Database: UniProt
Entry: P98135
LinkDB: P98135
Original site: P98135 
ID   TGFA_SHEEP              Reviewed;         133 AA.
AC   P98135;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   10-APR-2019, entry version 94.
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; Fragment;
GN   Name=TGFA; Synonyms=TGF-A;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RC   STRAIN=Merino; TISSUE=Dorsal skin;
RX   PubMed=7749621; DOI=10.1016/0305-0491(94)00208-C;
RA   Sutton R., Ward W.G., Raphael K.A., Cam G.R.;
RT   "Growth factor expression in skin during wool follicle development.";
RL   Comp. Biochem. Physiol. 110B:697-705(1995).
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. {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. Interacts (via cytoplasmic C-terminal
CC       domain) with NKD2 (By 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}.
CC   -!- DEVELOPMENTAL STAGE: Wool follicle development.
DR   EMBL; L36232; AAA53113.1; -; mRNA.
DR   UniGene; Oar.396; -.
DR   ProteinModelPortal; P98135; -.
DR   SMR; P98135; -.
DR   STRING; 9940.ENSOARP00000011905; -.
DR   HOVERGEN; HBG000330; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; ISS:HGNC.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:HGNC.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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   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   Cell membrane; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Growth factor; Membrane; Mitogen; Reference proteome;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24   >133       Protransforming growth factor alpha.
FT                                /FTId=PRO_0000302749.
FT   PROPEP       24     38       Removed in mature form.
FT                                /FTId=PRO_0000007767.
FT   CHAIN        39     88       Transforming growth factor alpha.
FT                                /FTId=PRO_0000007768.
FT   PROPEP       89   >133       Removed in mature form.
FT                                /FTId=PRO_0000007769.
FT   TOPO_DOM     24     97       Extracellular. {ECO:0000255}.
FT   TRANSMEM     98    120       Helical. {ECO:0000255}.
FT   TOPO_DOM    121   >133       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       42     82       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
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   NON_TER     133    133
SQ   SEQUENCE   133 AA;  14027 MW;  F9F8E03BAA28AFB1 CRC64;
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