TGFA_MACMU
ID TGFA_MACMU Reviewed; 121 AA.
AC P55244;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
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;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=7545971; DOI=10.1159/000126769;
RA Ma Y.J., Costa M.E., Ojeda S.R.;
RT "Developmental expression of the genes encoding transforming growth factor
RT alpha and its receptor in the hypothalamus of female rhesus macaques.";
RL Neuroendocrinology 60:346-359(1994).
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: Hypothalamus. {ECO:0000269|PubMed:7545971}.
CC -!- DEVELOPMENTAL STAGE: Levels in the medial basal hypothalamus and
CC preoptic area are elevated during neonatal life (1 week-6 months),
CC decrease during juvenile development (8-18 months) and markedly
CC increase during the expected time of puberty (30-36 months).
CC {ECO:0000269|PubMed:7545971}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S75913; AAB33094.1; -; mRNA.
DR PIR; I58134; I58134.
DR AlphaFoldDB; P55244; -.
DR BMRB; P55244; -.
DR STRING; 9544.ENSMMUP00000013878; -.
DR eggNOG; ENOG502RYAF; Eukaryota.
DR InParanoid; P55244; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; IEA:UniProt.
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:HGNC.
DR GO; GO:0008083; F:growth factor activity; ISS:HGNC-UCL.
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-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..1
FT /evidence="ECO:0000255"
FT CHAIN 2..121
FT /note="Protransforming growth factor alpha"
FT /id="PRO_0000302745"
FT PROPEP 2..16
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007755"
FT CHAIN 17..66
FT /note="Transforming growth factor alpha"
FT /id="PRO_0000007756"
FT PROPEP 67..121
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007757"
FT TOPO_DOM 2..75
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..101
FT /note="Helical"
FT /evidence="ECO:0000250"
FT DOMAIN 20..60
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 32..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 50..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT NON_TER 121
SQ SEQUENCE 121 AA; 13182 MW; 463031DFBBC14816 CRC64;
LENSTSLLSD PPVAAAVVSH FNDCPDSHTQ FCFHGTCRFL VQEDRPACVC HSGYVGARCE
HADLLAVVAA SQKKQAITAL VVVSIVALAV LIITCVLIHC CQVRKHCEWC RALICRHEKP
S
