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P01134

- TGFA_RAT

UniProt

P01134 - TGFA_RAT

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Protein
Protransforming growth factor alpha
Gene
Tgfa
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. MAP kinase kinase activity Source: HGNC
  2. epidermal growth factor receptor binding Source: UniProtKB
  3. growth factor activity Source: HGNC

GO - Biological processi

  1. activation of MAPK activity Source: HGNC
  2. angiogenesis Source: Ensembl
  3. epidermal growth factor receptor signaling pathway Source: RGD
  4. mammary gland alveolus development Source: Ensembl
  5. negative regulation of apoptotic process Source: RGD
  6. negative regulation of cellular process Source: RGD
  7. positive regulation of cell division Source: UniProtKB-KW
  8. positive regulation of cell proliferation Source: RGD
  9. positive regulation of epidermal growth factor-activated receptor activity Source: HGNC
  10. positive regulation of epithelial cell proliferation Source: HGNC
  11. positive regulation of mitosis Source: HGNC
  12. response to drug Source: RGD
  13. wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Mitogen

Names & Taxonomyi

Protein namesi
Recommended name:
Protransforming growth factor alpha
Cleaved into the following chain:
Alternative name(s):
EGF-like TGF
Short name:
ETGF
TGF type 1
Gene namesi
Name:Tgfa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi3849. Tgfa.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 9774Extracellular Reviewed prediction
Add
BLAST
Transmembranei98 – 12326Helical; Reviewed prediction
Add
BLAST
Topological domaini124 – 15936Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. cell surface Source: Ensembl
  3. cytoplasmic vesicle Source: Ensembl
  4. extracellular space Source: RGD
  5. integral component of plasma membrane Source: RGD
  6. nucleus Source: RGD
  7. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 159136Protransforming growth factor alpha
PRO_0000302748Add
BLAST
Propeptidei24 – 3815Removed in mature form
PRO_0000007764Add
BLAST
Chaini39 – 8850Transforming growth factor alpha
PRO_0000007765Add
BLAST
Propeptidei89 – 15971Removed in mature form
PRO_0000007766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi46 ↔ 59 By similarity
Disulfide bondi54 ↔ 70 By similarity
Disulfide bondi72 ↔ 81 By similarity
Lipidationi152 – 1521S-palmitoyl cysteine By similarity
Lipidationi153 – 1531S-palmitoyl cysteine By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Expressioni

Gene expression databases

GenevestigatoriP01134.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000054248.

Structurei

3D structure databases

ProteinModelPortaliP01134.
SMRiP01134. Positions 39-88.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 8241EGF-like
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41326.
GeneTreeiENSGT00730000110951.
HOGENOMiHOG000013036.
HOVERGENiHBG000330.
InParanoidiP01134.
KOiK08774.
OMAiCHSETGC.
OrthoDBiEOG7VQJGP.
PhylomeDBiP01134.
TreeFamiTF332938.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERiPTHR10740. PTHR10740. 1 hit.
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01134-1 [UniParc]FASTAAdd to Basket

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MVPAAGQLAL LALGILVAVC QALENSTSPL SDSPVAAAVV SHFNKCPDSH    50
TQYCFHGTCR FLVQEEKPAC VCHSGYVGVR CEHADLLAVV AASQKKQAIT 100
ALVVVSIVAL AVLIITCVLI HCCQVRKHCE WCRALVCRHE KPSALLKGRT 150
ACCHSETVV 159
Length:159
Mass (Da):16,960
Last modified:July 15, 1998 - v2
Checksum:iE9664EF04DFCF4D5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281S → P in CAA26036. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02004 mRNA. Translation: CAA26036.1.
M31075 Genomic DNA. Translation: AAA42234.1.
M31076 mRNA. Translation: AAA42233.1.
PIRiA93356. WFRT1.
I57497.
RefSeqiNP_036803.1. NM_012671.2.
UniGeneiRn.9952.

Genome annotation databases

EnsembliENSRNOT00000057441; ENSRNOP00000054248; ENSRNOG00000016182.
GeneIDi24827.
KEGGirno:24827.
UCSCiRGD:3849. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02004 mRNA. Translation: CAA26036.1 .
M31075 Genomic DNA. Translation: AAA42234.1 .
M31076 mRNA. Translation: AAA42233.1 .
PIRi A93356. WFRT1.
I57497.
RefSeqi NP_036803.1. NM_012671.2.
UniGenei Rn.9952.

3D structure databases

ProteinModelPortali P01134.
SMRi P01134. Positions 39-88.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000054248.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000057441 ; ENSRNOP00000054248 ; ENSRNOG00000016182 .
GeneIDi 24827.
KEGGi rno:24827.
UCSCi RGD:3849. rat.

Organism-specific databases

CTDi 7039.
RGDi 3849. Tgfa.

Phylogenomic databases

eggNOGi NOG41326.
GeneTreei ENSGT00730000110951.
HOGENOMi HOG000013036.
HOVERGENi HBG000330.
InParanoidi P01134.
KOi K08774.
OMAi CHSETGC.
OrthoDBi EOG7VQJGP.
PhylomeDBi P01134.
TreeFami TF332938.

Miscellaneous databases

NextBioi 604544.
PROi P01134.

Gene expression databases

Genevestigatori P01134.

Family and domain databases

InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR015497. EGF_rcpt_ligand.
[Graphical view ]
PANTHERi PTHR10740. PTHR10740. 1 hit.
SMARTi SM00181. EGF. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiTGFA_RAT
AccessioniPrimary (citable) accession number: P01134
Secondary accession number(s): Q63749
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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