TGFA_PIG
ID TGFA_PIG Reviewed; 160 AA.
AC Q06922;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 125.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8280083; DOI=10.1042/bj2960837;
RA Vaughan T.J., James P.S., Pascall J.C., Brown K.D.;
RT "Molecular cloning and tissue distribution of pig transforming growth
RT factor alpha.";
RL Biochem. J. 296:837-842(1993).
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 {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: [Transforming growth factor alpha]: Secreted,
CC extracellular space {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protransforming growth factor alpha]: Cell
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
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DR EMBL; X71014; CAA50333.1; -; mRNA.
DR PIR; S39795; S39795.
DR RefSeq; NP_999416.1; NM_214251.1.
DR AlphaFoldDB; Q06922; -.
DR BMRB; Q06922; -.
DR SMR; Q06922; -.
DR STRING; 9823.ENSSSCP00000008889; -.
DR PRIDE; Q06922; -.
DR GeneID; 397484; -.
DR KEGG; ssc:397484; -.
DR CTD; 7039; -.
DR eggNOG; ENOG502S1CF; Eukaryota.
DR InParanoid; Q06922; -.
DR OrthoDB; 1401257at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:HGNC.
DR GO; GO:0008083; F:growth factor activity; ISS:HGNC-UCL.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
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 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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Growth factor; Lipoprotein; Membrane; Mitogen; Palmitate;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..160
FT /note="Protransforming growth factor alpha"
FT /id="PRO_0000302747"
FT PROPEP 24..39
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007761"
FT CHAIN 40..89
FT /note="Transforming growth factor alpha"
FT /id="PRO_0000007762"
FT PROPEP 90..160
FT /note="Removed in mature form"
FT /id="PRO_0000007763"
FT TOPO_DOM 24..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 125..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..83
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT LIPID 153
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 154
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 55..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 73..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 160 AA; 17056 MW; 14E2900710333AC9 CRC64;
MVPSAGQFAL FALGILLAVC QALENSTSAL SADPPIAAAV VSHFNDCPDS HSQFCFHGTC
RFLVQEDKPA CVCHSGYVGA RCEHADLLAV VAASQKKQAI TALVVVSIVA LAVLIITCVL
IHCCQVRKHC EWCRALICRH EKPSALLKGR TACCHSETVV
