.;
RT "SorCS2 regulates dopaminergic wiring and is processed into an apoptotic
RT two-chain receptor in peripheral glia.";
RL Neuron 82:1074-1087(2014).
RN [10] {ECO:0007744|PDB:1BET}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 131-237, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=1956407; DOI=10.1038/354411a0;
RA McDonald N.Q., Lapatto R., Murray-Rust J., Gunning J., Wlodawer A.,
RA Blundell T.L.;
RT "New protein fold revealed by a 2.3-A resolution crystal structure of nerve
RT growth factor.";
RL Nature 354:411-414(1991).
RN [11] {ECO:0007744|PDB:1BTG}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 130-239, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=8201620; DOI=10.1006/jmbi.1994.1380;
RA Holland D.R., Cousens L.S., Meng W., Matthews B.W.;
RT "Nerve growth factor in different crystal forms displays structural
RT flexibility and reveals zinc binding sites.";
RL J. Mol. Biol. 239:385-400(1994).
RN [12] {ECO:0007744|PDB:1SGF}
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 122-239 OF 7S COMPLEX.
RC STRAIN=Swiss Webster; TISSUE=Submandibular gland;
RX PubMed=9351801; DOI=10.1016/s0969-2126(97)00280-3;
RA Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q.;
RT "Structure of mouse 7S NGF: a complex of nerve growth factor with four
RT binding proteins.";
RL Structure 5:1275-1285(1997).
RN [13] {ECO:0007744|PDB:3IJ2}
RP X-RAY CRYSTALLOGRAPHY (3.75 ANGSTROMS) OF 19-241 IN COMPLEX WITH NGFR,
RP FUNCTION, SUBUNIT, INTERACTION WITH SORT1 AND NGFR, SUBCELLULAR LOCATION,
RP PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF 49-ARG-ARG-50; 79-ARG-LYS-80 AND
RP 120-ARG-LYS-121, AND DISULFIDE BONDS.
RX PubMed=20036257; DOI=10.1016/j.jmb.2009.12.030;
RA Feng D., Kim T., Ozkan E., Light M., Torkin R., Teng K.K., Hempstead B.L.,
RA Garcia K.C.;
RT "Molecular and structural insight into proNGF engagement of p75NTR and
RT sortilin.";
RL J. Mol. Biol. 396:967-984(2010).
RN [14] {ECO:0007744|PDB:4EAX}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 122-241 IN COMPLEX WITH
RP LYSOPHOSPHATIDYLSERINE, FUNCTION, INTERACTION WITH NTRK1, SUBUNIT,
RP LIPID-BINDING, DISULFIDE BONDS, AND MUTAGENESIS OF LYS-209.
RX PubMed=22649032; DOI=10.1096/fj.12-207316;
RA Tong Q., Wang F., Zhou H.Z., Sun H.L., Song H., Shu Y.Y., Gong Y.,
RA Zhang W.T., Cai T.X., Yang F.Q., Tang J., Jiang T.;
RT "Structural and functional insights into lipid-bound nerve growth
RT factors.";
RL FASEB J. 26:3811-3821(2012).
RN [15] {ECO:0007744|PDB:4XPJ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 122-241 IN COMPLEX WITH
RP LYSOPHOSPHATIDYLINOSITOL, FUNCTION, SUBUNIT, LIPID-BINDING, AND DISULFIDE
RP BONDS.
RX PubMed=26144237; DOI=10.1107/s2053230x15008870;
RA Sun H.L., Jiang T.;
RT "The structure of nerve growth factor in complex with
RT lysophosphatidylinositol.";
RL Acta Crystallogr. F 71:906-912(2015).
RN [16] {ECO:0007744|PDB:6FFY}
RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) OF 122-238 IN COMPLEX WITH SORCS2,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=30061605; DOI=10.1038/s41467-018-05405-z;
RA Leloup N., Chataigner L.M.P., Janssen B.J.C.;
RT "Structural insights into SorCS2-Nerve Growth Factor complex formation.";
RL Nat. Commun. 9:2979-2979(2018).
CC -!- FUNCTION: Nerve growth factor is important for the development and
CC maintenance of the sympathetic and sensory nervous systems
CC (PubMed:20036257). Extracellular ligand for the NTRK1 and NGFR
CC receptors, activates cellular signaling cascades to regulate neuronal
CC proliferation, differentiation and survival (PubMed:22649032). The
CC immature NGF precursor (proNGF) functions as ligand for the
CC heterodimeric receptor formed by SORCS2 and NGFR, and activates
CC cellular signaling cascades that lead to inactivation of RAC1 and/or
CC RAC2, reorganization of the actin cytoskeleton and neuronal growth cone
CC collapse (PubMed:22155786). In contrast to mature NGF, the precursor
CC form (proNGF) promotes neuronal apoptosis (in vitro) (PubMed:20036257).
CC Inhibits metalloproteinase-dependent proteolysis of platelet
CC glycoprotein VI (By similarity). Binds lysophosphatidylinositol and
CC lysophosphatidylserine between the two chains of the homodimer
CC (PubMed:22649032, PubMed:26144237). The lipid-bound form promotes
CC histamine relase from mast cells, contrary to the lipid-free form
CC (PubMed:22649032). {ECO:0000250|UniProtKB:P01138,
CC ECO:0000269|PubMed:20036257, ECO:0000269|PubMed:22155786,
CC ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237}.
CC -!- SUBUNIT: Homodimer (PubMed:1956407, PubMed:8201620, PubMed:20036257,
CC PubMed:22649032, PubMed:26144237, PubMed:30061605). The homodimer
CC interacts with a single NTRK1 chain (PubMed:22649032). The homodimer
CC interacts with a single NGFR chain (By similarity). The NGF dimer
CC interacts with a single SORCS2 chain (via extracellular domain)
CC (PubMed:30061605). The NGF precursor (proNGF) binds to a receptor
CC complex formed by SORT1 and NGFR, which leads to NGF endocytosis
CC (PubMed:20036257). Both mature NGF and the immature NGF precursor
CC (proNGF) interact with SORCS2 and with the heterodimer formed by SORCS2
CC and NGFR (via extracellular domains) (PubMed:22155786,
CC PubMed:30061605). The NGF precursor (proNGF) has much higher affinity
CC for SORCS2 than mature NGF (PubMed:24908487). The NGF precursor
CC (proNGF) has much higher affinity for SORT1 than mature NGF
CC (PubMed:20036257). Interacts with ADAM10 in a divalent cation-dependent
CC manner (By similarity). {ECO:0000250|UniProtKB:P01138,
CC ECO:0000269|PubMed:1956407, ECO:0000269|PubMed:20036257,
CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:22649032,
CC ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:26144237,
CC ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1284621}. Endosome
CC lumen {ECO:0000269|PubMed:20036257}. Note=ProNGF is endocytosed after
CC binding to the cell surface receptor formed by SORT1 and NGFR.
CC {ECO:0000269|PubMed:20036257}.
CC -!- TISSUE SPECIFICITY: Detected in submaxillary gland (at protein level)
CC (PubMed:1284621). Highly expressed in male submaxillary gland. Levels
CC are much lower in female submaxillary gland (PubMed:6336309,
CC PubMed:1284621). {ECO:0000269|PubMed:1284621,
CC ECO:0000269|PubMed:6336309}.
CC -!- INDUCTION: Expression oscillates in a circadian manner in the
CC suprachiasmatic nucleus (SCN) of the brain.
CC {ECO:0000269|PubMed:23785138}.
CC -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA39818.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA39820.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA39821.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA24221.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M35075; AAA39818.1; ALT_INIT; mRNA.
DR EMBL; V00836; CAA24221.1; ALT_INIT; mRNA.
DR EMBL; K01759; AAA39820.1; ALT_INIT; mRNA.
DR EMBL; M14805; AAA39821.1; ALT_INIT; mRNA.
DR EMBL; M17298; AAA37687.1; ALT_INIT; Genomic_DNA.
DR EMBL; M17296; AAA37687.1; JOINED; Genomic_DNA.
DR EMBL; M17297; AAA37687.1; JOINED; Genomic_DNA.
DR EMBL; S62089; AAB26820.2; -; mRNA.
DR CCDS; CCDS51025.1; -.
DR RefSeq; NP_001106168.1; NM_001112698.2.
DR RefSeq; NP_038637.1; NM_013609.3.
DR RefSeq; XP_006501171.1; XM_006501108.3.
DR PDB; 1BET; X-ray; 2.30 A; A=131-237.
DR PDB; 1BTG; X-ray; 2.50 A; A/B/C=130-239.
DR PDB; 1SGF; X-ray; 3.15 A; B/Y=122-239.
DR PDB; 3IJ2; X-ray; 3.75 A; A/B=19-241.
DR PDB; 4EAX; X-ray; 2.30 A; A/B/C/D=122-241.
DR PDB; 4XPJ; X-ray; 2.60 A; A/B=122-241.
DR PDB; 5LSD; NMR; -; A/B=122-239.
DR PDB; 6FFY; X-ray; 3.90 A; B/C=122-238.
DR PDBsum; 1BET; -.
DR PDBsum; 1BTG; -.
DR PDBsum; 1SGF; -.
DR PDBsum; 3IJ2; -.
DR PDBsum; 4EAX; -.
DR PDBsum; 4XPJ; -.
DR PDBsum; 5LSD; -.
DR PDBsum; 6FFY; -.
DR AlphaFoldDB; P01139; -.
DR SMR; P01139; -.
DR BioGRID; 201764; 6.
DR DIP; DIP-59840N; -.
DR IntAct; P01139; 4.
DR STRING; 10090.ENSMUSP00000102538; -.
DR GlyGen; P01139; 2 sites.
DR PhosphoSitePlus; P01139; -.
DR MaxQB; P01139; -.
DR PaxDb; P01139; -.
DR PeptideAtlas; P01139; -.
DR PRIDE; P01139; -.
DR ProteomicsDB; 252833; -.
DR ABCD; P01139; 53 sequenced antibodies.
DR Antibodypedia; 20173; 1041 antibodies from 44 providers.
DR DNASU; 18049; -.
DR Ensembl; ENSMUST00000035952; ENSMUSP00000040345; ENSMUSG00000027859.
DR GeneID; 18049; -.
DR KEGG; mmu:18049; -.
DR UCSC; uc012cuz.2; mouse.
DR CTD; 4803; -.
DR MGI; MGI:97321; Ngf.
DR VEuPathDB; HostDB:ENSMUSG00000027859; -.
DR eggNOG; ENOG502RYPU; Eukaryota.
DR GeneTree; ENSGT00390000007725; -.
DR HOGENOM; CLU_059942_1_1_1; -.
DR InParanoid; P01139; -.
DR OrthoDB; 1156054at2759; -.
DR PhylomeDB; P01139; -.
DR Reactome; R-MMU-167060; NGF processing.
DR Reactome; R-MMU-170968; Frs2-mediated activation.
DR Reactome; R-MMU-170984; ARMS-mediated activation.
DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
DR Reactome; R-MMU-187042; TRKA activation by NGF.
DR Reactome; R-MMU-198203; PI3K/AKT activation.
DR Reactome; R-MMU-205017; NFG and proNGF binds to p75NTR.
DR Reactome; R-MMU-205025; NADE modulates death signalling.
DR Reactome; R-MMU-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
DR Reactome; R-MMU-209560; NF-kB is activated and signals survival.
DR Reactome; R-MMU-209563; Axonal growth stimulation.
DR BioGRID-ORCS; 18049; 0 hits in 75 CRISPR screens.
DR EvolutionaryTrace; P01139; -.
DR PRO; PR:P01139; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P01139; protein.
DR Bgee; ENSMUSG00000027859; Expressed in submandibular gland and 68 other tissues.
DR ExpressionAtlas; P01139; baseline and differential.
DR Genevisible; P01139; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0038177; F:death receptor agonist activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005163; F:nerve growth factor receptor binding; ISO:MGI.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:BHF-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IMP:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; ISO:MGI.
DR GO; GO:0021675; P:nerve development; IBA:GO_Central.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IDA:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; IMP:ARUK-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0014042; P:positive regulation of neuron maturation; IDA:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:MGI.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0045664; P:regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IGI:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR DisProt; DP00836; -.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR020408; Nerve_growth_factor-like.
DR InterPro; IPR002072; Nerve_growth_factor-rel.
DR InterPro; IPR020425; Nerve_growth_factor_bsu.
DR InterPro; IPR020437; Nerve_growth_factor_bsu_mml.
DR InterPro; IPR019846; Nerve_growth_factor_CS.
DR PANTHER; PTHR11589; PTHR11589; 1.
DR Pfam; PF00243; NGF; 1.
DR PIRSF; PIRSF001789; NGF; 1.
DR PRINTS; PR01925; MAMLNGFBETA.
DR PRINTS; PR00268; NGF.
DR PRINTS; PR01913; NGFBETA.
DR SMART; SM00140; NGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00248; NGF_1; 1.
DR PROSITE; PS50270; NGF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein;
KW Growth factor; Lipid-binding; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:20036257"
FT PROPEP 19..121
FT /evidence="ECO:0000305|PubMed:20036257,
FT ECO:0000305|PubMed:4566923"
FT /id="PRO_0000019601"
FT CHAIN 122..241
FT /note="Beta-nerve growth factor"
FT /id="PRO_0000019602"
FT BINDING 171
FT /ligand="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol)"
FT /ligand_id="ChEBI:CHEBI:64771"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:26144237,
FT ECO:0007744|PDB:4XPJ"
FT BINDING 171
FT /ligand="a 1-acyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:64379"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:22649032,
FT ECO:0007744|PDB:4EAX"
FT BINDING 173
FT /ligand="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol)"
FT /ligand_id="ChEBI:CHEBI:64771"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:26144237,
FT ECO:0007744|PDB:4XPJ"
FT BINDING 209
FT /ligand="a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol)"
FT /ligand_id="ChEBI:CHEBI:64771"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:26144237,
FT ECO:0007744|PDB:4XPJ"
FT BINDING 209
FT /ligand="a 1-acyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:64379"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:22649032,
FT ECO:0007744|PDB:4EAX"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 136..201
FT /evidence="ECO:0000269|PubMed:1956407,
FT ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237,
FT ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620,
FT ECO:0007744|PDB:1BET, ECO:0007744|PDB:1BTG,
FT ECO:0007744|PDB:1SGF, ECO:0007744|PDB:3IJ2,
FT ECO:0007744|PDB:4EAX, ECO:0007744|PDB:4XPJ,
FT ECO:0007744|PDB:5LSD, ECO:0007744|PDB:6FFY"
FT DISULFID 179..229
FT /evidence="ECO:0000269|PubMed:1956407,
FT ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237,
FT ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620,
FT ECO:0007744|PDB:1BET, ECO:0007744|PDB:1BTG,
FT ECO:0007744|PDB:1SGF, ECO:0007744|PDB:3IJ2,
FT ECO:0007744|PDB:4EAX, ECO:0007744|PDB:4XPJ,
FT ECO:0007744|PDB:5LSD, ECO:0007744|PDB:6FFY"
FT DISULFID 189..231
FT /evidence="ECO:0000269|PubMed:1956407,
FT ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:26144237,
FT ECO:0000269|PubMed:30061605, ECO:0000269|PubMed:8201620,
FT ECO:0007744|PDB:1BET, ECO:0007744|PDB:1BTG,
FT ECO:0007744|PDB:1SGF, ECO:0007744|PDB:3IJ2,
FT ECO:0007744|PDB:4EAX, ECO:0007744|PDB:4XPJ,
FT ECO:0007744|PDB:5LSD, ECO:0007744|PDB:6FFY"
FT MUTAGEN 49..50
FT /note="RR->AA: Abolishes production of the mature chain and
FT promotes apoptosis of superior cervical ganglion neurons;
FT when associated with 79-A-A-80 and 120-A-A-121."
FT /evidence="ECO:0000269|PubMed:20036257"
FT MUTAGEN 79..80
FT /note="KR->AA: Abolishes production of the mature chain and
FT promotes apoptosis of superior cervical ganglion neurons;
FT when associated with 49-A-A-50 and 120-A-A-121."
FT /evidence="ECO:0000269|PubMed:20036257"
FT MUTAGEN 120..121
FT /note="KR->AA: Abolishes production of the mature chain and
FT promotes apoptosis of superior cervical ganglion neurons;
FT when associated with 49-A-A-50 and 79-A-A-80."
FT /evidence="ECO:0000269|PubMed:20036257"
FT MUTAGEN 209
FT /note="K->L: Near loss of the ability to trigger histamine
FT release from mast cells. No effect on interaction with
FT NTRK1."
FT /evidence="ECO:0000269|PubMed:22649032"
FT CONFLICT 233..241
FT /note="LSRKATRRG -> CSAGRLQEEADLPAAPFPTCPLHTLLGPSLPQPVNYFKL
FT (in Ref. 5; AAB26820)"
FT /evidence="ECO:0000305"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5LSD"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:4EAX"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1BET"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1BET"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1BET"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1BET"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1BET"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1BET"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1BET"
FT STRAND 197..213
FT /evidence="ECO:0007829|PDB:1BET"
FT STRAND 218..235
FT /evidence="ECO:0007829|PDB:1BET"
SQ SEQUENCE 241 AA; 27077 MW; 164465E1DC550081 CRC64;
MSMLFYTLIT AFLIGVQAEP YTDSNVPEGD SVPEAHWTKL QHSLDTALRR ARSAPTAPIA
ARVTGQTRNI TVDPRLFKKR RLHSPRVLFS TQPPPTSSDT LDLDFQAHGT IPFNRTHRSK
RSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR
ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR
G
