ID   TGFA_RABIT              Reviewed;          50 AA.
AC   P98138;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 99.
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: Fragment;
GN   Name=TGFA;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8426908; DOI=10.1016/0167-0115(93)90405-w;
RA   Goldenring J.R., Tsunoda Y., Stoch S.A., Coffey R.J., Modlin I.M.;
RT   "Transforming growth factor-alpha (TGF alpha) inhibition of parietal cell
RT   secretion: structural requirements for activity.";
RL   Regul. Pept. 43:37-47(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 (By
CC       similarity). Inhibitor of acid secretion. Inhibitor of aminopyrine
CC       uptake in parietal cells (in vitro). {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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Gastric parietal cells.
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DR   EMBL; M86827; AAA73200.1; -; mRNA.
DR   PIR; A48545; A48545.
DR   AlphaFoldDB; P98138; -.
DR   BMRB; P98138; -.
DR   SMR; P98138; -.
DR   STRING; 9986.ENSOCUP00000026700; -.
DR   eggNOG; ENOG502RYAF; Eukaryota.
DR   InParanoid; P98138; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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   Disulfide bond; EGF-like domain; Growth factor; Mitogen;
KW   Reference proteome; Secreted.
FT   CHAIN           <1..>50
FT                   /note="Transforming growth factor alpha"
FT                   /id="PRO_0000055635"
FT   DOMAIN          4..44
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        8..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        16..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        34..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT   NON_TER         50
SQ   SEQUENCE   50 AA;  5565 MW;  BDD508F4053625DB CRC64;
     VVSHFNQCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA