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Q8BPB5 (FBLN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EGF-containing fibulin-like extracellular matrix protein 1
Alternative name(s):
Fibulin-3
Short name=FIBL-3
Gene names
Name:Efemp1
Synonyms:Fbln3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with ECM1 By similarity. Interacts with TIMP3 By similarity.

Subcellular location

Secreted › extracellular space By similarity. Secreted › extracellular space › extracellular matrix By similarity. Note: Localizes to the lamina propria underneath the olfactory epithelium By similarity.

Disruption phenotype

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. Ref.4

Sequence similarities

Belongs to the fibulin family.

Contains 6 EGF-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 493476EGF-containing fibulin-like extracellular matrix protein 1
PRO_0000007572

Regions

Domain26 – 7146EGF-like 1; atypical
Domain173 – 21341EGF-like 2; calcium-binding Potential
Domain214 – 25340EGF-like 3; calcium-binding Potential
Domain254 – 29340EGF-like 4; calcium-binding Potential
Domain294 – 33340EGF-like 5; calcium-binding Potential
Domain334 – 37845EGF-like 6; calcium-binding Potential
Region259 – 493235Mediates interaction with TIMP3 By similarity

Amino acid modifications

Glycosylation2491N-linked (GlcNAc...) Potential
Disulfide bond177 ↔ 190 By similarity
Disulfide bond184 ↔ 199 By similarity
Disulfide bond201 ↔ 212 By similarity
Disulfide bond218 ↔ 228 By similarity
Disulfide bond224 ↔ 237 By similarity
Disulfide bond239 ↔ 252 By similarity
Disulfide bond258 ↔ 268 By similarity
Disulfide bond264 ↔ 277 By similarity
Disulfide bond279 ↔ 292 By similarity
Disulfide bond298 ↔ 309 By similarity
Disulfide bond305 ↔ 318 By similarity
Disulfide bond320 ↔ 332 By similarity
Disulfide bond338 ↔ 350 By similarity
Disulfide bond344 ↔ 359 By similarity
Disulfide bond365 ↔ 377 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BPB5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9CEDC7BF2FF9430F

FASTA49354,953
        10         20         30         40         50         60 
MLQTLFLTML TLALVKSQYT EETITYTQCT DGYEWDPIRQ QCKDIDECDI VPDACKGGMK 

        70         80         90        100        110        120 
CVNHYGGYLC LPKTAQIIVN NEHPQQETPA AEASSGATTG TVAARSMATS GVVPGGGFMA 

       130        140        150        160        170        180 
SATAVAGPEV QTGRNNFVIR RNPADPQRIP SNPSHRIQCA AGYEQSEHNV CQDIDECTSG 

       190        200        210        220        230        240 
THNCRTDQVC INLRGSFTCQ CLPGYQKRGE QCVDIDECTV PPYCHQRCVN TPGSFYCQCS 

       250        260        270        280        290        300 
PGFQLAANNY TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT 

       310        320        330        340        350        360 
SSYLCQYQCV NEPGKFSCMC PQGYEVVRSR TCQDINECET TNECREDEMC WNYHGGFRCY 

       370        380        390        400        410        420 
PRNPCQDHYV LTSENRCVCP VSNTMCRELP QSIVYKYMSI RSDRSVPSDI FQIQATMIYA 

       430        440        450        460        470        480 
NTINTFRIKS GNENGEFYLR QTSPVSAMLV LVKSLSGPRE YIVDLEMLTV SSIGTFRTSS 

       490 
VLRLTIIVGP FSF

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression and characterization of the murine Efemp1, a gene mutated in Doyne-Honeycomb retinal dystrophy."
Ehlermann J., Weber S., Pfisterer P., Schorle H.
Gene Expr. Patterns 3:441-447(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Xiphoid cartilage.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Lack of fibulin-3 causes early aging and herniation, but not macular degeneration in mice."
McLaughlin P.J., Bakall B., Choi J., Liu Z., Sasaki T., Davis E.C., Marmorstein A.D., Marmorstein L.Y.
Hum. Mol. Genet. 16:3059-3070(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY251056 mRNA. Translation: AAP79577.1.
AY185605 mRNA. Translation: AAO37642.1.
AK077302 mRNA. Translation: BAC36738.1.
AL954346 Genomic DNA. Translation: CAI25011.1.
IPIIPI00223457.
RefSeqNP_666127.2. NM_146015.2.
UniGeneMm.44176.

3D structure databases

ProteinModelPortalQ8BPB5.
SMRQ8BPB5. Positions 44-78, 160-409.
ModBaseSearch...

PTM databases

PhosphoSiteQ8BPB5.

Proteomic databases

PaxDbQ8BPB5.
PRIDEQ8BPB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020759; ENSMUSP00000020759; ENSMUSG00000020467.
GeneID216616.
KEGGmmu:216616.
UCSCuc007ign.2. mouse.

Organism-specific databases

CTD2202.
MGIMGI:1339998. Efemp1.

Phylogenomic databases

eggNOGNOG250502.
GeneTreeENSGT00700000104291.
HOGENOMHOG000234337.
HOVERGENHBG051560.
InParanoidQ8BPB5.
OMAVQTGRNN.
OrthoDBEOG4PNXGR.

Gene expression databases

ArrayExpressQ8BPB5.
BgeeQ8BPB5.
GenevestigatorQ8BPB5.
GermOnlineENSMUSG00000020467. Mus musculus.

Family and domain databases

InterProIPR026823. cEGF.
IPR026824. Efemp1/Efemp2.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
[Graphical view]
PANTHERPTHR24048:SF2. PTHR24048:SF2. 1 hit.
PfamPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTSM00179. EGF_CA. 4 hits.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio375234.
SOURCESearch...

Entry information

Entry nameFBLN3_MOUSE
AccessionPrimary (citable) accession number: Q8BPB5
Secondary accession number(s): Q6Y3N6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents