Beta-nerve growth factor precursor - Mus musculus (Mouse)

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P01139 (NGF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-nerve growth factor
Short name=Beta-NGF

Gene names

Name:	Ngf
Synonyms:	Ngfb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Growth factor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of neuron apoptotic process Inferred from genetic interaction PubMed 11731452. 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 nerve growth factor 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 neurotransmitter secretion Inferred from genetic interaction PubMed 16298082. Source: MGI sensory perception of pain Inferred from mutant phenotype PubMed 8137419. Source: MGI
Cellular_component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome
Molecular_function	receptor signaling protein activity Inferred from direct assay PubMed 12473665. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Potential

Propeptide

19 – 121

103

PRO_0000019601

Chain

122 – 241

120

Beta-nerve growth factor

PRO_0000019602

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

114

N-linked (GlcNAc...) Potential

Disulfide bond

136 ↔ 201

Disulfide bond

179 ↔ 229

Disulfide bond

189 ↔ 231

Experimental info

Sequence conflict

233 – 241

LSRKATRRG → CSAGRLQEEADLPAAPFPTC PLHTLLGPSLPQPVNYFKL in AAB26820. Ref.5

Secondary structure

241

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P01139 [UniParc].

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

241

27,077

        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.

IPI

IPI00882237.

RefSeq

NP_001106168.1. NM_001112698.1.
NP_038637.1. NM_013609.2.

UniGene

Mm.1259.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BET	X-ray	2.30	A	131-237	[»]
1BTG	X-ray	2.50	A/B/C	130-239	[»]
1SGF	X-ray	3.15	B/Y	122-239	[»]
3IJ2	X-ray	3.75	A/B	19-238	[»]
4EAX	X-ray	2.30	A/B/C/D	122-241	[»]

ProteinModelPortal

P01139.

SMR

P01139. Positions 131-238.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59840N.

PTM databases

PhosphoSite

P01139.

Proteomic databases

PRIDE

P01139.

Protocols and materials databases

DNASU

18049.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000035952; ENSMUSP00000040345; ENSMUSG00000027859.

GeneID

18049.

KEGG

mmu:18049.

Organism-specific databases

CTD

4803.

MGI

MGI:97321. Ngf.

Phylogenomic databases

eggNOG

NOG44820.

GeneTree

ENSGT00390000007725.

HOVERGEN

HBG006494.

InParanoid

P01139.

K02582.

OrthoDB

EOG4BRWMZ.

Enzyme and pathway databases

Reactome

REACT_115202. Signal Transduction.

Gene expression databases

ArrayExpress

P01139.

Bgee

P01139.

CleanEx

MM_NGF.

Genevestigator

P01139.

GermOnline

ENSMUSG00000027859. Mus musculus.

Family and domain databases

InterPro

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]

PANTHER

PTHR11589. PTHR11589. 1 hit.

Pfam

PF00243. NGF. 1 hit.
[Graphical view]

PIRSF

PIRSF001789. NGF. 1 hit.

PRINTS

PR01925. MAMLNGFBETA.
PR00268. NGF.
PR01913. NGFBETA.

ProDom

PD002052. Nerve_growth_factor-rel. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00140. NGF. 1 hit.
[Graphical view]

PROSITE

PS00248. NGF_1. 1 hit.
PS50270. NGF_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P01139.

NextBio

293175.

SOURCE

Search...

Entry information

Entry name

NGF_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents