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Protein

Beta-nerve growth factor

Gene

Ngf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survival. Inhibits metalloproteinase dependent proteolysis of platelet glycoprotein VI.By similarity

GO - Molecular functioni

GO - Biological processi

  • cell-cell signaling Source: GO_Central
  • circadian rhythm Source: UniProtKB
  • extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • intracellular signal transduction Source: GOC
  • negative regulation of endopeptidase activity Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • nerve growth factor signaling pathway Source: MGI
  • neuron apoptotic process Source: MGI
  • neuron projection morphogenesis Source: MGI
  • peripheral nervous system development Source: MGI
  • positive regulation of axon extension Source: MGI
  • positive regulation of collateral sprouting Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of neuron maturation Source: MGI
  • positive regulation of neuron projection development Source: MGI
  • positive regulation of neurotrophin TRK receptor signaling pathway Source: MGI
  • positive regulation of protein autophosphorylation Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • regulation of neuron differentiation Source: MGI
  • regulation of neurotransmitter secretion Source: MGI
  • regulation of release of sequestered calcium ion into cytosol Source: MGI
  • sensory perception of pain Source: MGI
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Enzyme and pathway databases

ReactomeiREACT_280416. PI3K/AKT activation.
REACT_283484. Frs2-mediated activation.
REACT_289095. NRAGE signals death through JNK.
REACT_290178. PLC-gamma1 signalling.
REACT_294694. p75NTR negatively regulates cell cycle via SC1.
REACT_295008. p75NTR recruits signalling complexes.
REACT_304279. Retrograde neurotrophin signalling.
REACT_312205. Signalling to p38 via RIT and RIN.
REACT_317611. NGF processing.
REACT_320246. Signalling to RAS.
REACT_324521. NADE modulates death signalling.
REACT_324620. ARMS-mediated activation.
REACT_333825. NF-kB is activated and signals survival.
REACT_342872. NRIF signals cell death from the nucleus.
REACT_343028. Signalling to STAT3.
REACT_345090. Ceramide signalling.
REACT_348617. Axonal growth stimulation.
REACT_348780. NFG and proNGF binds to p75NTR.
REACT_351184. TRKA activation by NGF.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-nerve growth factor
Short name:
Beta-NGF
Gene namesi
Name:Ngf
Synonyms:Ngfb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:97321. Ngf.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 1211031 PublicationPRO_0000019601Add
BLAST
Chaini122 – 241120Beta-nerve growth factorPRO_0000019602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi136 ↔ 201
Disulfide bondi179 ↔ 229
Disulfide bondi189 ↔ 231

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01139.
PRIDEiP01139.

PTM databases

PhosphoSiteiP01139.

Expressioni

Inductioni

Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain.1 Publication

Gene expression databases

BgeeiP01139.
CleanExiMM_NGF.
ExpressionAtlasiP01139. baseline and differential.
GenevisibleiP01139. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with ADAM10 in a divalent cation-dependent manner.By similarity

Protein-protein interaction databases

BioGridi201764. 1 interaction.
DIPiDIP-59840N.
IntActiP01139. 3 interactions.
STRINGi10090.ENSMUSP00000102538.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi133 – 1364Combined sources
Beta strandi138 – 1447Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi174 – 1807Combined sources
Turni194 – 1963Combined sources
Beta strandi197 – 21317Combined sources
Beta strandi218 – 23518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BETX-ray2.30A131-237[»]
1BTGX-ray2.50A/B/C130-239[»]
1SGFX-ray3.15B/Y122-239[»]
3IJ2X-ray3.75A/B19-241[»]
4EAXX-ray2.30A/B/C/D122-241[»]
ProteinModelPortaliP01139.
SMRiP01139. Positions 131-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01139.

Family & Domainsi

Sequence similaritiesi

Belongs to the NGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG44820.
GeneTreeiENSGT00390000007725.
HOVERGENiHBG006494.
InParanoidiP01139.
KOiK02582.
PhylomeDBiP01139.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR020408. Nerve_growth_factor-like.
IPR002072. Nerve_growth_factor-rel.
IPR020425. Nerve_growth_factor_bsu.
IPR020437. Nerve_growth_factor_bsu_mml.
IPR019846. Nerve_growth_factor_CS.
[Graphical view]
PANTHERiPTHR11589. PTHR11589. 1 hit.
PfamiPF00243. NGF. 1 hit.
[Graphical view]
PIRSFiPIRSF001789. NGF. 1 hit.
PRINTSiPR01925. MAMLNGFBETA.
PR00268. NGF.
PR01913. NGFBETA.
ProDomiPD002052. Nerve_growth_factor-rel. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00140. NGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00248. NGF_1. 1 hit.
PS50270. NGF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01139-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMLFYTLIT AFLIGVQAEP YTDSNVPEGD SVPEAHWTKL QHSLDTALRR
60 70 80 90 100
ARSAPTAPIA ARVTGQTRNI TVDPRLFKKR RLHSPRVLFS TQPPPTSSDT
110 120 130 140 150
LDLDFQAHGT IPFNRTHRSK RSSTHPVFHM GEFSVCDSVS VWVGDKTTAT
160 170 180 190 200
DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY
210 220 230 240
CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G
Length:241
Mass (Da):27,077
Last modified:January 1, 1990 - v2
Checksum:i164465E1DC550081
GO

Sequence cautioni

The sequence AAA37687.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA39818.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA39820.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA39821.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA24221.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2419LSRKATRRG → CSAGRLQEEADLPAAPFPTC PLHTLLGPSLPQPVNYFKL in AAB26820 (PubMed:1284621).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35075 mRNA. Translation: AAA39818.1. Different initiation.
V00836 mRNA. Translation: CAA24221.1. Different initiation.
K01759 mRNA. Translation: AAA39820.1. Different initiation.
M14805 mRNA. Translation: AAA39821.1. Different initiation.
M17298, M17296, M17297 Genomic DNA. Translation: AAA37687.1. Different initiation.
S62089 mRNA. Translation: AAB26820.2.
CCDSiCCDS51025.1.
RefSeqiNP_001106168.1. NM_001112698.2.
NP_038637.1. NM_013609.3.
XP_006501171.1. XM_006501108.2.
XP_006501172.1. XM_006501109.2.
XP_006501173.1. XM_006501110.2.
UniGeneiMm.1259.

Genome annotation databases

EnsembliENSMUST00000035952; ENSMUSP00000040345; ENSMUSG00000027859.
GeneIDi18049.
KEGGimmu:18049.
UCSCiuc012cuz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35075 mRNA. Translation: AAA39818.1. Different initiation.
V00836 mRNA. Translation: CAA24221.1. Different initiation.
K01759 mRNA. Translation: AAA39820.1. Different initiation.
M14805 mRNA. Translation: AAA39821.1. Different initiation.
M17298, M17296, M17297 Genomic DNA. Translation: AAA37687.1. Different initiation.
S62089 mRNA. Translation: AAB26820.2.
CCDSiCCDS51025.1.
RefSeqiNP_001106168.1. NM_001112698.2.
NP_038637.1. NM_013609.3.
XP_006501171.1. XM_006501108.2.
XP_006501172.1. XM_006501109.2.
XP_006501173.1. XM_006501110.2.
UniGeneiMm.1259.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BETX-ray2.30A131-237[»]
1BTGX-ray2.50A/B/C130-239[»]
1SGFX-ray3.15B/Y122-239[»]
3IJ2X-ray3.75A/B19-241[»]
4EAXX-ray2.30A/B/C/D122-241[»]
ProteinModelPortaliP01139.
SMRiP01139. Positions 131-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201764. 1 interaction.
DIPiDIP-59840N.
IntActiP01139. 3 interactions.
STRINGi10090.ENSMUSP00000102538.

PTM databases

PhosphoSiteiP01139.

Proteomic databases

MaxQBiP01139.
PRIDEiP01139.

Protocols and materials databases

DNASUi18049.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035952; ENSMUSP00000040345; ENSMUSG00000027859.
GeneIDi18049.
KEGGimmu:18049.
UCSCiuc012cuz.1. mouse.

Organism-specific databases

CTDi4803.
MGIiMGI:97321. Ngf.

Phylogenomic databases

eggNOGiNOG44820.
GeneTreeiENSGT00390000007725.
HOVERGENiHBG006494.
InParanoidiP01139.
KOiK02582.
PhylomeDBiP01139.

Enzyme and pathway databases

ReactomeiREACT_280416. PI3K/AKT activation.
REACT_283484. Frs2-mediated activation.
REACT_289095. NRAGE signals death through JNK.
REACT_290178. PLC-gamma1 signalling.
REACT_294694. p75NTR negatively regulates cell cycle via SC1.
REACT_295008. p75NTR recruits signalling complexes.
REACT_304279. Retrograde neurotrophin signalling.
REACT_312205. Signalling to p38 via RIT and RIN.
REACT_317611. NGF processing.
REACT_320246. Signalling to RAS.
REACT_324521. NADE modulates death signalling.
REACT_324620. ARMS-mediated activation.
REACT_333825. NF-kB is activated and signals survival.
REACT_342872. NRIF signals cell death from the nucleus.
REACT_343028. Signalling to STAT3.
REACT_345090. Ceramide signalling.
REACT_348617. Axonal growth stimulation.
REACT_348780. NFG and proNGF binds to p75NTR.
REACT_351184. TRKA activation by NGF.

Miscellaneous databases

EvolutionaryTraceiP01139.
NextBioi293175.
PROiP01139.
SOURCEiSearch...

Gene expression databases

BgeeiP01139.
CleanExiMM_NGF.
ExpressionAtlasiP01139. baseline and differential.
GenevisibleiP01139. MM.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR020408. Nerve_growth_factor-like.
IPR002072. Nerve_growth_factor-rel.
IPR020425. Nerve_growth_factor_bsu.
IPR020437. Nerve_growth_factor_bsu_mml.
IPR019846. Nerve_growth_factor_CS.
[Graphical view]
PANTHERiPTHR11589. PTHR11589. 1 hit.
PfamiPF00243. NGF. 1 hit.
[Graphical view]
PIRSFiPIRSF001789. NGF. 1 hit.
PRINTSiPR01925. MAMLNGFBETA.
PR00268. NGF.
PR01913. NGFBETA.
ProDomiPD002052. Nerve_growth_factor-rel. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00140. NGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00248. NGF_1. 1 hit.
PS50270. NGF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and nucleotide sequence of a cDNA encoding the precursor of mouse nerve growth factor."
    Scott J., Selby M.J., Urdea M.S., Quiroga M., Bell G.I., Rutter W.J.
    Nature 302:538-540(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Submandibular gland.
  2. "Human beta-nerve growth factor gene sequence highly homologous to that of mouse."
    Ullrich A., Gray A., Berman C., Dull T.J.
    Nature 303:821-825(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequence homology of human and mouse beta-NGF subunit genes."
    Ullrich A., Gray A., Berman C., Coussens L., Dull T.J.
    Cold Spring Harb. Symp. Quant. Biol. 48:435-442(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Mouse nerve growth factor gene: structure and expression."
    Selby M.J., Edwards R., Sharp F., Rutter W.J.
    Mol. Cell. Biol. 7:3057-3064(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6.
    Tissue: Submandibular gland.
  5. "Production and secretion of nerve growth factor by clonal striated muscle cell line, G8-1."
    Yamamoto T., Yamakuni T., Okabe N., Amano T.
    Neurochem. Int. 21:251-258(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  6. "Amino acid sequences of mouse 2.5S nerve growth factor. II. Isolation and characterization of the thermolytic and peptic peptides and the complete covalent structure."
    Angeletti R.H., Hermodson M.A., Bradshaw R.A.
    Biochemistry 12:100-115(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 122-239.
  7. "p75 neurotrophin receptor is a clock gene that regulates oscillatory components of circadian and metabolic networks."
    Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., Sassone-Corsi P., Ptacek L.J., Akassoglou K.
    J. Neurosci. 33:10221-10234(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor."
    McDonald N.Q., Lapatto R., Murray-Rust J., Gunning J., Wlodawer A., Blundell T.L.
    Nature 354:411-414(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  9. "Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites."
    Holland D.R., Cousens L.S., Meng W., Matthews B.W.
    J. Mol. Biol. 239:385-400(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  10. "Structure of mouse 7S NGF: a complex of nerve growth factor with four binding proteins."
    Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q.
    Structure 5:1275-1285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX.
    Strain: Swiss Webster.
    Tissue: Submandibular gland.

Entry informationi

Entry nameiNGF_MOUSE
AccessioniPrimary (citable) accession number: P01139
Secondary accession number(s): Q63864, Q6LDB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: June 24, 2015
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.