ID A0A3Q3GY77_9LABR Unreviewed; 144 AA.
AC A0A3Q3GY77;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU049442, ECO:0000256|RuleBase:RU364136};
DE Includes:
DE RecName: Full=Fibroblast growth factor 1 {ECO:0000256|RuleBase:RU364136};
DE AltName: Full=Acidic fibroblast growth factor {ECO:0000256|RuleBase:RU364136};
DE AltName: Full=Heparin-binding growth factor 1 {ECO:0000256|RuleBase:RU364136};
DE Includes:
DE RecName: Full=Fibroblast growth factor {ECO:0000256|RuleBase:RU049442};
DE Short=FGF {ECO:0000256|RuleBase:RU049442};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000035623.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000035623.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays an important role in the regulation of cell survival,
CC cell division, angiogenesis, cell differentiation and cell migration.
CC Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and
CC integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1
CC dimerization and activation via sequential autophosphorylation on
CC tyrosine residues which act as docking sites for interacting proteins,
CC leading to the activation of several signaling cascades. Binds to
CC integrins. Its binding to integrins and subsequent ternary complex
CC formation with integrins and FGFR1 are essential for FGF1 signaling.
CC {ECO:0000256|RuleBase:RU364136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544, ECO:0000256|RuleBase:RU364136}.
CC Secreted {ECO:0000256|RuleBase:RU364136}. Cytoplasm
CC {ECO:0000256|RuleBase:RU364136}. Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU364136}. Nucleus
CC {ECO:0000256|RuleBase:RU364136}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000256|ARBA:ARBA00007936, ECO:0000256|RuleBase:RU049442}.
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DR AlphaFoldDB; A0A3Q3GY77; -.
DR Ensembl; ENSLBET00000037126.1; ENSLBEP00000035623.1; ENSLBEG00000026702.1.
DR GeneTree; ENSGT00940000165035; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR CDD; cd00058; FGF; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; FIBROBLAST GROWTH FACTOR; 1.
DR PANTHER; PTHR11486:SF86; FIBROBLAST GROWTH FACTOR 1; 1.
DR Pfam; PF00167; FGF; 1.
DR PRINTS; PR00263; HBGFFGF.
DR PRINTS; PR00262; IL1HBGF.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; Cytokine; 1.
DR PROSITE; PS00247; HBGF_FGF; 1.
PE 3: Inferred from homology;
KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657,
KW ECO:0000256|RuleBase:RU364136}; Cytoplasm {ECO:0000256|RuleBase:RU364136};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU364136};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782,
KW ECO:0000256|RuleBase:RU364136};
KW Growth factor {ECO:0000256|RuleBase:RU364136};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674,
KW ECO:0000256|RuleBase:RU364136}; Mitogen {ECO:0000256|RuleBase:RU364136};
KW Nucleus {ECO:0000256|RuleBase:RU364136};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364136}.
SQ SEQUENCE 144 AA; 16564 MW; 49BF85E46FD1C170 CRC64;
MQHFGSADGG LRRDFRRLTR LYCMNGGHHL QILPDGTVQG QREDRDDHSK LTAVDIGVVI
IQGTEAGQYL AMSDEGRLYS SVTVTDECYF VEKLEENHYN TYRSQKYVEE NWYVALKKNG
KPKLGPRTHI GQKAIFFLPR QLNE
//
