TGFA_RAT
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 03-AUG-2022, entry version 167.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2325647; DOI=10.1128/mcb.10.5.2111-2121.1990;
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]
RP PROTEIN SEQUENCE OF 39-88.
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 epidermal
RT growth factor.";
RL Science 223:1079-1082(1984).
RN [4]
RP PROTEIN SEQUENCE OF 39-67.
RX PubMed=6605968; DOI=10.1016/s0021-9258(17)43958-5;
RA Massague J.;
RT "Epidermal growth factor-like transforming growth factor. I. Isolation,
RT chemical characterization, and potentiation by other transforming factors
RT from feline sarcoma virus-transformed rat cells.";
RL J. Biol. Chem. 258:13606-13613(1983).
CC -!- FUNCTION: TGF alpha is a mitogenic polypeptide that is able to bind to
CC the EGF receptor/EGFR and to act synergistically with TGF beta to
CC promote anchorage-independent cell proliferation in soft agar.
CC -!- SUBUNIT: Interacts with the PDZ domains of MAGI3, SDCBP and SNTA1. The
CC interaction with SDCBP, is required for the targeting to the cell
CC surface. In the endoplasmic reticulum, in its immature form (i.e. with
CC a prosegment and lacking full N-glycosylation), interacts with CNIH. In
CC the Golgi apparatus, may form a complex with CNIH and GORASP2.
CC Interacts (via cytoplasmic C-terminal domain) with NKD2 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P01134; 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.
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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 AlphaFoldDB; P01134; -.
DR SMR; P01134; -.
DR IntAct; P01134; 2.
DR STRING; 10116.ENSRNOP00000054248; -.
DR GlyGen; P01134; 1 site.
DR PaxDb; P01134; -.
DR PRIDE; P01134; -.
DR GeneID; 24827; -.
DR KEGG; rno:24827; -.
DR UCSC; RGD:3849; rat.
DR CTD; 7039; -.
DR RGD; 3849; Tgfa.
DR VEuPathDB; HostDB:ENSRNOG00000016182; -.
DR eggNOG; ENOG502RYAF; Eukaryota.
DR HOGENOM; CLU_109645_1_0_1; -.
DR InParanoid; P01134; -.
DR OMA; SACCHSE; -.
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 Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P01134; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000016182; Expressed in ovary and 15 other tissues.
DR Genevisible; P01134; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
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:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:RGD.
DR GO; GO:0008083; F:growth factor activity; ISS:HGNC-UCL.
DR GO; GO:0048018; F:receptor ligand activity; ISO:RGD.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; ISO:RGD.
DR GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
DR GO; GO:0060749; P:mammary gland alveolus development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic 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-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:HGNC-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:HGNC-UCL.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:HGNC-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Growth factor; Lipoprotein; Membrane; Mitogen; Palmitate;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..159
FT /note="Protransforming growth factor alpha"
FT /id="PRO_0000302748"
FT PROPEP 24..38
FT /note="Removed in mature form"
FT /id="PRO_0000007764"
FT CHAIN 39..88
FT /note="Transforming growth factor alpha"
FT /id="PRO_0000007765"
FT PROPEP 89..159
FT /note="Removed in mature form"
FT /id="PRO_0000007766"
FT TOPO_DOM 24..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..82
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT LIPID 152
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 153
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 54..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 72..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 28
FT /note="S -> P (in Ref. 1; CAA26036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 16960 MW; E9664EF04DFCF4D5 CRC64;
MVPAAGQLAL LALGILVAVC QALENSTSPL SDSPVAAAVV SHFNKCPDSH TQYCFHGTCR
FLVQEEKPAC VCHSGYVGVR CEHADLLAVV AASQKKQAIT ALVVVSIVAL AVLIITCVLI
HCCQVRKHCE WCRALVCRHE KPSALLKGRT ACCHSETVV
