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P01134 (TGFA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Protransforming growth factor alpha

Cleaved into the following chain:

  1. Transforming growth factor alpha
    Short name=TGF-alpha
    Alternative name(s):
    EGF-like TGF
    Short name=ETGF
    TGF type 1
Gene names
Name:Tgfa
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.

Subunit structure

Interacts with the PDZ domains of MAGI3, SDCBP and SNTA1. The interaction with SDCBP, is required for the targeting to the cell surface. In the endoplasmic reticulum, in its immature form (i.e. with a prosegment and lacking full N-glycosylation), interacts with CNIH. In the Golgi apparatus, may form a complex with CNIH and GORASP2. Interacts (via cytoplasmic C-terminal domain) with NKD2 By similarity.

Subcellular location

Transforming growth factor alpha: Secretedextracellular space.

Protransforming growth factor alpha: Cell membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 1 EGF-like domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   DomainEGF-like domain
Signal
Transmembrane
Transmembrane helix
   Molecular functionGrowth factor
Mitogen
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from sequence or structural similarity. Source: HGNC

angiogenesis

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement PubMed 2103501. Source: RGD

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 11487584. Source: RGD

negative regulation of cellular process

Inferred from direct assay PubMed 11487584. Source: RGD

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 12021046PubMed 19346670. Source: RGD

positive regulation of epidermal growth factor-activated receptor activity

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of mitosis

Inferred from sequence or structural similarity. Source: HGNC

response to drug

Inferred from expression pattern PubMed 16704299. Source: RGD

wound healing

Inferred from expression pattern PubMed 16966143. Source: RGD

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 11487584. Source: RGD

integral component of plasma membrane

Traceable author statement PubMed 2103501. Source: RGD

nucleus

Inferred from direct assay PubMed 14656002. Source: RGD

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionMAP kinase kinase activity

Inferred from sequence or structural similarity. Source: HGNC

epidermal growth factor receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

growth factor activity

Inferred from sequence or structural similarity. Source: HGNC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 159136Protransforming growth factor alpha
PRO_0000302748
Propeptide24 – 3815Removed in mature form
PRO_0000007764
Chain39 – 8850Transforming growth factor alpha
PRO_0000007765
Propeptide89 – 15971Removed in mature form
PRO_0000007766

Regions

Topological domain24 – 9774Extracellular Potential
Transmembrane98 – 12326Helical; Potential
Topological domain124 – 15936Cytoplasmic Potential
Domain42 – 8241EGF-like

Amino acid modifications

Lipidation1521S-palmitoyl cysteine By similarity
Lipidation1531S-palmitoyl cysteine By similarity
Glycosylation251N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 59 By similarity
Disulfide bond54 ↔ 70 By similarity
Disulfide bond72 ↔ 81 By similarity

Experimental info

Sequence conflict281S → P in CAA26036. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P01134 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: E9664EF04DFCF4D5

FASTA15916,960
        10         20         30         40         50         60 
MVPAAGQLAL LALGILVAVC QALENSTSPL SDSPVAAAVV SHFNKCPDSH TQYCFHGTCR 

        70         80         90        100        110        120 
FLVQEEKPAC VCHSGYVGVR CEHADLLAVV AASQKKQAIT ALVVVSIVAL AVLIITCVLI 

       130        140        150 
HCCQVRKHCE WCRALVCRHE KPSALLKGRT ACCHSETVV 

« Hide

References

[1]"Cloning and sequence analysis of a cDNA for rat transforming growth factor-alpha."
Lee D.C., Rose T.M., Webb N.R., Todaro G.J.
Nature 313:489-491(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of the rat transforming growth factor alpha gene and identification of promoter sequences."
Blasband A.J., Rogers K.T., Chen X., Azizkhan J.C., Lee D.C.
Mol. Cell. Biol. 10:2111-2121(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Rat transforming growth factor type 1: structure and relation to epidermal growth factor."
Marquardt H., Hunkapiller M.W., Hood L.E., Todaro G.J.
Science 223:1079-1082(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-88.
[4]"Epidermal growth factor-like transforming growth factor. I. Isolation, chemical characterization, and potentiation by other transforming factors from feline sarcoma virus-transformed rat cells."
Massague J.
J. Biol. Chem. 258:13606-13613(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-67.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02004 mRNA. Translation: CAA26036.1.
M31075 Genomic DNA. Translation: AAA42234.1.
M31076 mRNA. Translation: AAA42233.1.
PIRWFRT1. A93356.
I57497.
RefSeqNP_036803.1. NM_012671.2.
UniGeneRn.9952.

3D structure databases

ProteinModelPortalP01134.
SMRP01134. Positions 39-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000054248.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000057441; ENSRNOP00000054248; ENSRNOG00000016182.
GeneID24827.
KEGGrno:24827.
UCSCRGD:3849. rat.

Organism-specific databases

CTD7039.
RGD3849. Tgfa.

Phylogenomic databases

eggNOGNOG41326.
GeneTreeENSGT00730000110951.
HOGENOMHOG000013036.
HOVERGENHBG000330.
InParanoidP01134.
KOK08774.
OMACHSETGC.
OrthoDBEOG7VQJGP.
PhylomeDBP01134.
TreeFamTF332938.

Gene expression databases

GenevestigatorP01134.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERPTHR10740. PTHR10740. 1 hit.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604544.
PROP01134.

Entry information

Entry nameTGFA_RAT
AccessionPrimary (citable) accession number: P01134
Secondary accession number(s): Q63749
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 123 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