LE756_CAEEL
ID LE756_CAEEL Reviewed; 425 AA.
AC Q11184; O76831;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein let-756;
DE AltName: Full=Lethal protein 756;
GN Name=let-756; ORFNames=C05D11.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=9010135; DOI=10.1007/pl00006120;
RA Coulier F., Pontarotti P., Roubin R., Hartung H., Goldfarb M., Birnbaum D.;
RT "Of worms and men: an evolutionary perspective on the fibroblast growth
RT factor (FGF) and FGF receptor families.";
RL J. Mol. Evol. 44:43-56(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=9331368; DOI=10.1101/gr.7.10.974;
RA Janke D.L., Schein J.E., Ha T., Franz N.W., O'Neil N.J., Vatcher G.P.,
RA Stewart H.I., Kuervers L.M., Baillie D.L., Rose A.M.;
RT "Interpreting a sequenced genome: toward a cosmid transgenic library of
RT Caenorhabditis elegans.";
RL Genome Res. 7:974-985(1997).
RN [4]
RP INTERACTION WITH PAL-1.
RX PubMed=16672054; DOI=10.1186/1471-2164-7-105;
RA Popovici C., Berda Y., Conchonaud F., Harbis A., Birnbaum D., Roubin R.;
RT "Direct and heterologous approaches to identify the LET-756/FGF
RT interactome.";
RL BMC Genomics 7:105-105(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
CC -!- FUNCTION: Required for larval development (PubMed:9331368). Probably by
CC binding receptor egl-15, regulates negatively membrane protrusion from
CC body wall muscles during larval development (PubMed:16495308).
CC {ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:9331368}.
CC -!- SUBUNIT: Interacts with pal-1. {ECO:0000269|PubMed:16672054}.
CC -!- INTERACTION:
CC Q11184; Q09958: C18A3.3; NbExp=2; IntAct=EBI-3843983, EBI-2412471;
CC Q11184; Q21556: col-129; NbExp=4; IntAct=EBI-3843983, EBI-3844027;
CC Q11184; Q18688: daf-21; NbExp=3; IntAct=EBI-3843983, EBI-313329;
CC Q11184; Q20655: ftt-2; NbExp=3; IntAct=EBI-3843983, EBI-966073;
CC Q11184; P28548: kin-10; NbExp=3; IntAct=EBI-3843983, EBI-317777;
CC Q11184; P18334: kin-3; NbExp=3; IntAct=EBI-3843983, EBI-367861;
CC Q11184; P41932: par-5; NbExp=3; IntAct=EBI-3843983, EBI-318108;
CC Q11184; P47991: rpl-6; NbExp=3; IntAct=EBI-3843983, EBI-316106;
CC Q11184; Q22054: rps-16; NbExp=4; IntAct=EBI-3843983, EBI-3844009;
CC Q11184; G5EDD8: skr-2; NbExp=3; IntAct=EBI-3843983, EBI-314583;
CC Q11184; P31946: YWHAB; Xeno; NbExp=2; IntAct=EBI-3843983, EBI-359815;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16495308}. Membrane
CC {ECO:0000269|PubMed:9331368}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16495308}.
CC -!- TISSUE SPECIFICITY: Expressed in pharynx, CAN neuron and body wall
CC muscles. {ECO:0000269|PubMed:16495308}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; AJ010553; CAA09234.1; -; mRNA.
DR EMBL; FO080365; CCD63193.1; -; Genomic_DNA.
DR PIR; H88481; H88481.
DR RefSeq; NP_498403.1; NM_066002.4.
DR AlphaFoldDB; Q11184; -.
DR SMR; Q11184; -.
DR BioGRID; 41127; 199.
DR IntAct; Q11184; 21.
DR STRING; 6239.C05D11.4; -.
DR PaxDb; Q11184; -.
DR EnsemblMetazoa; C05D11.4.1; C05D11.4.1; WBGene00002881.
DR GeneID; 175909; -.
DR KEGG; cel:CELE_C05D11.4; -.
DR UCSC; C05D11.4; c. elegans.
DR CTD; 175909; -.
DR WormBase; C05D11.4; CE24786; WBGene00002881; let-756.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000165881; -.
DR HOGENOM; CLU_045880_0_0_1; -.
DR InParanoid; Q11184; -.
DR OMA; YYNLYAS; -.
DR OrthoDB; 1201908at2759; -.
DR Reactome; R-CEL-189200; Cellular hexose transport.
DR Reactome; R-CEL-190372; FGFR3c ligand binding and activation.
DR Reactome; R-CEL-3000170; Syndecan interactions.
DR Reactome; R-CEL-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-5658623; FGFRL1 modulation of FGFR1 signaling.
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q11184; -.
DR PRO; PR:Q11184; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002881; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:WormBase.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; ISS:WormBase.
DR GO; GO:0008083; F:growth factor activity; IMP:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:WormBase.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:WormBase.
DR GO; GO:0031345; P:negative regulation of cell projection organization; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR Pfam; PF00167; FGF; 1.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; SSF50353; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Growth factor; Membrane; Nucleus;
KW Reference proteome.
FT CHAIN 1..425
FT /note="Protein let-756"
FT /id="PRO_0000147619"
FT REGION 277..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 49569 MW; E04A5A2D94F044D2 CRC64;
MAVPAASSIV SYGGAATSNF LTTPVTPFLA GFYNSNFVTD RINSCAPYRV DRIRKQLQDE
EENGYPPADD RRRGALFCRS GTWLEMLPIE NPDDGSTRVK VHGTKEESSK FSIVEFVSVA
MSLVSIRGVE TKNFICMDPS GKLYATPSSN YSTECVFLEE MMENYYNLYA SCAYGDRFNP
WYIELRRSGK PRRGPNSKKR RKASHFLVVH HDLDRLRSPV PNGNDVTDLV VASLFHQPPS
HPLFRQQTVT KPPNPHRISN LRAKVEMTNQ AEKQRLLEEK KRRREKKKRR REDRLRKEEQ
IREARRQELK SLREEELRRR YQQQQQQQAS TQTRYNRPQN PANPYPTYRP LPTRSTVQSP
RPAYNPYWQS PVTQAPHHNS HHHHHHHPRV SSSSDPQQRH QSQQHYLAQT VSNPNRQNVN
YQRYP
