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Database: UniProt
Entry: Q9TTC5
LinkDB: Q9TTC5
Original site: Q9TTC5 
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   24-JAN-2024, entry version 117.
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   GlyCosmos; Q9TTC5; 1 site, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000005549; -.
DR   eggNOG; ENOG502RZHQ; Eukaryota.
DR   InParanoid; Q9TTC5; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
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:0045840; P:positive regulation of mitotic nuclear division; IBA:GO_Central.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   PANTHER; PTHR10740:SF3; PROBETACELLULIN; 1.
DR   PANTHER; PTHR10740; TRANSFORMING GROWTH FACTOR ALPHA; 1.
DR   PRINTS; PR00009; EGFTGF.
DR   SUPFAM; SSF57196; EGF/Laminin; 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
//
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