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P01139 (NGF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-nerve growth factor

Short name=Beta-NGF
Gene names
Name:Ngf
Synonyms:Ngfb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer.

Subcellular location

Secreted.

Sequence similarities

Belongs to the NGF-beta family.

Sequence caution

The sequence AAA37687.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA39818.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA39820.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA39821.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA24221.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGrowth factor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processextrinsic apoptotic signaling pathway in absence of ligand

Inferred from direct assay PubMed 14623868. Source: MGI

intracellular signal transduction

Inferred from direct assay PubMed 12473665. Source: GOC

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 11731452. Source: MGI

neuron apoptotic process

Inferred from mutant phenotype PubMed 14623868. Source: MGI

neuron projection morphogenesis

Inferred from sequence orthology PubMed 17724343. Source: MGI

peripheral nervous system development

Inferred from mutant phenotype PubMed 14736860. Source: MGI

positive regulation of axon extension

Inferred from mutant phenotype PubMed 8861722. Source: MGI

positive regulation of neurotrophin TRK receptor signaling pathway

Inferred from sequence orthology PubMed 19029245. Source: MGI

positive regulation of protein autophosphorylation

Inferred from sequence orthology PubMed 19029245. Source: MGI

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence orthology PubMed 19029245. Source: MGI

regulation of neuron differentiation

Inferred from direct assay PubMed 16516892. Source: MGI

regulation of neurotransmitter secretion

Inferred from genetic interaction PubMed 16298082. Source: MGI

sensory perception of pain

Inferred from mutant phenotype PubMed 8137419. Source: MGI

   Cellular_componentendoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

   Molecular_functionreceptor signaling protein activity

Inferred from direct assay PubMed 12473665. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 121103
PRO_0000019601
Chain122 – 241120Beta-nerve growth factor
PRO_0000019602

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Disulfide bond136 ↔ 201
Disulfide bond179 ↔ 229
Disulfide bond189 ↔ 231

Experimental info

Sequence conflict233 – 2419LSRKATRRG → CSAGRLQEEADLPAAPFPTC PLHTLLGPSLPQPVNYFKL in AAB26820. Ref.5

Secondary structure

.................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01139 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 164465E1DC550081

FASTA24127,077
        10         20         30         40         50         60 
MSMLFYTLIT AFLIGVQAEP YTDSNVPEGD SVPEAHWTKL QHSLDTALRR ARSAPTAPIA 

        70         80         90        100        110        120 
ARVTGQTRNI TVDPRLFKKR RLHSPRVLFS TQPPPTSSDT LDLDFQAHGT IPFNRTHRSK 

       130        140        150        160        170        180 
RSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR 

       190        200        210        220        230        240 
ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR 


G 

« Hide

References

[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]"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).
[8]"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).
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001106168.1. NM_001112698.2.
NP_038637.1. NM_013609.3.
XP_006501171.1. XM_006501108.1.
XP_006501172.1. XM_006501109.1.
XP_006501173.1. XM_006501110.1.
UniGeneMm.1259.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BETX-ray2.30A131-237[»]
1BTGX-ray2.50A/B/C130-239[»]
1SGFX-ray3.15B/Y122-239[»]
3IJ2X-ray3.75A/B19-238[»]
4EAXX-ray2.30A/B/C/D122-241[»]
ProteinModelPortalP01139.
SMRP01139. Positions 131-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201764. 1 interaction.
DIPDIP-59840N.

PTM databases

PhosphoSiteP01139.

Proteomic databases

PRIDEP01139.

Protocols and materials databases

DNASU18049.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035952; ENSMUSP00000040345; ENSMUSG00000027859.
GeneID18049.
KEGGmmu:18049.
UCSCuc012cuz.1. mouse.

Organism-specific databases

CTD4803.
MGIMGI:97321. Ngf.

Phylogenomic databases

eggNOGNOG44820.
GeneTreeENSGT00390000007725.
HOVERGENHBG006494.
InParanoidP01139.
KOK02582.
PhylomeDBP01139.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

BgeeP01139.
CleanExMM_NGF.
GenevestigatorP01139.

Family and domain databases

InterProIPR020408. 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]
PANTHERPTHR11589. PTHR11589. 1 hit.
PfamPF00243. NGF. 1 hit.
[Graphical view]
PIRSFPIRSF001789. NGF. 1 hit.
PRINTSPR01925. MAMLNGFBETA.
PR00268. NGF.
PR01913. NGFBETA.
ProDomPD002052. Nerve_growth_factor-rel. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00140. NGF. 1 hit.
[Graphical view]
PROSITEPS00248. NGF_1. 1 hit.
PS50270. NGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01139.
NextBio293175.
PROP01139.
SOURCESearch...

Entry information

Entry nameNGF_MOUSE
AccessionPrimary (citable) accession number: P01139
Secondary accession number(s): Q63864, Q6LDB7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot