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FGRL1_RAT
ID   FGRL1_RAT               Reviewed;         529 AA.
AC   Q7TQM3; Q4V8P8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Fibroblast growth factor receptor-like 1;
DE            Short=FGF receptor-like protein 1;
DE   Flags: Precursor;
GN   Name=Fgfrl1;
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].
RC   STRAIN=Sprague-Dawley;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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).
CC   -!- FUNCTION: Has a negative effect on cell proliferation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FGF2 with a low affinity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}. Cytoplasmic vesicle,
CC       secretory vesicle membrane {ECO:0000250}; Single-pass type I membrane
CC       protein {ECO:0000250}. Note=Predominantly localized in the plasma
CC       membrane but also detected in the Golgi and in secretory vesicles.
CC       {ECO:0000250}.
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DR   EMBL; AJ536020; CAD59914.1; -; mRNA.
DR   EMBL; BC097261; AAH97261.1; -; mRNA.
DR   RefSeq; NP_954545.1; NM_199114.1.
DR   AlphaFoldDB; Q7TQM3; -.
DR   SMR; Q7TQM3; -.
DR   STRING; 10116.ENSRNOP00000000037; -.
DR   GlyGen; Q7TQM3; 4 sites.
DR   PaxDb; Q7TQM3; -.
DR   PRIDE; Q7TQM3; -.
DR   GeneID; 360903; -.
DR   KEGG; rno:360903; -.
DR   UCSC; RGD:735156; rat.
DR   CTD; 53834; -.
DR   RGD; 735156; Fgfrl1.
DR   VEuPathDB; HostDB:ENSRNOG00000024207; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   HOGENOM; CLU_038830_1_0_1; -.
DR   InParanoid; Q7TQM3; -.
DR   OMA; WAQPRFT; -.
DR   OrthoDB; 612548at2759; -.
DR   PhylomeDB; Q7TQM3; -.
DR   Reactome; R-RNO-5658623; FGFRL1 modulation of FGFR1 signaling.
DR   PRO; PR:Q7TQM3; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000024207; Expressed in pancreas and 19 other tissues.
DR   Genevisible; Q7TQM3; RN.
DR   GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0030133; C:transport vesicle; ISO:RGD.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017134; F:fibroblast growth factor binding; ISO:RGD.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; ISO:RGD.
DR   GO; GO:0008201; F:heparin binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:RGD.
DR   GO; GO:0060539; P:diaphragm development; ISO:RGD.
DR   GO; GO:0003179; P:heart valve morphogenesis; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
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   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW   Golgi apparatus; Immunoglobulin domain; Membrane; Receptor;
KW   Reference proteome; Repeat; 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_0000021252"
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          117..152
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"
SQ   SEQUENCE   529 AA;  57144 MW;  23D67B419335FFFC CRC64;
     MTRSPALLLL LLGALPSAEA ARGPPRMADK VVPRQVARLG RTVRLQCPVE GDPPPLTMWT
     KDGRTIHSGW SRFRVLPQGL KVKEVEAEDA GVYVCKATNG FGSLSVNYTL IIMDDISPGK
     ENPGPGGSSG GQEDPVSQQW ARPRFTQPSK MRRRVIARPV GSSVRLKCVA SGHPRPDIMW
     MKDDQTLTRL EASEHRKKKW TLSLKNLKPE DSGKYTCRVS NRAGAINATY KVDVIQRTRS
     KPVLTGTHPV NTTVDFGGTT SFQCKVRSDV KPVIQWLKRV EYGSEGRHNS TIDVGGQKFV
     VLPTGDVWSR PDGSYLNKLL ISRARQDDAG MYICLGANTM GYSFRSAFLT VLPDPKPPGP
     PVAHSSSTTS LPWPVVIGIP AGAVFILGTV LLWLCQTKKK PCAPASTLPV PGHRPPGTSR
     ERSGDKDLPS LAVGICEEHG STMAPQHILA PGSTAGPKLY PKLYTDVHTH THTHTCTHTL
     SCGGQGSSAP ACPLSVLNTA NLQALCPEVG VWGPRQQVGR IENNGGRVS
 
 
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