ID FBLN3_RAT Reviewed; 493 AA. AC O35568; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=EGF-containing fibulin-like extracellular matrix protein 1; DE AltName: Full=Fibulin-3; DE Short=FIBL-3; DE AltName: Full=T16 protein; DE Flags: Precursor; GN Name=Efemp1; Synonyms=Fbln3; 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], AND TISSUE SPECIFICITY. RC TISSUE=Lung; RX PubMed=9268694; DOI=10.1006/bbrc.1997.7122; RA Ozaki T., Kondo K., Nakamura Y., Ichimiya S., Nakagawara A., Sakiyama S.; RT "Interaction of DA41, a DAN-binding protein, with the epidermal growth RT factor-like protein, S(1-5)."; RL Biochem. Biophys. Res. Commun. 237:245-250(1997). RN [2] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18803302; DOI=10.1002/glia.20771; RA Vukovic J., Ruitenberg M.J., Roet K., Franssen E., Arulpragasam A., RA Sasaki T., Verhaagen J., Harvey A.R., Busfield S.J., Plant G.W.; RT "The glycoprotein fibulin-3 regulates morphology and motility of olfactory RT ensheathing cells in vitro."; RL Glia 57:424-443(2009). CC -!- FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR CC autophosphorylation and the activation of downstream signaling CC pathways. May play a role in cell adhesion and migration. May function CC as a negative regulator of chondrocyte differentiation. In the CC olfactory epithelium, it may regulate glial cell migration, CC differentiation and the ability of glial cells to support neuronal CC neurite outgrowth. {ECO:0000269|PubMed:18803302}. CC -!- SUBUNIT: Interacts with ECM1. Interacts with TIMP3. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000269|PubMed:18803302}. Secreted, extracellular space, CC extracellular matrix {ECO:0000269|PubMed:18803302}. Note=Localizes to CC the lamina propria underneath the olfactory epithelium. CC -!- TISSUE SPECIFICITY: Expressed by olfactory ensheathing cells (at CC protein level). Detected in lung, intestine and kidney. CC {ECO:0000269|PubMed:9268694}. CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D89730; BAA22265.1; -; mRNA. DR PIR; JC5621; JC5621. DR AlphaFoldDB; O35568; -. DR STRING; 10116.ENSRNOP00000004764; -. DR GlyCosmos; O35568; 1 site, No reported glycans. DR GlyGen; O35568; 1 site. DR PhosphoSitePlus; O35568; -. DR PaxDb; 10116-ENSRNOP00000004764; -. DR UCSC; RGD:1308528; rat. DR AGR; RGD:1308528; -. DR RGD; 1308528; Efemp1. DR eggNOG; KOG1217; Eukaryota. DR InParanoid; O35568; -. DR PhylomeDB; O35568; -. DR PRO; PR:O35568; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005604; C:basement membrane; IDA:RGD. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005006; F:epidermal growth factor receptor activity; ISS:UniProtKB. DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. DR GO; GO:0043010; P:camera-type eye development; ISO:RGD. DR GO; GO:0048048; P:embryonic eye morphogenesis; ISO:RGD. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:UniProtKB. DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD. DR GO; GO:0031346; P:positive regulation of cell projection organization; IDA:RGD. DR GO; GO:0048050; P:post-embryonic eye morphogenesis; ISO:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1903975; P:regulation of glial cell migration; IDA:RGD. DR CDD; cd00054; EGF_CA; 4. DR Gene3D; 2.10.25.10; Laminin; 5. DR InterPro; IPR026823; cEGF. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR PANTHER; PTHR24034:SF102; EGF-CONTAINING FIBULIN-LIKE EXTRACELLULAR MATRIX PROTEIN 1; 1. DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF12662; cEGF; 3. DR Pfam; PF07645; EGF_CA; 2. DR SMART; SM00181; EGF; 5. DR SMART; SM00179; EGF_CA; 6. DR SUPFAM; SSF57196; EGF/Laminin; 2. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 4. DR PROSITE; PS01186; EGF_2; 4. DR PROSITE; PS50026; EGF_3; 4. DR PROSITE; PS01187; EGF_CA; 6. PE 1: Evidence at protein level; KW Calcium; Disulfide bond; EGF-like domain; Extracellular matrix; KW Glycoprotein; Growth factor; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..493 FT /note="EGF-containing fibulin-like extracellular matrix FT protein 1" FT /id="PRO_0000007573" FT DOMAIN 26..71 FT /note="EGF-like 1; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 173..213 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 214..253 FT /note="EGF-like 3; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 254..293 FT /note="EGF-like 4; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 294..333 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 334..378 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 259..493 FT /note="Mediates interaction with TIMP3" FT /evidence="ECO:0000250" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 177..190 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 184..199 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 201..212 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 218..228 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 224..237 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 239..252 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 258..268 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 264..277 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 279..292 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 298..309 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 305..318 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 320..332 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 338..350 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 344..359 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 365..377 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" SQ SEQUENCE 493 AA; 54596 MW; 22DAFD70BACF1CA5 CRC64; MLQTVFLTML TLALVKSQVT EETITYTQCT DGYEWDPVRQ QCKDIDECDI VPDACKGGMK CVNHYGGYLC LPKTAQIIVN NEQPQQETPA AEASSGAATG TIAARSMATS GVIPGGGFIA SATAVAGPEV QTGRNNFVIR RNPADPQRIP SNPSHRIQCA AGYEQSEHNV CQDIDECTSG THNCRLDQVC INLRGSFTCH CLPGYQKRGE QCVDIDECSV PPYCHQGCVN TPGSFYCQCN PGFQLAANNY TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC WNYHGGFRCY PQNPCQDPYV LTSENRCVCP VSNTMCRDVP QSIVYKYMNI RSDRSVPSDI FQIQATTIYA NTINTFRIKS GNENGEFYLR QTSPVSAMLV LVKSLTGPRE HIVGLEMLTV SSIGTFRTSS VLRLTIIVGP FSF //