FBLN3_RAT
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 03-AUG-2022, entry version 136.
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}.
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DR EMBL; D89730; BAA22265.1; -; mRNA.
DR PIR; JC5621; JC5621.
DR AlphaFoldDB; O35568; -.
DR STRING; 10116.ENSRNOP00000004764; -.
DR GlyGen; O35568; 1 site.
DR PhosphoSitePlus; O35568; -.
DR PaxDb; O35568; -.
DR PRIDE; O35568; -.
DR UCSC; RGD:1308528; rat.
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:0005737; C:cytoplasm; 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:1903975; P:regulation of glial cell migration; IDA:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR032973; EFEMP1.
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; PTHR24034:SF102; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 3.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57184; SSF57184; 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
