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   25-MAY-2022, entry version 105.
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; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 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}.
CC   -!- TISSUE SPECIFICITY: Skin.
CC   -!- DEVELOPMENTAL STAGE: Wool follicle development.
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DR   EMBL; L36232; AAA53113.1; -; mRNA.
DR   AlphaFoldDB; P98135; -.
DR   SMR; P98135; -.
DR   STRING; 9940.ENSOARP00000011905; -.
DR   eggNOG; ENOG502RYAF; Eukaryota.
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:HGNC.
DR   GO; GO:0008083; F:growth factor activity; ISS:HGNC-UCL.
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-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; Membrane; Mitogen; Reference proteome; Secreted; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..>133
FT                   /note="Protransforming growth factor alpha"
FT                   /id="PRO_0000302749"
FT   PROPEP          24..38
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000007767"
FT   CHAIN           39..88
FT                   /note="Transforming growth factor alpha"
FT                   /id="PRO_0000007768"
FT   PROPEP          89..>133
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000007769"
FT   TOPO_DOM        24..97
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..>133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..82
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
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   NON_TER         133
SQ   SEQUENCE   133 AA;  14027 MW;  F9F8E03BAA28AFB1 CRC64;
     MVPSAGQLAL FALGIFLAVC QALENSTSAL SDPPVAAAVV SHFNDCPDSH TQFCFHGTCR
     FLLQEEKPAC VCHSGYVGAR CEHADLLAVV AASQKKQAIT ALVVVTIVAL AVLIITCVLI
     HCCEVRKHSV VVP