ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P01139


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name NGF_MOUSE
Primary accession number P01139
Secondary accession numbers Q63864 Q6LDB7
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 1, 1990 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 88)
Name and origin of the protein
Protein name Beta-nerve growth factor [Precursor]
Synonym Beta-NGF
Gene name
Name: Ngf
Synonyms: Ngfb
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Submandibular gland;
DOI=10.1038/302538a0; PubMed=6336309 [NCBI, ExPASy, EBI, Israel, Japan]
Scott J., Selby M.J., Urdea M.S., Quiroga M., Bell G.I., Rutter W.J.;
"Isolation and nucleotide sequence of a cDNA encoding the precursor of mouse nerve growth factor.";
Nature 302:538-540(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/303821a0; PubMed=6688123 [NCBI, ExPASy, EBI, Israel, Japan]
Ullrich A., Gray A., Berman C., Dull T.J.;
"Human beta-nerve growth factor gene sequence highly homologous to that of mouse.";
Nature 303:821-825(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6327169 [NCBI, ExPASy, EBI, Israel, Japan]
Ullrich A., Gray A., Berman C., Coussens L., Dull T.J.;
"Sequence homology of human and mouse beta-NGF subunit genes.";
Cold Spring Harb. Symp. Quant. Biol. 48:435-442(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6;
TISSUE=Submandibular gland;
PubMed=3670305 [NCBI, ExPASy, EBI, Israel, Japan]
Selby M.J., Edwards R., Sharp F., Rutter W.J.;
"Mouse nerve growth factor gene: structure and expression.";
Mol. Cell. Biol. 7:3057-3064(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
DOI=10.1016/0197-0186(92)90155-K; PubMed=1284621 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto T., Yamakuni T., Okabe N., Amano T.;
"Production and secretion of nerve growth factor by clonal striated muscle cell line, G8-1.";
Neurochem. Int. 21:251-258(1992).
[6]
PROTEIN SEQUENCE OF 122-239.
DOI=10.1021/bi00725a018; PubMed=4566923 [NCBI, ExPASy, EBI, Israel, Japan]
Angeletti R.H., Hermodson M.A., Bradshaw R.A.;
"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.";
Biochemistry 12:100-115(1973).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1038/354411a0; PubMed=1956407 [NCBI, ExPASy, EBI, Israel, Japan]
McDonald N.Q., Lapatto R., Murray-Rust J., Gunning J., Wlodawer A., Blundell T.L.;
"New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor.";
Nature 354:411-414(1991).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1006/jmbi.1994.1380; PubMed=8201620 [NCBI, ExPASy, EBI, Israel, Japan]
Holland D.R., Cousens L.S., Meng W., Matthews B.W.;
"Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites.";
J. Mol. Biol. 239:385-400(1994).
[9]
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX.
STRAIN=Swiss Webster;
TISSUE=Submandibular gland;
DOI=10.1016/S0969-2126(97)00280-3; PubMed=9351801 [NCBI, ExPASy, EBI, Israel, Japan]
Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q.;
"Structure of mouse 7S NGF: a complex of nerve growth factor with four binding proteins.";
Structure 5:1275-1285(1997).
Comments
  • FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons.
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Secreted.
  • SIMILARITY: Belongs to the NGF-beta family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M35075; AAA39818.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00836; CAA24221.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K01759; AAA39820.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14805; AAA39821.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17298; AAA37687.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17296; AAA37687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17297; AAA37687.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S62089; AAB26820.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001106168.1; -.
UniGene Mm.1259
3D structure databases
PDB
1BET; X-ray; 2.30 A; A=131-237.[ExPASy / RCSB / EBI]
1BTG; X-ray; 2.50 A; A/B/C=130-239.[ExPASy / RCSB / EBI]
1SGF; X-ray; 3.15 A; B/Y=122-239.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BET; -.
1BTG; -.
1SGF; -.
ModBase P01139.
Organism-specific databases
MGI MGI:97321; Ngf.
Gene expression databases
ArrayExpress P01139; -.
CleanEx MM_NGF; -.
GermOnline ENSMUSG00000027859; Mus musculus.
Ontologies
GO
GO:0005788; Cellular component: endoplasmic reticulum lumen (inferred from experiment from Reactome).
GO:0005576; Cellular component: extracellular region (inferred from experiment from Reactome).
GO:0005057; Molecular function: receptor signaling protein activity (inferred from direct assay from MGI).
GO:0007422; Biological process: peripheral nervous system development (inferred from mutant phenotype from MGI).
GO:0045773; Biological process: positive regulation of axon extension (inferred from mutant phenotype from MGI).
GO:0045664; Biological process: regulation of neuron differentiation (inferred from direct assay from MGI).
GO:0046928; Biological process: regulation of neurotransmitter secretion (inferred from genetic interaction from MGI).
GO:0019233; Biological process: sensory perception of pain (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR002072; NGF.
Graphical view of domain structure.
PANTHER PTHR11589; NGF; 1.
Pfam PF00243; NGF; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001789; NGF; 1.
PRINTS PR00268; NGF.
ProDom PD002052; NGF; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00140; NGF; 1.
SMART graphical view of domain structure.
PROSITE PS00248; NGF_1; 1.
PS50270; NGF_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P01139.
Other
SWISS-3DIMAGE P01139.
Genome annotation databases
Ensembl ENSMUSG00000027859; Mus musculus. [Contig view]
GeneID 18049; -.
KEGG mmu:18049; -.
Phylogenomic databases
HOVERGEN P01139; -.
Other
LinkHub P01139; -.
SOURCE Ngf; Mus musculus.
ProtoNet P01139.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cleavage on pair of basic residues; Direct protein sequencing; Glycoprotein; Growth factor; Phosphoprotein; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18     Potential. 
PROPEP   19   121  103      PRO_0000019601
CHAIN   122   241  120     Beta-nerve growth factor. PRO_0000019602
MOD_RES   84    84        Phosphoserine (By similarity). 
CARBOHYD   69    69        N-linked (GlcNAc...) (Potential). 
CARBOHYD   114   114        N-linked (GlcNAc...) (Potential). 
DISULFID   136   201         
DISULFID   179   229         
DISULFID   189   231         
CONFLICT   233   241        LSRKATRRG -> CSAGRLQEEADLPAAPFPTCPLHTLLGPSLPQPVNYFKL (in Ref. 5; AAB26820). 
STRAND   133   136  4      
STRAND   138   144  7      
STRAND   148   151  4      
STRAND   156   159  4      
STRAND   161   165  5      
STRAND   168   171  4      
STRAND   174   180  7      
TURN   194   196  3      
STRAND   197   213  17      
STRAND   218   235  18      
Sequence information
Length: 241 AA [This is the length of the unprocessed precursor] Molecular weight: 27077 Da [This is the MW of the unprocessed precursor] CRC64: 164465E1DC550081 [This is a checksum on the sequence]
        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 

P01139 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!