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Database: UniProt
Entry: P98138
LinkDB: P98138
Original site: P98138 
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   10-APR-2019, entry version 90.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   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
RT   cell secretion: structural requirements for activity.";
RL   Regul. Pept. 43:37-47(1993).
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 (By similarity). Inhibitor of acid secretion. Inhibitor of
CC       aminopyrine uptake in parietal cells (in vitro). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Gastric parietal cells.
DR   EMBL; M86827; AAA73200.1; -; mRNA.
DR   PIR; A48545; A48545.
DR   UniGene; Ocu.6422; -.
DR   ProteinModelPortal; P98138; -.
DR   SMR; P98138; -.
DR   STRING; 9986.ENSOCUP00000026700; -.
DR   eggNOG; ENOG410IVW5; Eukaryota.
DR   eggNOG; ENOG4111Z4I; LUCA.
DR   HOGENOM; HOG000013036; -.
DR   InParanoid; P98138; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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; 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   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; EGF-like domain; Growth factor;
KW   Mitogen; Reference proteome; Secreted.
FT   CHAIN        <1    >50       Transforming growth factor alpha.
FT                                /FTId=PRO_0000055635.
FT   DOMAIN        4     44       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID      8     21       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     16     32       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     34     43       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   NON_TER       1      1
FT   NON_TER      50     50
SQ   SEQUENCE   50 AA;  5565 MW;  BDD508F4053625DB CRC64;
     VVSHFNQCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA
//
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