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Database: UniProt
Entry: Q06922
LinkDB: Q06922
Original site: Q06922 
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   10-APR-2019, entry version 113.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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
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}.
DR   EMBL; X71014; CAA50333.1; -; mRNA.
DR   PIR; S39795; S39795.
DR   RefSeq; NP_999416.1; NM_214251.1.
DR   UniGene; Ssc.16220; -.
DR   UniGene; Ssc.94427; -.
DR   ProteinModelPortal; Q06922; -.
DR   SMR; Q06922; -.
DR   STRING; 9823.ENSSSCP00000008889; -.
DR   PRIDE; Q06922; -.
DR   GeneID; 397484; -.
DR   KEGG; ssc:397484; -.
DR   CTD; 7039; -.
DR   HOGENOM; HOG000013036; -.
DR   HOVERGEN; HBG000330; -.
DR   InParanoid; Q06922; -.
DR   KO; K08774; -.
DR   OrthoDB; 1401257at2759; -.
DR   Proteomes; UP000008227; 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: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: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.
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; Lipoprotein; Membrane; Mitogen;
KW   Palmitate; Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000250}.
FT   CHAIN        24    160       Protransforming growth factor alpha.
FT                                /FTId=PRO_0000302747.
FT   PROPEP       24     39       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000007761.
FT   CHAIN        40     89       Transforming growth factor alpha.
FT                                /FTId=PRO_0000007762.
FT   PROPEP       90    160       Removed in mature form.
FT                                /FTId=PRO_0000007763.
FT   TOPO_DOM     24     98       Extracellular. {ECO:0000255}.
FT   TRANSMEM     99    124       Helical. {ECO:0000250}.
FT   TOPO_DOM    125    160       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       43     83       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   LIPID       153    153       S-palmitoyl cysteine. {ECO:0000250}.
FT   LIPID       154    154       S-palmitoyl cysteine. {ECO:0000250}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47     60       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     55     71       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     73     82       {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
//
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