BTC_BOVIN
ID BTC_BOVIN Reviewed; 178 AA.
AC Q9TTC5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probetacellulin;
DE Contains:
DE RecName: Full=Betacellulin;
DE Short=BTC;
DE Flags: Precursor;
GN Name=BTC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney, and Milk;
RX PubMed=10585857; DOI=10.1042/bj3440713;
RA Dunbar A.J., Goddard C., Priebe I.K.P., Belford D.A.;
RT "Identification of betacellulin as a major peptide growth factor in milk:
RT purification, characterization, and molecular cloning of bovine
RT betacellulin.";
RL Biochem. J. 344:713-721(1999).
CC -!- FUNCTION: Growth factor that binds to EGFR, ERBB4 and other EGF
CC receptor family members. Potent mitogen for retinal pigment epithelial
CC cells and vascular smooth muscle cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with EGFR and ERBB4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Betacellulin]: Secreted, extracellular space
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Probetacellulin]: Cell membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues, including the
CC mammary gland.
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DR EMBL; AF140597; AAF15401.1; -; mRNA.
DR AlphaFoldDB; Q9TTC5; -.
DR SMR; Q9TTC5; -.
DR STRING; 9913.ENSBTAP00000005549; -.
DR PaxDb; Q9TTC5; -.
DR eggNOG; ENOG502RZHQ; Eukaryota.
DR InParanoid; Q9TTC5; -.
DR Proteomes; UP000009136; 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; IEA:InterPro.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR015497; EGF_rcpt_ligand.
DR PANTHER; PTHR10740; PTHR10740; 1.
DR Pfam; PF00008; EGF; 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..31
FT /evidence="ECO:0000250"
FT CHAIN 32..178
FT /note="Probetacellulin"
FT /id="PRO_0000300684"
FT CHAIN 32..111
FT /note="Betacellulin"
FT /id="PRO_0000007488"
FT PROPEP 112..178
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007489"
FT TOPO_DOM 32..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 65..105
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 77..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 95..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 178 AA; 19640 MW; 158B67B24A64E0CB CRC64;
MARAAPGSGA SPLPLLPALA LGLVILHCVV ADGNSTRSPE DDGLLCGDHA ENCPATTTQP
KRRGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYA GARCERVDLF YLRGDRGQIL
VICLIAVMVI FIILVVSICT CCHPLRKRRK RRKKEEEMET LGKDITPIND DIQETSIA