HBEGF_PIG
ID HBEGF_PIG Reviewed; 208 AA.
AC Q01580;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Proheparin-binding EGF-like growth factor;
DE Contains:
DE RecName: Full=Heparin-binding EGF-like growth factor;
DE Short=HB-EGF;
DE Short=HBEGF;
DE Flags: Precursor;
GN Name=HBEGF; Synonyms=DTR, HEGFL;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pascall J.C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-182.
RC STRAIN=Large white; TISSUE=Heart;
RX PubMed=1445231; DOI=10.1042/bj2870681;
RA Vaughan T.J., Pascall J.C., Brown K.D.;
RT "Tissue distribution of mRNA for heparin-binding epidermal growth factor.";
RL Biochem. J. 287:681-684(1992).
CC -!- FUNCTION: Growth factor that mediates its effects via EGFR, ERBB2 and
CC ERBB4. Required for normal cardiac valve formation and normal heart
CC function. Promotes smooth muscle cell proliferation. May be involved in
CC macrophage-mediated cellular proliferation. It is mitogenic for
CC fibroblasts, but not endothelial cells. It is able to bind EGF
CC receptor/EGFR with higher affinity than EGF itself and is a far more
CC potent mitogen for smooth muscle cells than EGF. Also acts as a
CC diphtheria toxin receptor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FBLN1. Interacts with EGFR and ERBB4 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Heparin-binding EGF-like growth factor]:
CC Secreted, extracellular space {ECO:0000250}. Note=Mature HB-EGF is
CC released into the extracellular space and probably binds to a receptor.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Proheparin-binding EGF-like growth factor]: Cell
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Macrophages, midbrain, cerebellum, hypothalamus,
CC cerebral cortex, bulbourethral gland, lung, heart ventricle, kidney,
CC skin, prostate, seminal vesicle, testis; at low levels in lymph node,
CC thymus, spleen; not detected in pituitary, olfactory bulb, thyroid,
CC duodenum, pancreas, liver, submaxillary gland.
CC -!- PTM: O-glycosylated. {ECO:0000305}.
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DR EMBL; Y15731; CAA75740.1; -; mRNA.
DR EMBL; X67295; CAA47709.1; -; mRNA.
DR PIR; S27162; S27162.
DR RefSeq; NP_999464.1; NM_214299.1.
DR AlphaFoldDB; Q01580; -.
DR SMR; Q01580; -.
DR MINT; Q01580; -.
DR STRING; 9823.ENSSSCP00000015279; -.
DR PaxDb; Q01580; -.
DR Ensembl; ENSSSCT00000015692; ENSSSCP00000015279; ENSSSCG00000014362.
DR Ensembl; ENSSSCT00015005594; ENSSSCP00015002232; ENSSSCG00015004214.
DR Ensembl; ENSSSCT00025065260; ENSSSCP00025027827; ENSSSCG00025047977.
DR Ensembl; ENSSSCT00030045257; ENSSSCP00030020347; ENSSSCG00030032732.
DR Ensembl; ENSSSCT00035103018; ENSSSCP00035044010; ENSSSCG00035075778.
DR Ensembl; ENSSSCT00040085561; ENSSSCP00040037443; ENSSSCG00040062792.
DR Ensembl; ENSSSCT00055006535; ENSSSCP00055005145; ENSSSCG00055003344.
DR Ensembl; ENSSSCT00060014326; ENSSSCP00060005558; ENSSSCG00060010975.
DR Ensembl; ENSSSCT00065071021; ENSSSCP00065030954; ENSSSCG00065051871.
DR Ensembl; ENSSSCT00070000161; ENSSSCP00070000130; ENSSSCG00070000111.
DR GeneID; 397564; -.
DR KEGG; ssc:397564; -.
DR CTD; 1839; -.
DR VGNC; VGNC:88792; HBEGF.
DR eggNOG; ENOG502S0ZP; Eukaryota.
DR GeneTree; ENSGT00940000156901; -.
DR HOGENOM; CLU_096527_2_0_1; -.
DR InParanoid; Q01580; -.
DR OMA; YSYDHTT; -.
DR OrthoDB; 1348306at2759; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000014362; Expressed in longissimus lumborum muscle and 41 other tissues.
DR ExpressionAtlas; Q01580; baseline and differential.
DR Genevisible; Q01580; SS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IEA:Ensembl.
DR GO; GO:0038135; P:ERBB2-ERBB4 signaling pathway; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
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; Heparin-binding; Membrane; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..208
FT /note="Proheparin-binding EGF-like growth factor"
FT /id="PRO_0000302805"
FT PROPEP 24..62
FT /evidence="ECO:0000250"
FT /id="PRO_0000007617"
FT CHAIN 63..148
FT /note="Heparin-binding EGF-like growth factor"
FT /id="PRO_0000007618"
FT PROPEP 149..208
FT /note="C-terminal"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007619"
FT TOPO_DOM 24..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..144
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 37..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 108..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 116..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 134..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 208 AA; 22986 MW; 0A7DA97AE30C8967 CRC64;
MKLLPSVVLK LFLAAVFSAL VTGESLERLR RGLADGTSNL VSPTESTDQL LPPGGGRGRE
VLDLEEADLD LLRADFSSKP QALATPSKEE RGKRKKKGKG LGKKRDPCLR KYKDFCIHGE
CKYVKELRAP SCICHPGYHG ERCHGLSLPV KNRLYTYDHT TILAVVAVVL SSVCLLVIVG
LLMFRYHRRG GYDVENEEKV KLGVTASH
