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Probetacellulin [Cleaved into: Betacellulin (BTC)]

 BTC_HUMAN               Reviewed;         178 AA.
P35070; Q96F48;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
07-NOV-2018, entry version 166.
RecName: Full=Probetacellulin;
Contains:
RecName: Full=Betacellulin;
Short=BTC;
Flags: Precursor;
Name=BTC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=8439318; DOI=10.1006/bbrc.1993.1173;
Sasada R., Ono Y., Taniyama Y., Shing Y., Folkman J., Igarashi K.;
"Cloning and expression of cDNA encoding human betacellulin, a new
member of the EGF family.";
Biochem. Biophys. Res. Commun. 190:1173-1179(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-124.
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION AS EGFR LIGAND.
PubMed=8144591;
Watanabe T., Shintani A., Nakata M., Shing Y., Folkman J.,
Igarashi K., Sasada R.;
"Recombinant human betacellulin. Molecular structure, biological
activities, and receptor interaction.";
J. Biol. Chem. 269:9966-9973(1994).
[4]
TISSUE SPECIFICITY.
PubMed=8919026; DOI=10.3109/08977199609003220;
Seno M., Tada H., Kosaka M., Sasada R., Igarashi K., Shing Y.,
Folkman J., Ueda M., Yamada H.;
"Human betacellulin, a member of the EGF family dominantly expressed
in pancreas and small intestine, is fully active in a monomeric
form.";
Growth Factors 13:181-191(1996).
[5]
FUNCTION, AND INTERACTION WITH EGFR AND ERBB4.
PubMed=8570211;
Riese D.J. II, Bermingham Y., van Raaij T.M., Buckley S.,
Plowman G.D., Stern D.F.;
"Betacellulin activates the epidermal growth factor receptor and erbB-
4, and induces cellular response patterns distinct from those
stimulated by epidermal growth factor or neuregulin-beta.";
Oncogene 12:345-353(1996).
[6]
INTERACTION WITH ERBB4.
PubMed=10867024; DOI=10.1074/jbc.C901015199;
Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C.,
Carraway K.L. III;
"Ligand discrimination in signaling through an ErbB4 receptor
homodimer.";
J. Biol. Chem. 275:19803-19807(2000).
[7]
STRUCTURE BY NMR OF 62-111.
PubMed=12074582; DOI=10.1016/S0006-291X(02)00585-5;
Miura K., Doura H., Aizawa T., Tada H., Seno M., Yamada H., Kawano K.;
"Solution structure of betacellulin, a new member of EGF-family
ligands.";
Biochem. Biophys. Res. Commun. 294:1040-1046(2002).
-!- FUNCTION: Growth factor that binds to EGFR, ERBB4 and other EGF
receptor family members. Potent mitogen for retinal pigment
epithelial cells and vascular smooth muscle cells.
{ECO:0000269|PubMed:8570211}.
-!- SUBUNIT: Monomer. Interacts with EGFR and ERBB4.
{ECO:0000269|PubMed:10867024, ECO:0000269|PubMed:8570211}.
-!- INTERACTION:
Q96IJ6:GMPPA; NbExp=6; IntAct=EBI-6590057, EBI-750953;
Q15323:KRT31; NbExp=5; IntAct=EBI-6590057, EBI-948001;
P26447:S100A4; NbExp=2; IntAct=EBI-6590057, EBI-717058;
O43765:SGTA; NbExp=5; IntAct=EBI-6590057, EBI-347996;
-!- SUBCELLULAR LOCATION: Betacellulin: Secreted, extracellular space.
-!- SUBCELLULAR LOCATION: Probetacellulin: Cell membrane; Single-pass
type I membrane protein.
-!- TISSUE SPECIFICITY: Synthesized in several tissues and tumor
cells. Predominantly expressed in pancreas and small intestine.
{ECO:0000269|PubMed:8919026}.
-----------------------------------------------------------------------
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EMBL; S55606; AAB25452.1; -; mRNA.
EMBL; BC011618; AAH11618.1; -; mRNA.
CCDS; CCDS3566.1; -.
PIR; JC1467; JC1467.
RefSeq; NP_001303892.1; NM_001316963.1.
RefSeq; NP_001720.1; NM_001729.3.
RefSeq; XP_011530513.1; XM_011532211.1.
UniGene; Hs.591704; -.
UniGene; Hs.710156; -.
PDB; 1IOX; NMR; -; A=62-111.
PDB; 1IP0; NMR; -; A=62-111.
PDBsum; 1IOX; -.
PDBsum; 1IP0; -.
ProteinModelPortal; P35070; -.
SMR; P35070; -.
BioGrid; 107150; 20.
DIP; DIP-5768N; -.
IntAct; P35070; 7.
MINT; P35070; -.
STRING; 9606.ENSP00000379092; -.
PhosphoSitePlus; P35070; -.
SwissPalm; P35070; -.
BioMuta; BTC; -.
DMDM; 461653; -.
PaxDb; P35070; -.
PeptideAtlas; P35070; -.
PRIDE; P35070; -.
ProteomicsDB; 54977; -.
DNASU; 685; -.
Ensembl; ENST00000395743; ENSP00000379092; ENSG00000174808.
GeneID; 685; -.
KEGG; hsa:685; -.
UCSC; uc003hig.3; human.
CTD; 685; -.
DisGeNET; 685; -.
EuPathDB; HostDB:ENSG00000174808.11; -.
GeneCards; BTC; -.
HGNC; HGNC:1121; BTC.
MIM; 600345; gene.
neXtProt; NX_P35070; -.
OpenTargets; ENSG00000174808; -.
PharmGKB; PA25442; -.
eggNOG; ENOG410IWUI; Eukaryota.
eggNOG; ENOG41126JP; LUCA.
GeneTree; ENSGT00730000110951; -.
HOGENOM; HOG000237352; -.
HOVERGEN; HBG004905; -.
InParanoid; P35070; -.
KO; K09783; -.
OMA; PKRKGHF; -.
OrthoDB; EOG091G0RK4; -.
PhylomeDB; P35070; -.
TreeFam; TF332938; -.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1236394; Signaling by ERBB4.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling.
Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
SignaLink; P35070; -.
SIGNOR; P35070; -.
ChiTaRS; BTC; human.
EvolutionaryTrace; P35070; -.
GenomeRNAi; 685; -.
PRO; PR:P35070; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000174808; Expressed in 145 organ(s), highest expression level in lower esophagus.
CleanEx; HS_BTC; -.
ExpressionAtlas; P35070; baseline and differential.
Genevisible; P35070; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl.
GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR015497; EGF_rcpt_ligand.
PANTHER; PTHR10740; PTHR10740; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Growth factor; Membrane; Mitogen;
Polymorphism; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 31 {ECO:0000250}.
CHAIN 32 178 Probetacellulin.
/FTId=PRO_0000300685.
CHAIN 32 111 Betacellulin.
/FTId=PRO_0000007490.
PROPEP 112 178 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000007491.
TOPO_DOM 32 118 Extracellular. {ECO:0000255}.
TRANSMEM 119 139 Helical. {ECO:0000255}.
TOPO_DOM 140 178 Cytoplasmic. {ECO:0000255}.
DOMAIN 65 105 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
COMPBIAS 146 154 Arg/Lys-rich (basic).
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 69 82
DISULFID 77 93
DISULFID 95 104
VARIANT 7 7 C -> G (in dbSNP:rs28549760).
/FTId=VAR_029307.
VARIANT 44 44 L -> F (in dbSNP:rs56320257).
/FTId=VAR_061151.
VARIANT 124 124 L -> M (in dbSNP:rs11938093).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_029308.
STRAND 66 68 {ECO:0000244|PDB:1IP0}.
HELIX 71 73 {ECO:0000244|PDB:1IOX}.
STRAND 82 85 {ECO:0000244|PDB:1IOX}.
TURN 86 89 {ECO:0000244|PDB:1IOX}.
STRAND 90 93 {ECO:0000244|PDB:1IOX}.
TURN 101 104 {ECO:0000244|PDB:1IOX}.
STRAND 106 108 {ECO:0000244|PDB:1IP0}.
SEQUENCE 178 AA; 19746 MW; 27AC77BD92001F0F CRC64;
MDRAARCSGA SSLPLLLALA LGLVILHCVV ADGNSTRSPE TNGLLCGDPE ENCAATTTQS
KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF YLRGDRGQIL
VICLIAVMVV FIILVIGVCT CCHPLRKRRK RKKKEEEMET LGKDITPINE DIEETNIA


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