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O35568

- FBLN3_RAT

UniProt

O35568 - FBLN3_RAT

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Protein
EGF-containing fibulin-like extracellular matrix protein 1
Gene
Efemp1, Fbln3
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. epidermal growth factor receptor binding Source: UniProtKB
  3. epidermal growth factor-activated receptor activity Source: UniProtKB
  4. protein binding Source: RGD

GO - Biological processi

  1. epidermal growth factor receptor signaling pathway Source: UniProtKB
  2. negative regulation of chondrocyte differentiation Source: UniProtKB
  3. peptidyl-tyrosine phosphorylation Source: UniProtKB
  4. regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
EGF-containing fibulin-like extracellular matrix protein 1
Alternative name(s):
Fibulin-3
Short name:
FIBL-3
T16 protein
Gene namesi
Name:Efemp1
Synonyms:Fbln3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1308528. Efemp1.

Subcellular locationi

Secretedextracellular space. Secretedextracellular spaceextracellular matrix
Note: Localizes to the lamina propria underneath the olfactory epithelium.1 Publication

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 493476EGF-containing fibulin-like extracellular matrix protein 1
PRO_0000007573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi177 ↔ 190 By similarity
Disulfide bondi184 ↔ 199 By similarity
Disulfide bondi201 ↔ 212 By similarity
Disulfide bondi218 ↔ 228 By similarity
Disulfide bondi224 ↔ 237 By similarity
Disulfide bondi239 ↔ 252 By similarity
Glycosylationi249 – 2491N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi258 ↔ 268 By similarity
Disulfide bondi264 ↔ 277 By similarity
Disulfide bondi279 ↔ 292 By similarity
Disulfide bondi298 ↔ 309 By similarity
Disulfide bondi305 ↔ 318 By similarity
Disulfide bondi320 ↔ 332 By similarity
Disulfide bondi338 ↔ 350 By similarity
Disulfide bondi344 ↔ 359 By similarity
Disulfide bondi365 ↔ 377 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO35568.
PRIDEiO35568.

PTM databases

PhosphoSiteiO35568.

Expressioni

Tissue specificityi

Expressed by olfactory ensheathing cells (at protein level). Detected in lung, intestine and kidney.1 Publication

Gene expression databases

GenevestigatoriO35568.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062660.

Structurei

3D structure databases

ProteinModelPortaliO35568.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 7146EGF-like 1; atypical
Add
BLAST
Domaini173 – 21341EGF-like 2; calcium-binding Reviewed prediction
Add
BLAST
Domaini214 – 25340EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini254 – 29340EGF-like 4; calcium-binding Reviewed prediction
Add
BLAST
Domaini294 – 33340EGF-like 5; calcium-binding Reviewed prediction
Add
BLAST
Domaini334 – 37845EGF-like 6; calcium-binding Reviewed prediction
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni259 – 493235Mediates interaction with TIMP3 By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the fibulin family.
Contains 6 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG250502.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiO35568.
PhylomeDBiO35568.

Family and domain databases

InterProiIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF12662. cEGF. 3 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view]
SMARTiSM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
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.

O35568-1 [UniParc]FASTAAdd to Basket

« Hide

MLQTVFLTML TLALVKSQVT EETITYTQCT DGYEWDPVRQ QCKDIDECDI    50
VPDACKGGMK CVNHYGGYLC LPKTAQIIVN NEQPQQETPA AEASSGAATG 100
TIAARSMATS GVIPGGGFIA SATAVAGPEV QTGRNNFVIR RNPADPQRIP 150
SNPSHRIQCA AGYEQSEHNV CQDIDECTSG THNCRLDQVC INLRGSFTCH 200
CLPGYQKRGE QCVDIDECSV PPYCHQGCVN TPGSFYCQCN PGFQLAANNY 250
TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT 300
SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC 350
WNYHGGFRCY PQNPCQDPYV LTSENRCVCP VSNTMCRDVP QSIVYKYMNI 400
RSDRSVPSDI FQIQATTIYA NTINTFRIKS GNENGEFYLR QTSPVSAMLV 450
LVKSLTGPRE HIVGLEMLTV SSIGTFRTSS VLRLTIIVGP FSF 493
Length:493
Mass (Da):54,596
Last modified:January 1, 1998 - v1
Checksum:i22DAFD70BACF1CA5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D89730 mRNA. Translation: BAA22265.1.
PIRiJC5621.
UniGeneiRn.163265.

Genome annotation databases

UCSCiRGD:1308528. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D89730 mRNA. Translation: BAA22265.1 .
PIRi JC5621.
UniGenei Rn.163265.

3D structure databases

ProteinModelPortali O35568.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000062660.

PTM databases

PhosphoSitei O35568.

Proteomic databases

PaxDbi O35568.
PRIDEi O35568.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:1308528. rat.

Organism-specific databases

RGDi 1308528. Efemp1.

Phylogenomic databases

eggNOGi NOG250502.
HOGENOMi HOG000234337.
HOVERGENi HBG051560.
InParanoidi O35568.
PhylomeDBi O35568.

Miscellaneous databases

PROi O35568.

Gene expression databases

Genevestigatori O35568.

Family and domain databases

InterProi IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view ]
Pfami PF12662. cEGF. 3 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view ]
SMARTi SM00179. EGF_CA. 4 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 1 hit.
PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Interaction of DA41, a DAN-binding protein, with the epidermal growth factor-like protein, S(1-5)."
    Ozaki T., Kondo K., Nakamura Y., Ichimiya S., Nakagawara A., Sakiyama S.
    Biochem. Biophys. Res. Commun. 237:245-250(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Lung.
  2. "The glycoprotein fibulin-3 regulates morphology and motility of olfactory ensheathing cells in vitro."
    Vukovic J., Ruitenberg M.J., Roet K., Franssen E., Arulpragasam A., Sasaki T., Verhaagen J., Harvey A.R., Busfield S.J., Plant G.W.
    Glia 57:424-443(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFBLN3_RAT
AccessioniPrimary (citable) accession number: O35568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 108 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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