Database: UniProt
Entry: P01134
LinkDB: P01134
Original site: P01134 
ID   TGFA_RAT                Reviewed;         159 AA.
AC   P01134; Q63749;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   13-FEB-2019, entry version 150.
DE   RecName: Full=Protransforming growth factor alpha;
DE   Contains:
DE     RecName: Full=Transforming growth factor alpha;
DE              Short=TGF-alpha;
DE     AltName: Full=EGF-like TGF;
DE              Short=ETGF;
DE     AltName: Full=TGF type 1;
DE   Flags: Precursor;
GN   Name=Tgfa;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RX   PubMed=3855503; DOI=10.1038/313489a0;
RA   Lee D.C., Rose T.M., Webb N.R., Todaro G.J.;
RT   "Cloning and sequence analysis of a cDNA for rat transforming growth
RT   factor-alpha.";
RL   Nature 313:489-491(1985).
RN   [2]
RX   PubMed=2325647; DOI=10.1128/MCB.10.5.2111;
RA   Blasband A.J., Rogers K.T., Chen X., Azizkhan J.C., Lee D.C.;
RT   "Characterization of the rat transforming growth factor alpha gene and
RT   identification of promoter sequences.";
RL   Mol. Cell. Biol. 10:2111-2121(1990).
RN   [3]
RX   PubMed=6320373; DOI=10.1126/science.6320373;
RA   Marquardt H., Hunkapiller M.W., Hood L.E., Todaro G.J.;
RT   "Rat transforming growth factor type 1: structure and relation to
RT   epidermal growth factor.";
RL   Science 223:1079-1082(1984).
RN   [4]
RX   PubMed=6605968;
RA   Massague J.;
RT   "Epidermal growth factor-like transforming growth factor. I.
RT   Isolation, chemical characterization, and potentiation by other
RT   transforming factors from feline sarcoma virus-transformed rat
RT   cells.";
RL   J. Biol. Chem. 258:13606-13613(1983).
CC   -!- FUNCTION: TGF alpha is a mitogenic polypeptide that is able to
CC       bind to the EGF receptor/EGFR and to act synergistically with TGF
CC       beta to promote anchorage-independent cell proliferation in soft
CC       agar.
CC   -!- SUBUNIT: Interacts with the PDZ domains of MAGI3, SDCBP and SNTA1.
CC       The interaction with SDCBP, is required for the targeting to the
CC       cell surface. In the endoplasmic reticulum, in its immature form
CC       (i.e. with a prosegment and lacking full N-glycosylation),
CC       interacts with CNIH. In the Golgi apparatus, may form a complex
CC       with CNIH and GORASP2. Interacts (via cytoplasmic C-terminal
CC       domain) with NKD2 (By similarity). {ECO:0000250}.
CC       Q9H190:SDCBP2 (xeno); NbExp=6; IntAct=EBI-16418721, EBI-742426;
CC   -!- SUBCELLULAR LOCATION: Transforming growth factor alpha: Secreted,
CC       extracellular space.
CC   -!- SUBCELLULAR LOCATION: Protransforming growth factor alpha: Cell
CC       membrane; Single-pass type I membrane protein.
DR   EMBL; X02004; CAA26036.1; -; mRNA.
DR   EMBL; M31075; AAA42234.1; -; Genomic_DNA.
DR   EMBL; M31076; AAA42233.1; -; mRNA.
DR   PIR; A93356; WFRT1.
DR   PIR; I57497; I57497.
DR   RefSeq; NP_036803.1; NM_012671.2.
DR   UniGene; Rn.9952; -.
DR   ProteinModelPortal; P01134; -.
DR   SMR; P01134; -.
DR   IntAct; P01134; 2.
DR   STRING; 10116.ENSRNOP00000054248; -.
DR   PaxDb; P01134; -.
DR   PRIDE; P01134; -.
DR   Ensembl; ENSRNOT00000057441; ENSRNOP00000054248; ENSRNOG00000016182.
DR   GeneID; 24827; -.
DR   KEGG; rno:24827; -.
DR   UCSC; RGD:3849; rat.
DR   CTD; 7039; -.
DR   RGD; 3849; Tgfa.
DR   eggNOG; ENOG410IVW5; Eukaryota.
DR   eggNOG; ENOG4111Z4I; LUCA.
DR   GeneTree; ENSGT00940000160058; -.
DR   HOGENOM; HOG000013036; -.
DR   HOVERGEN; HBG000330; -.
DR   InParanoid; P01134; -.
DR   KO; K08774; -.
DR   OrthoDB; 1401257at2759; -.
DR   PhylomeDB; P01134; -.
DR   TreeFam; TF332938; -.
DR   Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-RNO-177929; Signaling by EGFR.
DR   Reactome; R-RNO-179812; GRB2 events in EGFR signaling.
DR   Reactome; R-RNO-180292; GAB1 signalosome.
DR   Reactome; R-RNO-180336; SHC1 events in EGFR signaling.
DR   Reactome; R-RNO-182971; EGFR downregulation.
DR   Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR   Reactome; R-RNO-212718; EGFR interacts with phospholipase C-gamma.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:P01134; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000016182; Expressed in 10 organ(s), highest expression level in brain.
DR   Genevisible; P01134; RN.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:RGD.
DR   GO; GO:0008083; F:growth factor activity; ISS:HGNC.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:HGNC.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0048523; P:negative regulation of cellular process; IDA:RGD.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; ISS:HGNC.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:HGNC.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:HGNC.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0042060; P:wound healing; IEP:RGD.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015497; EGF_rcpt_ligand.
DR   PANTHER; PTHR10740; PTHR10740; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Growth factor;
KW   Lipoprotein; Membrane; Mitogen; Palmitate; Reference proteome;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    159       Protransforming growth factor alpha.
FT                                /FTId=PRO_0000302748.
FT   PROPEP       24     38       Removed in mature form.
FT                                /FTId=PRO_0000007764.
FT   CHAIN        39     88       Transforming growth factor alpha.
FT                                /FTId=PRO_0000007765.
FT   PROPEP       89    159       Removed in mature form.
FT                                /FTId=PRO_0000007766.
FT   TOPO_DOM     24     97       Extracellular. {ECO:0000255}.
FT   TRANSMEM     98    123       Helical. {ECO:0000255}.
FT   TOPO_DOM    124    159       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       42     82       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   LIPID       152    152       S-palmitoyl cysteine. {ECO:0000250}.
FT   LIPID       153    153       S-palmitoyl cysteine. {ECO:0000250}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     46     59       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     54     70       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     72     81       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT     28     28       S -> P (in Ref. 1; CAA26036).
FT                                {ECO:0000305}.
SQ   SEQUENCE   159 AA;  16960 MW;  E9664EF04DFCF4D5 CRC64;
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