ID   FGRL1_HUMAN             Reviewed;         504 AA.
AC   Q8N441; B2RAU9; Q6PJN1; Q9BXN7; Q9H4D7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Fibroblast growth factor receptor-like 1;
DE            Short=FGF receptor-like protein 1;
DE   AltName: Full=FGF homologous factor receptor;
DE   AltName: Full=FGFR-like protein;
DE   AltName: Full=Fibroblast growth factor receptor 5;
DE            Short=FGFR-5;
DE   Flags: Precursor;
GN   Name=FGFRL1; Synonyms=FGFR5, FHFR; ORFNames=UNQ480/PRO943;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT GLN-362.
RC   TISSUE=Cartilage;
RX   PubMed=11031111; DOI=10.1006/geno.2000.6332;
RA   Wiedemann M., Trueb B.;
RT   "Characterization of a novel protein (FGFRL1) from human cartilage related
RT   to FGF receptors.";
RL   Genomics 69:275-279(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT GLN-362.
RX   PubMed=11267671; DOI=10.1016/s0167-4781(00)00282-7;
RA   Kim I., Moon S.-O., Yu K.-H., Kim U.-H., Koh G.Y.;
RT   "A novel fibroblast growth factor receptor-5 preferentially expressed in
RT   the pancreas.";
RL   Biochim. Biophys. Acta 1518:152-156(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Aggarwal S., Xie M.-H., Foster J., Frantz G., Stinson J., Corpuz R.T.,
RA   Simmons L., Hillan K., Yansura D.G., Vandlen R.L., Goddard A.D.,
RA   Gurney A.L.;
RT   "FHFR, a novel fibroblast growth factor receptor that uniquely binds the
RT   fibroblast growth factor homologous factors.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-362.
RC   TISSUE=Brain;
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   [7]
RP   PROTEIN SEQUENCE OF 25-39.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [8]
RP   TISSUE SPECIFICITY.
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   [9]
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Cartilage;
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   -!- SUBUNIT: Interacts with FGF2 with a low affinity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12813049}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:12813049}.
CC       Note=Predominantly localized in the plasma membrane but also detected
CC       in the Golgi and in secretory vesicles.
CC   -!- TISSUE SPECIFICITY: Expressed preferentially in cartilaginous tissues
CC       and pancreas. Highly expressed in the liver, kidney, heart, brain and
CC       skeletal muscle. Weakly expressed in the lung, small intestine and
CC       spleen. {ECO:0000269|PubMed:11031111, ECO:0000269|PubMed:11267671,
CC       ECO:0000269|PubMed:11418238}.
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DR   EMBL; AJ277437; CAC14171.1; -; mRNA.
DR   EMBL; AF279689; AAK26742.1; -; mRNA.
DR   EMBL; AF312678; AAK15273.1; -; mRNA.
DR   EMBL; AY358303; AAQ88670.1; -; mRNA.
DR   EMBL; AK314365; BAG36996.1; -; mRNA.
DR   EMBL; BC036769; AAH36769.1; -; mRNA.
DR   CCDS; CCDS3344.1; -.
DR   RefSeq; NP_001004356.1; NM_001004356.2.
DR   RefSeq; NP_001004358.1; NM_001004358.1.
DR   RefSeq; NP_068742.2; NM_021923.3.
DR   RefSeq; XP_011511788.1; XM_011513486.1.
DR   AlphaFoldDB; Q8N441; -.
DR   SMR; Q8N441; -.
DR   BioGRID; 119806; 61.
DR   IntAct; Q8N441; 23.
DR   MINT; Q8N441; -.
DR   STRING; 9606.ENSP00000381498; -.
DR   TCDB; 8.A.23.1.6; the basigin (basigin) family.
DR   GlyConnect; 1240; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q8N441; 4 sites, 2 glycans.
DR   GlyGen; Q8N441; 4 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q8N441; -.
DR   PhosphoSitePlus; Q8N441; -.
DR   BioMuta; FGFRL1; -.
DR   DMDM; 68052359; -.
DR   jPOST; Q8N441; -.
DR   MassIVE; Q8N441; -.
DR   MaxQB; Q8N441; -.
DR   PaxDb; 9606-ENSP00000381498; -.
DR   PeptideAtlas; Q8N441; -.
DR   ProteomicsDB; 71879; -.
DR   Pumba; Q8N441; -.
DR   Antibodypedia; 22198; 374 antibodies from 32 providers.
DR   DNASU; 53834; -.
DR   Ensembl; ENST00000264748.6; ENSP00000264748.6; ENSG00000127418.15.
DR   Ensembl; ENST00000398484.6; ENSP00000381498.2; ENSG00000127418.15.
DR   Ensembl; ENST00000504138.5; ENSP00000423091.1; ENSG00000127418.15.
DR   Ensembl; ENST00000510644.6; ENSP00000425025.1; ENSG00000127418.15.
DR   GeneID; 53834; -.
DR   KEGG; hsa:53834; -.
DR   MANE-Select; ENST00000510644.6; ENSP00000425025.1; NM_001004356.3; NP_001004356.1.
DR   UCSC; uc003gcf.4; human.
DR   AGR; HGNC:3693; -.
DR   CTD; 53834; -.
DR   DisGeNET; 53834; -.
DR   GeneCards; FGFRL1; -.
DR   HGNC; HGNC:3693; FGFRL1.
DR   HPA; ENSG00000127418; Low tissue specificity.
DR   MalaCards; FGFRL1; -.
DR   MIM; 605830; gene.
DR   neXtProt; NX_Q8N441; -.
DR   OpenTargets; ENSG00000127418; -.
DR   PharmGKB; PA28132; -.
DR   VEuPathDB; HostDB:ENSG00000127418; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   GeneTree; ENSGT00940000156736; -.
DR   HOGENOM; CLU_038830_1_0_1; -.
DR   InParanoid; Q8N441; -.
DR   OMA; GSMNVNY; -.
DR   OrthoDB; 3464773at2759; -.
DR   PhylomeDB; Q8N441; -.
DR   PathwayCommons; Q8N441; -.
DR   Reactome; R-HSA-5658623; FGFRL1 modulation of FGFR1 signaling.
DR   SignaLink; Q8N441; -.
DR   BioGRID-ORCS; 53834; 15 hits in 1160 CRISPR screens.
DR   ChiTaRS; FGFRL1; human.
DR   GeneWiki; FGFRL1; -.
DR   GenomeRNAi; 53834; -.
DR   Pharos; Q8N441; Tbio.
DR   PRO; PR:Q8N441; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q8N441; Protein.
DR   Bgee; ENSG00000127418; Expressed in right uterine tube and 115 other cell types or tissues.
DR   ExpressionAtlas; Q8N441; baseline and differential.
DR   GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; IDA:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
DR   GO; GO:0060539; P:diaphragm development; IEA:Ensembl.
DR   GO; GO:0003179; P:heart valve morphogenesis; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR   CDD; cd05856; IgI_2_FGFRL1-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR19890; FIBROBLAST GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR19890:SF10; FIBROBLAST GROWTH FACTOR RECEPTOR-LIKE 1; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   Genevisible; Q8N441; HS.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           25..504
FT                   /note="Fibroblast growth factor receptor-like 1"
FT                   /id="PRO_0000021250"
FT   TOPO_DOM        25..378
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        400..504
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..115
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          147..237
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          246..354
FT                   /note="Ig-like C2-type 3"
FT   REGION          123..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..99
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        172..221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        268..338
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         362
FT                   /note="P -> Q (in dbSNP:rs4647930)"
FT                   /evidence="ECO:0000269|PubMed:11031111,
FT                   ECO:0000269|PubMed:11267671, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_022642"
FT   VARIANT         464
FT                   /note="P -> L (in dbSNP:rs4647932)"
FT                   /id="VAR_024316"
FT   CONFLICT        374..380
FT                   /note="Missing (in Ref. 3; AAK15273)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  54537 MW;  56E35E57D5FC141B CRC64;
     MTPSPLLLLL LPPLLLGAFP PAAAARGPPK MADKVVPRQV ARLGRTVRLQ CPVEGDPPPL
     TMWTKDGRTI HSGWSRFRVL PQGLKVKQVE REDAGVYVCK ATNGFGSLSV NYTLVVLDDI
     SPGKESLGPD SSSGGQEDPA SQQWARPRFT QPSKMRRRVI ARPVGSSVRL KCVASGHPRP
     DITWMKDDQA LTRPEAAEPR KKKWTLSLKN LRPEDSGKYT CRVSNRAGAI NATYKVDVIQ
     RTRSKPVLTG THPVNTTVDF GGTTSFQCKV RSDVKPVIQW LKRVEYGAEG RHNSTIDVGG
     QKFVVLPTGD VWSRPDGSYL NKLLITRARQ DDAGMYICLG ANTMGYSFRS AFLTVLPDPK
     PPGPPVASSS SATSLPWPVV IGIPAGAVFI LGTLLLWLCQ AQKKPCTPAP APPLPGHRPP
     GTARDRSGDK DLPSLAALSA GPGVGLCEEH GSPAAPQHLL GPGPVAGPKL YPKLYTDIHT
     HTHTHSHTHS HVEGKVHQHI HYQC
//