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Protransforming growth factor alpha [Cleaved into: Transforming growth factor alpha (TGF-alpha) (EGF-like TGF) (ETGF) (TGF type 1)]

 TGFA_MOUSE              Reviewed;         159 AA.
P48030;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
12-SEP-2018, entry version 145.
RecName: Full=Protransforming growth factor alpha;
Contains:
RecName: Full=Transforming growth factor alpha;
Short=TGF-alpha;
AltName: Full=EGF-like TGF;
Short=ETGF;
AltName: Full=TGF type 1;
Flags: Precursor;
Name=Tgfa;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1420315; DOI=10.1016/0167-4781(92)90170-5;
Vaughan T.J., Pascall J.C., Brown K.D.;
"Nucleotide sequence and tissue distribution of mouse transforming
growth factor-alpha.";
Biochim. Biophys. Acta 1132:322-324(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/Sv; TISSUE=Brain;
PubMed=8877107;
Berkowitz E.A., Seroogy K.B., Schroeder J.A., Russell W.E.,
Evans E.P., Riedel R.F., Phillips H.K., Harrison C.A., Lee D.C.,
Luetteke N.C.;
"Characterization of the mouse transforming growth factor alpha gene:
its expression during eyelid development and in waved 1 tissues.";
Cell Growth Differ. 7:1271-1282(1996).
[3]
INTERACTION WITH MAGI3.
PubMed=15652357; DOI=10.1016/j.yexcr.2004.10.007;
Franklin J.L., Yoshiura K., Dempsey P.J., Bogatcheva G., Jeyakumar L.,
Meise K.S., Pearsall R.S., Threadgill D., Coffey R.J.;
"Identification of MAGI-3 as a transforming growth factor-alpha tail
binding protein.";
Exp. Cell Res. 303:457-470(2005).
-!- 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: Interacts with the PDZ domains of 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). Interacts with MAGI3. {ECO:0000250,
ECO:0000269|PubMed:15652357}.
-!- SUBCELLULAR LOCATION: Transforming growth factor alpha: Secreted,
extracellular space.
-!- SUBCELLULAR LOCATION: Protransforming growth factor alpha: Cell
membrane; Single-pass type I membrane protein.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; M92420; AAA40481.1; -; mRNA.
EMBL; U65016; AAB50554.1; -; mRNA.
EMBL; U64873; AAB50553.1; -; Genomic_DNA.
CCDS; CCDS51832.1; -.
PIR; S27195; S27195.
RefSeq; NP_112476.1; NM_031199.4.
UniGene; Mm.137222; -.
ProteinModelPortal; P48030; -.
SMR; P48030; -.
IntAct; P48030; 1.
MINT; P48030; -.
STRING; 10090.ENSMUSP00000032066; -.
PaxDb; P48030; -.
PRIDE; P48030; -.
Ensembl; ENSMUST00000032066; ENSMUSP00000032066; ENSMUSG00000029999.
GeneID; 21802; -.
KEGG; mmu:21802; -.
UCSC; uc009crk.2; mouse.
CTD; 7039; -.
MGI; MGI:98724; Tgfa.
eggNOG; ENOG410IVW5; Eukaryota.
eggNOG; ENOG4111Z4I; LUCA.
GeneTree; ENSGT00730000110951; -.
HOGENOM; HOG000013036; -.
HOVERGEN; HBG000330; -.
InParanoid; P48030; -.
KO; K08774; -.
OMA; LIHCCEV; -.
OrthoDB; EOG091G0RK4; -.
PhylomeDB; P48030; -.
TreeFam; TF332938; -.
Reactome; R-MMU-204005; COPII-mediated vesicle transport.
Reactome; R-MMU-5694530; Cargo concentration in the ER.
PMAP-CutDB; P48030; -.
PRO; PR:P48030; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029999; Expressed in 257 organ(s), highest expression level in caudate-putamen.
CleanEx; MM_TGFA; -.
ExpressionAtlas; P48030; baseline and differential.
Genevisible; P48030; MM.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:MGI.
GO; GO:0008083; F:growth factor activity; ISS:HGNC.
GO; GO:0000187; P:activation of MAPK activity; ISS:HGNC.
GO; GO:0001525; P:angiogenesis; IDA:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
GO; GO:0060749; P:mammary gland alveolus development; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0048523; P:negative regulation of cellular process; ISO:MGI.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; ISS:HGNC.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:HGNC.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:HGNC.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR015497; EGF_rcpt_ligand.
PANTHER; PTHR10740; PTHR10740; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; EGF-like domain;
Glycoprotein; Growth factor; Lipoprotein; Membrane; Mitogen;
Palmitate; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 159 Protransforming growth factor alpha.
/FTId=PRO_0000302746.
PROPEP 24 38 Removed in mature form.
/FTId=PRO_0000007758.
CHAIN 39 88 Transforming growth factor alpha.
/FTId=PRO_0000007759.
PROPEP 89 159 Removed in mature form.
/FTId=PRO_0000007760.
TOPO_DOM 24 97 Extracellular. {ECO:0000255}.
TRANSMEM 98 123 Helical. {ECO:0000255}.
TOPO_DOM 124 159 Cytoplasmic. {ECO:0000255}.
DOMAIN 44 83 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
LIPID 152 152 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 153 153 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 59 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 54 70 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 72 81 {ECO:0000255|PROSITE-ProRule:PRU00076}.
SEQUENCE 159 AA; 17018 MW; BE0AE8D89CE7DDFD CRC64;
MVPATGQLAL LALGILLAVC QALENSTSPL SDSPVAAAVV SHFNKCPDSH TQYCFHGTCR
FLVQEEKPAC VCHSGYVGVR CEHADLLAVV AASQKKQAIT ALVVVSIVAL AVLIITCVLI
HCCQLRKHCE WCRALVCRHE KPSALLKGRT ACCHSETVV


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