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FGF5_CANLF
ID   FGF5_CANLF              Reviewed;         270 AA.
AC   Q20FD0; Q20FC9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Fibroblast growth factor 5;
DE            Short=FGF-5;
DE   Flags: Precursor;
GN   Name=FGF5;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), FUNCTION, VARIANTS
RP   THR-SER-50 INS AND PHE-95, AND POLYMORPHISM.
RC   STRAIN=Corgi;
RX   PubMed=16879338; DOI=10.1111/j.1365-2052.2006.01448.x;
RA   Housley D.J.E., Venta P.J.;
RT   "The long and the short of it: evidence that FGF5 is a major determinant of
RT   canine 'hair'-itability.";
RL   Anim. Genet. 37:309-315(2006).
CC   -!- FUNCTION: Plays an important role in the regulation of cell
CC       proliferation and cell differentiation. Required for normal regulation
CC       of the hair growth cycle. Functions as an inhibitor of hair elongation
CC       by promoting progression from anagen, the growth phase of the hair
CC       follicle, into catagen the apoptosis-induced regression phase.
CC       {ECO:0000269|PubMed:16879338}.
CC   -!- SUBUNIT: Interacts with FGFR1 and FGFR2. Affinity between fibroblast
CC       growth factors (FGFs) and their receptors is increased by heparan
CC       sulfate glycosaminoglycans that function as coreceptors (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q20FD0-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q20FD0-2; Sequence=VSP_023508, VSP_023509;
CC   -!- POLYMORPHISM: The polymorphism in position 95 is responsible for hair
CC       length variation. The long-haired phenotype is associated with Phe-95
CC       or with the insertion in position 50. {ECO:0000269|PubMed:16879338}.
CC   -!- MISCELLANEOUS: [Isoform Short]: Seems to have an antagonistic effect
CC       compared to that of the isoform Long. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC       {ECO:0000305}.
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DR   EMBL; DQ268832; ABB87177.1; -; mRNA.
DR   EMBL; DQ268833; ABB87178.1; -; mRNA.
DR   RefSeq; NP_001041594.1; NM_001048129.1.
DR   AlphaFoldDB; Q20FD0; -.
DR   SMR; Q20FD0; -.
DR   STRING; 9612.ENSCAFP00000034270; -.
DR   PaxDb; Q20FD0; -.
DR   Ensembl; ENSCAFT00000038532; ENSCAFP00000034270; ENSCAFG00000008886. [Q20FD0-1]
DR   GeneID; 608459; -.
DR   KEGG; cfa:608459; -.
DR   CTD; 2250; -.
DR   eggNOG; KOG3885; Eukaryota.
DR   InParanoid; Q20FD0; -.
DR   OrthoDB; 1157770at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005104; F:fibroblast growth factor receptor binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   CDD; cd00058; FGF; 1.
DR   InterPro; IPR028240; FGF5.
DR   InterPro; IPR002209; Fibroblast_GF_fam.
DR   InterPro; IPR008996; IL1/FGF.
DR   PANTHER; PTHR11486; PTHR11486; 1.
DR   PANTHER; PTHR11486:SF23; PTHR11486:SF23; 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   Alternative splicing; Glycoprotein; Growth factor; Mitogen;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..270
FT                   /note="Fibroblast growth factor 5"
FT                   /id="PRO_0000279864"
FT   REGION          26..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         122..125
FT                   /note="ILEI -> QVYR (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:16879338"
FT                   /id="VSP_023508"
FT   VAR_SEQ         126..270
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:16879338"
FT                   /id="VSP_023509"
FT   VARIANT         50
FT                   /note="S -> STS (in long hair dog breeds)"
FT                   /evidence="ECO:0000269|PubMed:16879338"
FT   VARIANT         95
FT                   /note="C -> F (in long hair dog breeds)"
FT                   /evidence="ECO:0000269|PubMed:16879338"
SQ   SEQUENCE   270 AA;  29183 MW;  FFCB8A537F27FFAE CRC64;
     MSLSLLLLLF LSHLILSAWA HGEKHLAPKG QPGPAATGRN PGGAGGSSTS GGTTSSSSSS
     VSSAPGASPG IRGSGSEQGS FQWSPSGRRT GSLYCRVGIG FHLQIYPDGK VNGSHEANML
     SILEIFAVSQ GIVGIRGVFS NKFLAMSKKG KLHASAKFTD DCKFRERFQE NSYNTYASAI
     HRSEPAGREW YVALNKRGKA KRGCSPRVKP QHVSTHFLPR FKQLEHPELS FTVTVPEKKK
     PPSHVKPKVP LSAPRKSPNT VKYRLKFRFG
 
 
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