FGF7_PIG
ID FGF7_PIG Reviewed; 194 AA.
AC Q9N198;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Fibroblast growth factor 7;
DE Short=FGF-7;
DE AltName: Full=Heparin-binding growth factor 7;
DE Short=HBGF-7;
DE AltName: Full=Keratinocyte growth factor;
DE Short=KGF;
DE Flags: Precursor;
GN Name=FGF7;
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].
RC TISSUE=Endometrium;
RX PubMed=10819782; DOI=10.1095/biolreprod62.6.1772;
RA Ka H., Spencer T.E., Johnson G.A., Bazer F.W.;
RT "Keratinocyte growth factor: expression by endometrial epithelia of the
RT porcine uterus.";
RL Biol. Reprod. 62:1772-1778(2000).
CC -!- FUNCTION: Plays an important role in the regulation of embryonic
CC development, cell proliferation and cell differentiation. Required for
CC normal branching morphogenesis. Growth factor active on keratinocytes.
CC Possible major paracrine effector of normal epithelial cell
CC proliferation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FGFBP1. Interacts with FGFR2. Affinity between
CC fibroblast growth factors (FGFs) and their receptors is increased by
CC heparan sulfate glycosaminoglycans that function as coreceptors (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; AF217463; AAF26734.1; -; mRNA.
DR AlphaFoldDB; Q9N198; -.
DR SMR; Q9N198; -.
DR STRING; 9823.ENSSSCP00000005010; -.
DR PaxDb; Q9N198; -.
DR PRIDE; Q9N198; -.
DR eggNOG; KOG3885; Eukaryota.
DR InParanoid; Q9N198; -.
DR ChiTaRS; FGF7; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005104; F:fibroblast 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; IEA:UniProtKB-KW.
DR GO; GO:0005111; F:type 2 fibroblast growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; IBA:GO_Central.
DR GO; GO:0050918; P:positive chemotaxis; 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:0050679; P:positive regulation of epithelial cell proliferation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028247; FGF7.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF20; PTHR11486:SF20; 1.
DR Pfam; PF00167; FGF; 1.
DR PRINTS; PR00263; HBGFFGF.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00247; HBGF_FGF; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Growth factor; Heparin-binding; Mitogen; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..194
FT /note="Fibroblast growth factor 7"
FT /id="PRO_0000008967"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 194 AA; 22463 MW; BA449B5B45A731B0 CRC64;
MRKWILTWIL PSLLHRSCFH IICLVGTLSL DCNDMTPEQM ATNVNCSSPE RHTRSYDYME
GGDIRVRRLF CRTQWYPRIG KRGKVKGTQE MKNNYNIMEI RTVAVGIVAI KGVVSEYYLA
MNKEGKLYAK KEYNEDCNFK ELILENHYNT YASAKWTHSG GEMFVALNQK GVPVRGKKTK
KEQKTAHFLP MAIT
