FGF7_RAT
ID FGF7_RAT Reviewed; 194 AA.
AC Q02195;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 144.
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 Flags: Precursor;
GN Name=Fgf7; Synonyms=Fgf-7, Kgf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1869483; DOI=10.1007/bf02631140;
RA Yan G., Nikolaropoulos S., Wang F., McKeehan W.L.;
RT "Sequence of rat keratinocyte growth factor (heparin-binding growth factor
RT type 7).";
RL In Vitro Cell. Dev. Biol. 27A:437-438(1991).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 55-150, AND HEPARIN BINDING.
RX PubMed=11724555; DOI=10.1021/bi011000u;
RA Ye S., Luo Y., Lu W., Jones R.B., Linhardt R.J., Capila I., Toida T.,
RA Kan M., Pelletier H., McKeehan W.L.;
RT "Structural basis for interaction of FGF-1, FGF-2, and FGF-7 with different
RT heparan sulfate motifs.";
RL Biochemistry 40:14429-14439(2001).
CC -!- FUNCTION: Growth factor active on keratinocytes. Possible major
CC paracrine effector of normal epithelial cell proliferation.
CC -!- SUBUNIT: Interacts with FGFBP1. Interacts with FGFR2 (By similarity).
CC Affinity between fibroblast growth factors (FGFs) and their receptors
CC is increased by heparan sulfate glycosaminoglycans that function as
CC coreceptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; X56551; CAA39892.1; -; mRNA.
DR PIR; S26049; S26049.
DR RefSeq; NP_071518.1; NM_022182.1.
DR PDB; 1QQK; X-ray; 3.10 A; A/B=55-194.
DR PDB; 1QQL; X-ray; 2.30 A; A=55-130.
DR PDBsum; 1QQK; -.
DR PDBsum; 1QQL; -.
DR AlphaFoldDB; Q02195; -.
DR SMR; Q02195; -.
DR STRING; 10116.ENSRNOP00000012700; -.
DR GlyGen; Q02195; 2 sites.
DR iPTMnet; Q02195; -.
DR PhosphoSitePlus; Q02195; -.
DR PaxDb; Q02195; -.
DR GeneID; 29348; -.
DR KEGG; rno:29348; -.
DR UCSC; RGD:61805; rat.
DR CTD; 2252; -.
DR RGD; 61805; Fgf7.
DR eggNOG; KOG3885; Eukaryota.
DR InParanoid; Q02195; -.
DR PhylomeDB; Q02195; -.
DR Reactome; R-RNO-109704; PI3K Cascade.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-190377; FGFR2b ligand binding and activation.
DR Reactome; R-RNO-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-RNO-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-RNO-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR EvolutionaryTrace; Q02195; -.
DR PRO; PR:Q02195; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0042056; F:chemoattractant activity; ISO:RGD.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IMP:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0005111; F:type 2 fibroblast growth factor receptor binding; IDA:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0030324; P:lung development; IMP:RGD.
DR GO; GO:0010463; P:mesenchymal cell proliferation; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:RGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:RGD.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:RGD.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0061033; P:secretion by lung epithelial cell involved in lung growth; ISO:RGD.
DR GO; GO:0043129; P:surfactant homeostasis; IMP:RGD.
DR GO; GO:0042060; P:wound healing; IDA:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Growth factor; Heparin-binding; Mitogen;
KW Reference proteome; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..194
FT /note="Fibroblast growth factor 7"
FT /id="PRO_0000008968"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1QQL"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1QQL"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1QQL"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1QQL"
FT TURN 158..162
FT /evidence="ECO:0007829|PDB:1QQL"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1QQL"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1QQK"
SQ SEQUENCE 194 AA; 22268 MW; 5242CDAC305CC8C1 CRC64;
MRKWILTRIL PTPLYRPCFH LVCLVGTISL ACNDMSPEQT ATSVNCSSPE RHTRSYDYME
GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MRNSYNIMEI MTVAVGIVAI KGVESEYYLA
MNKQGELYAK KECNEDCNFK ELILENHYNT SASAKWTHSG GEMFVALNQK GLPVKGKKTK
KEQKTAHFLP MAIT
