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FGRL1_MOUSE
ID   FGRL1_MOUSE             Reviewed;         529 AA.
AC   Q91V87; Q920C2; Q920C3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Fibroblast growth factor receptor-like 1;
DE            Short=FGF receptor-like protein 1;
DE   AltName: Full=Fibroblast growth factor receptor 5;
DE            Short=FGFR-5;
DE   Flags: Precursor;
GN   Name=Fgfrl1; Synonyms=Fgfr5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE
RP   SPECIFICITY, AND INTERACTION WITH FGF2.
RC   STRAIN=BALB/cJ;
RX   PubMed=11418238; DOI=10.1016/s0378-1119(01)00518-2;
RA   Sleeman M., Fraser J., McDonald M., Yuan S., White D., Grandison P.,
RA   Kumble K., Watson J.D., Murison J.G.;
RT   "Identification of a new fibroblast growth factor receptor, FGFR5.";
RL   Gene 271:171-182(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Cartilage;
RX   PubMed=11566361; DOI=10.1016/s0167-4781(01)00267-6;
RA   Wiedemann M., Trueb B.;
RT   "The mouse Fgfrl1 gene coding for a novel FGF receptor-like protein.";
RL   Biochim. Biophys. Acta 1520:247-250(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12813049; DOI=10.1074/jbc.m300281200;
RA   Trueb B., Zhuang L., Taeschler S., Wiedemann M.;
RT   "Characterization of FGFRL1, a novel fibroblast growth factor (FGF)
RT   receptor preferentially expressed in skeletal tissues.";
RL   J. Biol. Chem. 278:33857-33865(2003).
CC   -!- FUNCTION: Has a negative effect on cell proliferation. {ECO:0000250,
CC       ECO:0000269|PubMed:12813049}.
CC   -!- SUBUNIT: Interacts with FGF2 with a low affinity.
CC       {ECO:0000269|PubMed:11418238}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=FGFR5beta, FGFR5b;
CC         IsoId=Q91V87-1; Sequence=Displayed;
CC       Name=2; Synonyms=FGFR5gamma, FGFR5g;
CC         IsoId=Q91V87-2; Sequence=VSP_013976;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the kidney, brain and lung.
CC       Weakly expressed in the muscle, thymus, lymph node, stomach, intestine,
CC       colon and liver. Expressed in fetal cartilaginous structures like the
CC       nasal cartilage, the ribs and the sternum as well as in the
CC       cartilaginous rudiments of developing bones such as the vertebrae and
CC       the pelvic bone. High expression is found in the muscles of the tongue
CC       and the diaphragm. {ECO:0000269|PubMed:11418238,
CC       ECO:0000269|PubMed:12813049}.
CC   -!- DEVELOPMENTAL STAGE: First detected at embryonic day 7 and became
CC       clearly visible at day 11 and increased until day 17.
CC       {ECO:0000269|PubMed:11566361}.
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DR   EMBL; AF321300; AAL06295.1; -; mRNA.
DR   EMBL; AF321301; AAL06296.1; -; mRNA.
DR   EMBL; AF321302; AAL06297.1; -; Genomic_DNA.
DR   EMBL; AJ293947; CAC82376.1; -; mRNA.
DR   EMBL; AJ308490; CAC83768.1; -; Genomic_DNA.
DR   EMBL; BC058745; AAH58745.1; -; mRNA.
DR   CCDS; CCDS19518.1; -. [Q91V87-1]
DR   CCDS; CCDS51592.1; -. [Q91V87-2]
DR   RefSeq; NP_001157731.1; NM_001164259.1. [Q91V87-2]
DR   RefSeq; NP_473412.1; NM_054071.2. [Q91V87-1]
DR   RefSeq; XP_017176107.1; XM_017320618.1. [Q91V87-1]
DR   AlphaFoldDB; Q91V87; -.
DR   SMR; Q91V87; -.
DR   BioGRID; 227959; 1.
DR   STRING; 10090.ENSMUSP00000013633; -.
DR   GlyGen; Q91V87; 4 sites.
DR   iPTMnet; Q91V87; -.
DR   PhosphoSitePlus; Q91V87; -.
DR   PaxDb; Q91V87; -.
DR   PeptideAtlas; Q91V87; -.
DR   PRIDE; Q91V87; -.
DR   ProteomicsDB; 271588; -. [Q91V87-1]
DR   ProteomicsDB; 271589; -. [Q91V87-2]
DR   Antibodypedia; 22198; 359 antibodies from 32 providers.
DR   DNASU; 116701; -.
DR   Ensembl; ENSMUST00000013633; ENSMUSP00000013633; ENSMUSG00000008090. [Q91V87-1]
DR   Ensembl; ENSMUST00000112560; ENSMUSP00000108179; ENSMUSG00000008090. [Q91V87-2]
DR   GeneID; 116701; -.
DR   KEGG; mmu:116701; -.
DR   UCSC; uc008ypa.2; mouse. [Q91V87-1]
DR   UCSC; uc012eav.1; mouse. [Q91V87-2]
DR   CTD; 53834; -.
DR   MGI; MGI:2150920; Fgfrl1.
DR   VEuPathDB; HostDB:ENSMUSG00000008090; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   GeneTree; ENSGT00940000156736; -.
DR   HOGENOM; CLU_038830_1_0_1; -.
DR   InParanoid; Q91V87; -.
DR   OMA; WAQPRFT; -.
DR   OrthoDB; 612548at2759; -.
DR   PhylomeDB; Q91V87; -.
DR   Reactome; R-MMU-5658623; FGFRL1 modulation of FGFR1 signaling.
DR   BioGRID-ORCS; 116701; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Fgfrl1; mouse.
DR   PRO; PR:Q91V87; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q91V87; protein.
DR   Bgee; ENSMUSG00000008090; Expressed in humerus cartilage element and 298 other tissues.
DR   ExpressionAtlas; Q91V87; baseline and differential.
DR   Genevisible; Q91V87; MM.
DR   GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IPI:MGI.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; IDA:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0001571; F:non-tyrosine kinase fibroblast growth factor receptor activity; ISA:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISA:MGI.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:MGI.
DR   GO; GO:0060539; P:diaphragm development; IMP:MGI.
DR   GO; GO:0003179; P:heart valve morphogenesis; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR   GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IC:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP:MGI.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..529
FT                   /note="Fibroblast growth factor receptor-like 1"
FT                   /id="PRO_0000021251"
FT   TOPO_DOM        21..374
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        396..529
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..111
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          143..233
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          242..350
FT                   /note="Ig-like C2-type 3"
FT   REGION          116..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        168..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        264..334
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         23..113
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11418238"
FT                   /id="VSP_013976"
SQ   SEQUENCE   529 AA;  57013 MW;  6CE76A75BF2498DD CRC64;
     MTRSPALLLL LLGALPSAEA ARGPPRMADK VVPRQVARLG RTVRLQCPVE GDPPPLTMWT
     KDGRTIHSGW SRFRVLPQGL KVKEVEAEDA GVYVCKATNG FGSLSVNYTL IIMDDISPGK
     ESPGPGGSSG GQEDPASQQW ARPRFTQPSK MRRRVIARPV GSSVRLKCVA SGHPRPDIMW
     MKDDQTLTHL EASEHRKKKW TLSLKNLKPE DSGKYTCRVS NKAGAINATY KVDVIQRTRS
     KPVLTGTHPV NTTVDFGGTT SFQCKVRSDV KPVIQWLKRV EYGSEGRHNS TIDVGGQKFV
     VLPTGDVWSR PDGSYLNKLL ISRARQDDAG MYICLGANTM GYSFRSAFLT VLPDPKPPGP
     PMASSSSSTS LPWPVVIGIP AGAVFILGTV LLWLCQTKKK PCAPASTLPV PGHRPPGTSR
     ERSGDKDLPS LAVGICEEHG SAMAPQHILA SGSTAGPKLY PKLYTDVHTH THTHTCTHTL
     SCGGQGSSTP ACPLSVLNTA NLQALCPEVG IWGPRQQVGR IENNGGRVS
 
 
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