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Database: UniProt
Entry: NGF_MOUSE
LinkDB: NGF_MOUSE
Original site: 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   27-MAR-2024, entry version 207.
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 a 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   GlyCosmos; P01139; 2 sites, No reported glycans.
DR   GlyGen; P01139; 2 sites.
DR   PhosphoSitePlus; P01139; -.
DR   MaxQB; P01139; -.
DR   PaxDb; 10090-ENSMUSP00000102538; -.
DR   PeptideAtlas; P01139; -.
DR   ProteomicsDB; 252833; -.
DR   ABCD; P01139; 53 sequenced antibodies.
DR   Antibodypedia; 20173; 1453 antibodies from 44 providers.
DR   DNASU; 18049; -.
DR   Ensembl; ENSMUST00000035952.5; ENSMUSP00000040345.4; ENSMUSG00000027859.11.
DR   GeneID; 18049; -.
DR   KEGG; mmu:18049; -.
DR   UCSC; uc012cuz.2; mouse.
DR   AGR; MGI:97321; -.
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; 5399313at2759; -.
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 80 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 70 other cell types or 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: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: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: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: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; Cystine-knot cytokines; 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:SF10; BETA-NERVE GROWTH FACTOR; 1.
DR   PANTHER; PTHR11589; NERVE GROWTH FACTOR NGF -RELATED; 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; Cystine-knot cytokines; 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
//
DBGET integrated database retrieval system