GenomeNet

Database: UniProt
Entry: O35568
LinkDB: O35568
Original site: O35568 
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   13-FEB-2019, entry version 128.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   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
RT   olfactory 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
CC       function as a negative regulator of chondrocyte differentiation.
CC       In the 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
CC       to 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}.
DR   EMBL; D89730; BAA22265.1; -; mRNA.
DR   PIR; JC5621; JC5621.
DR   UniGene; Rn.163265; -.
DR   ProteinModelPortal; O35568; -.
DR   SMR; O35568; -.
DR   STRING; 10116.ENSRNOP00000004764; -.
DR   PhosphoSitePlus; O35568; -.
DR   PaxDb; O35568; -.
DR   PRIDE; O35568; -.
DR   UCSC; RGD:1308528; rat.
DR   RGD; 1308528; Efemp1.
DR   eggNOG; ENOG410KD9V; Eukaryota.
DR   eggNOG; ENOG410YCRW; LUCA.
DR   HOGENOM; HOG000234337; -.
DR   HOVERGEN; HBG051560; -.
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:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0005006; F:epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
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: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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR037287; Fibulin_3/4/5.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   PANTHER; PTHR44074; PTHR44074; 1.
DR   PANTHER; PTHR44074:SF2; PTHR44074:SF2; 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; Complete proteome; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Growth factor; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    493       EGF-containing fibulin-like extracellular
FT                                matrix protein 1.
FT                                /FTId=PRO_0000007573.
FT   DOMAIN       26     71       EGF-like 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      173    213       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      214    253       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      254    293       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      294    333       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      334    378       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION      259    493       Mediates interaction with TIMP3.
FT                                {ECO:0000250}.
FT   CARBOHYD    249    249       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    177    190       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    184    199       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    201    212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    218    228       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    224    237       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    239    252       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    258    268       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    264    277       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    279    292       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    298    309       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    305    318       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    320    332       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    338    350       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    344    359       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    365    377       {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
//
DBGET integrated database retrieval system