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Protein

EGF-containing fibulin-like extracellular matrix protein 1

Gene

Efemp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-MMU-2129379. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
EGF-containing fibulin-like extracellular matrix protein 1
Alternative name(s):
Fibulin-3
Short name:
FIBL-3
Gene namesi
Name:Efemp1
Synonyms:Fbln3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1339998. Efemp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are viable and have no overt phenotype at birth. However, they exhibit reduced reproductivity and an early onset of aging-associated phenotypes including reduced lifespan, decreased body mass, lordokyphosis, reduced hair growth and generalized fat, muscle and organ atrophy. They also display multiple hernias associated with a reduction of elastic fibers in facia, the thin layer of connective tissue maintaining and protecting structures throughout the body. However, there is no apparent macular degeneration.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000757218 – 493EGF-containing fibulin-like extracellular matrix protein 1Add BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi177 ↔ 190PROSITE-ProRule annotation
Disulfide bondi184 ↔ 199PROSITE-ProRule annotation
Disulfide bondi201 ↔ 212PROSITE-ProRule annotation
Disulfide bondi218 ↔ 228PROSITE-ProRule annotation
Disulfide bondi224 ↔ 237PROSITE-ProRule annotation
Disulfide bondi239 ↔ 252PROSITE-ProRule annotation
Glycosylationi249N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi258 ↔ 268PROSITE-ProRule annotation
Disulfide bondi264 ↔ 277PROSITE-ProRule annotation
Disulfide bondi279 ↔ 292PROSITE-ProRule annotation
Disulfide bondi298 ↔ 309PROSITE-ProRule annotation
Disulfide bondi305 ↔ 318PROSITE-ProRule annotation
Disulfide bondi320 ↔ 332PROSITE-ProRule annotation
Disulfide bondi338 ↔ 350PROSITE-ProRule annotation
Disulfide bondi344 ↔ 359PROSITE-ProRule annotation
Disulfide bondi365 ↔ 377PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8BPB5.
PaxDbiQ8BPB5.
PeptideAtlasiQ8BPB5.
PRIDEiQ8BPB5.

PTM databases

iPTMnetiQ8BPB5.
PhosphoSitePlusiQ8BPB5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020467.
ExpressionAtlasiQ8BPB5. baseline and differential.
GenevisibleiQ8BPB5. MM.

Interactioni

Subunit structurei

Interacts with ECM1. Interacts with TIMP3.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8BPB5. 1 interactor.
STRINGi10090.ENSMUSP00000020759.

Structurei

3D structure databases

ProteinModelPortaliQ8BPB5.
SMRiQ8BPB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 71EGF-like 1; atypicalPROSITE-ProRule annotationAdd BLAST46
Domaini173 – 213EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini214 – 253EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini254 – 293EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini294 – 333EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini334 – 378EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni259 – 493Mediates interaction with TIMP3By similarityAdd BLAST235

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 6 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410KD9V. Eukaryota.
ENOG410YCRW. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiQ8BPB5.
KOiK18262.
OMAiVQTGRNN.
OrthoDBiEOG091G04QP.
PhylomeDBiQ8BPB5.
TreeFamiTF317514.

Family and domain databases

InterProiIPR026823. cEGF.
IPR032973. EFEMP1.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
[Graphical view]
PANTHERiPTHR24044:SF310. PTHR24044:SF310. 2 hits.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 3 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BPB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQTLFLTML TLALVKSQYT EETITYTQCT DGYEWDPIRQ QCKDIDECDI
60 70 80 90 100
VPDACKGGMK CVNHYGGYLC LPKTAQIIVN NEHPQQETPA AEASSGATTG
110 120 130 140 150
TVAARSMATS GVVPGGGFMA SATAVAGPEV QTGRNNFVIR RNPADPQRIP
160 170 180 190 200
SNPSHRIQCA AGYEQSEHNV CQDIDECTSG THNCRTDQVC INLRGSFTCQ
210 220 230 240 250
CLPGYQKRGE QCVDIDECTV PPYCHQRCVN TPGSFYCQCS PGFQLAANNY
260 270 280 290 300
TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT
310 320 330 340 350
SSYLCQYQCV NEPGKFSCMC PQGYEVVRSR TCQDINECET TNECREDEMC
360 370 380 390 400
WNYHGGFRCY PRNPCQDHYV LTSENRCVCP VSNTMCRELP QSIVYKYMSI
410 420 430 440 450
RSDRSVPSDI FQIQATMIYA NTINTFRIKS GNENGEFYLR QTSPVSAMLV
460 470 480 490
LVKSLSGPRE YIVDLEMLTV SSIGTFRTSS VLRLTIIVGP FSF
Length:493
Mass (Da):54,953
Last modified:March 1, 2003 - v1
Checksum:i9CEDC7BF2FF9430F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY251056 mRNA. Translation: AAP79577.1.
AY185605 mRNA. Translation: AAO37642.1.
AK077302 mRNA. Translation: BAC36738.1.
AL954346 Genomic DNA. Translation: CAI25011.1.
CCDSiCCDS48761.1.
RefSeqiNP_666127.2. NM_146015.2.
XP_006514723.1. XM_006514660.1.
UniGeneiMm.44176.

Genome annotation databases

EnsembliENSMUST00000020759; ENSMUSP00000020759; ENSMUSG00000020467.
GeneIDi216616.
KEGGimmu:216616.
UCSCiuc007ign.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY251056 mRNA. Translation: AAP79577.1.
AY185605 mRNA. Translation: AAO37642.1.
AK077302 mRNA. Translation: BAC36738.1.
AL954346 Genomic DNA. Translation: CAI25011.1.
CCDSiCCDS48761.1.
RefSeqiNP_666127.2. NM_146015.2.
XP_006514723.1. XM_006514660.1.
UniGeneiMm.44176.

3D structure databases

ProteinModelPortaliQ8BPB5.
SMRiQ8BPB5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BPB5. 1 interactor.
STRINGi10090.ENSMUSP00000020759.

PTM databases

iPTMnetiQ8BPB5.
PhosphoSitePlusiQ8BPB5.

Proteomic databases

MaxQBiQ8BPB5.
PaxDbiQ8BPB5.
PeptideAtlasiQ8BPB5.
PRIDEiQ8BPB5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020759; ENSMUSP00000020759; ENSMUSG00000020467.
GeneIDi216616.
KEGGimmu:216616.
UCSCiuc007ign.2. mouse.

Organism-specific databases

CTDi2202.
MGIiMGI:1339998. Efemp1.

Phylogenomic databases

eggNOGiENOG410KD9V. Eukaryota.
ENOG410YCRW. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiQ8BPB5.
KOiK18262.
OMAiVQTGRNN.
OrthoDBiEOG091G04QP.
PhylomeDBiQ8BPB5.
TreeFamiTF317514.

Enzyme and pathway databases

ReactomeiR-MMU-2129379. Molecules associated with elastic fibres.

Miscellaneous databases

PROiQ8BPB5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020467.
ExpressionAtlasiQ8BPB5. baseline and differential.
GenevisibleiQ8BPB5. MM.

Family and domain databases

InterProiIPR026823. cEGF.
IPR032973. EFEMP1.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
[Graphical view]
PANTHERiPTHR24044:SF310. PTHR24044:SF310. 2 hits.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 3 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFBLN3_MOUSE
AccessioniPrimary (citable) accession number: Q8BPB5
Secondary accession number(s): Q6Y3N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2003
Last modified: November 30, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.