FBLN3_MACFA
ID FBLN3_MACFA Reviewed; 493 AA.
AC Q7YQD7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=EGF-containing fibulin-like extracellular matrix protein 1;
DE AltName: Full=Fibulin-3;
DE Short=FIBL-3;
DE Flags: Precursor;
GN Name=EFEMP1; Synonyms=FBLN3;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Umeda S., Suzuki M.T., Yoshikawa Y., Tanaka Y., Iwata T.;
RT "Molecular cloning of EFEMP1 gene from cynomolgus monkey (Macaca
RT fascicularis).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ECM1. Interacts with TIMP3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC Secreted, extracellular space, extracellular matrix {ECO:0000250}.
CC Note=Localizes to the lamina propria underneath the olfactory
CC epithelium. {ECO:0000250}.
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; AY312414; AAP82236.1; -; Genomic_DNA.
DR EMBL; AY312408; AAP82236.1; JOINED; Genomic_DNA.
DR EMBL; AY312409; AAP82236.1; JOINED; Genomic_DNA.
DR EMBL; AY312410; AAP82236.1; JOINED; Genomic_DNA.
DR EMBL; AY312411; AAP82236.1; JOINED; Genomic_DNA.
DR EMBL; AY312412; AAP82236.1; JOINED; Genomic_DNA.
DR EMBL; AY312413; AAP82236.1; JOINED; Genomic_DNA.
DR EMBL; AY312415; AAP82238.1; -; mRNA.
DR RefSeq; NP_001306340.1; NM_001319411.1.
DR RefSeq; XP_015289130.1; XM_015433644.1.
DR AlphaFoldDB; Q7YQD7; -.
DR STRING; 9541.XP_005576736.1; -.
DR GeneID; 102119251; -.
DR CTD; 2202; -.
DR eggNOG; KOG1217; Eukaryota.
DR OrthoDB; 1174178at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
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: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:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
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; 2.
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 2: Evidence at transcript 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_0000007571"
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; 54547 MW; B3DAC01BC0FC1C7F CRC64;
MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI VPDACKGGMK
CVNHYGGYLC LPKTAQIIVN NEQPQQETPP AEGTSGATTG VVAASSMATS GVLPGGGFVA
SAAAVAGPEV QAGRNNFVIR RNPADPQRIP SNPSHRIQCA AGYEQSEHNV CQDIDECTAG
THNCRADQVC INLRGSFACQ CPPGYQKRGE QCVDIDECTI PPYCHQRCVN TPGSFYCQCS
PGFQLAANNY TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT
SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC WNYHGGFRCY
PRNPCQDPYI LTPENRCVCP VSNAMCRELP QSIVYKYMSI RSDRSVPSDI FQIQATTIYA
NTINTFRIKS GNENGEFYLR QTSPVSAMLV LVKSLSGPRE HIVDLEMLTV SSIGTFRTSS
VLRLTIIVGP FSF
