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Q08879 (FBLN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibulin-1
Short name=FIBL-1
Alternative name(s):
Basement-membrane protein 90
Short name=BM-90
Gene names
Name:Fbln1
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 length705 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes.

Subunit structure

Homomultimerizes and interacts with various extracellular matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and type IV collagen. Interacts also with papillomavirus E6 proteins. Binding analysis demonstrated for isoform C a 100-fold stronger binding to the basement membrane protein NID than for isoform D. Interacts with FBLN7. Ref.1 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16

Subcellular location

Secreted › extracellular space › extracellular matrix.

Tissue specificity

Detected in most organs (brain, heart, lung, spleen, liver and kidney). Neurons are the predominant source of production in the brain. Not expressed significantly by astrocytes or microglia. Ref.13

Developmental stage

The differential expression of the fibulin family contributes to the formation of molecularly distinct extracellular matrices already during early developmental stages of a large number of tissues. Increase expression at neonate stage in the brain. Expressed in interdigital regions of the handplate of a 12 dpc embryo and in the lateral perichondrial region. Similar expression persists in the 13 dpc handplate particularly in the perichondrial regions and apical aspects of the developing digits. Ref.7 Ref.13 Ref.15

Induction

Glucocorticoids suppressed mRNA expression and protein synthesis. Ref.12

Sequence similarities

Belongs to the fibulin family.

Contains 3 anaphylatoxin-like domains.

Contains 9 EGF-like domains.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform D (identifier: Q08879-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: Q08879-3)

The sequence of this isoform is not available.
Isoform B (identifier: Q08879-4)

The sequence of this isoform is not available.
Isoform C (identifier: Q08879-2)

The sequence of this isoform differs from the canonical sequence as follows:
     569-705: FRQEKTDTVR...VHIFVSEYWF → RCERLPCHEN...KLFIFVSAEL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.5
Chain30 – 705676Fibulin-1
PRO_0000007564

Regions

Domain36 – 7641Anaphylatoxin-like 1
Domain77 – 11135Anaphylatoxin-like 2
Domain112 – 14433Anaphylatoxin-like 3
Domain178 – 21740EGF-like 1
Domain218 – 26346EGF-like 2; calcium-binding Potential
Domain264 – 30946EGF-like 3; calcium-binding Potential
Domain310 – 35748EGF-like 4; calcium-binding Potential
Domain358 – 40043EGF-like 5; calcium-binding Potential
Domain401 – 44242EGF-like 6; calcium-binding Potential
Domain443 – 48240EGF-like 7; calcium-binding Potential
Domain483 – 52644EGF-like 8; calcium-binding Potential
Domain527 – 58054EGF-like 9; calcium-binding Potential
Region358 – 44285Self-association and FN1-binding By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation5371N-linked (GlcNAc...) Potential
Glycosylation5411N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 61 By similarity
Disulfide bond37 ↔ 68 By similarity
Disulfide bond50 ↔ 69 By similarity
Disulfide bond78 ↔ 109 By similarity
Disulfide bond91 ↔ 110 By similarity
Disulfide bond112 ↔ 136 By similarity
Disulfide bond113 ↔ 143 By similarity
Disulfide bond126 ↔ 144 By similarity
Disulfide bond182 ↔ 192 By similarity
Disulfide bond188 ↔ 201 By similarity
Disulfide bond203 ↔ 216 By similarity
Disulfide bond222 ↔ 235 By similarity
Disulfide bond229 ↔ 244 By similarity
Disulfide bond250 ↔ 262 By similarity
Disulfide bond268 ↔ 281 By similarity
Disulfide bond275 ↔ 290 By similarity
Disulfide bond296 ↔ 308 By similarity
Disulfide bond314 ↔ 327 By similarity
Disulfide bond321 ↔ 336 By similarity
Disulfide bond343 ↔ 356 By similarity
Disulfide bond362 ↔ 375 By similarity
Disulfide bond369 ↔ 384 By similarity
Disulfide bond386 ↔ 399 By similarity
Disulfide bond405 ↔ 417 By similarity
Disulfide bond413 ↔ 426 By similarity
Disulfide bond428 ↔ 441 By similarity
Disulfide bond447 ↔ 456 By similarity
Disulfide bond452 ↔ 465 By similarity
Disulfide bond467 ↔ 481 By similarity
Disulfide bond487 ↔ 500 By similarity
Disulfide bond496 ↔ 509 By similarity
Disulfide bond511 ↔ 525 By similarity
Disulfide bond531 ↔ 544 By similarity
Disulfide bond538 ↔ 553 By similarity
Disulfide bond558 ↔ 579 By similarity

Natural variations

Alternative sequence569 – 705137FRQEK…SEYWF → RCERLPCHENQECPRLPLRI TYYHLSFPTNIQVPAVVFRM GPSSAVPGDSMQLAITAGNE EGFFTTRKVSHHSGVVALTK PIPEPRDLLLTVKMDLYRHG TVSSFVAKLFIFVSAEL in isoform C.
VSP_001386

Experimental info

Sequence conflict301D → N AA sequence Ref.5
Sequence conflict401G → P in CAA50207. Ref.1
Sequence conflict3631S → A in CAA50207. Ref.1
Sequence conflict3851E → K in BAC39669. Ref.2
Sequence conflict5531C → Q AA sequence Ref.5
Sequence conflict5581C → Q AA sequence Ref.5
Isoform C:
Sequence conflict5711E → A in CAA50206. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform D [UniParc].

Last modified May 9, 2003. Version 2.
Checksum: 76C527A12E97D0E1

FASTA70578,033
        10         20         30         40         50         60 
MERPVPSRLV PLPLLLLSSL SLLAARANAD ISMEACCTDG NQMANQHRDC SLPYTSESKE 

        70         80         90        100        110        120 
CRMVQEQCCH NQLEELHCAT GINLASEPEG CASLHSYNSS LETIFIKRCC HCCMLGKASL 

       130        140        150        160        170        180 
ARDQTCEPIV MISYQCGLVF RACCVKAREN SDFVQGNGAD LQDPAKIPDE EDQEDPYLND 

       190        200        210        220        230        240 
RCRGGGPCKQ QCRDTGDEVI CSCFVGYQLQ SDGVSCEDIN ECITGSHNCR LGESCINTVG 

       250        260        270        280        290        300 
SFRCQRDSSC GTGYELTEDN NCKDIDECET GIHNCPPDFI CQNTLGSFRC RPKLQCKSGF 

       310        320        330        340        350        360 
IQDALGNCID INECLSISAP CPVGQTCINT EGSYTCQKNV PNCGRGYHLN EEGTRCVDVD 

       370        380        390        400        410        420 
ECSPPAEPCG KGHHCLNSPG SFRCECKAGF YFDGISRTCV DINECQRYPG RLCGHKCENT 

       430        440        450        460        470        480 
PGSFHCSCSA GFRLSVDGRS CEDVNECLNS PCSQECANVY GSYQCYCRRG YQLSDVDGVT 

       490        500        510        520        530        540 
CEDIDECALP TGGHICSYRC INIPGSFQCS CPSSGYRLAP NGRNCQDIDE CVTGIHNCSI 

       550        560        570        580        590        600 
NETCFNIQGS FRCLSFECPE NYRRSADTFR QEKTDTVRCI KSCRPNDEAC VRDPVHTVSH 

       610        620        630        640        650        660 
TVISLPTFRE FTRPEEIIFL RAVTPLYPAN QADIIFDITE GNLRDSFDII KRYEDGMTVG 

       670        680        690        700 
VVRQVRPIVG PFYAVLKLEM NYVLGGVVSH RNVVNVHIFV SEYWF

« Hide

Isoform A (Sequence not available). ––
Isoform B (Sequence not available). ––
Isoform C [UniParc].

Checksum: EF0D77D7F66B73B8
Show »

FASTA68575,284

References

« Hide 'large scale' references
[1]"Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands."
Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.
Eur. J. Biochem. 215:733-740(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), LIGANDS INTERACTION.
[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] (ISOFORM C).
Strain: C57BL/6J.
Tissue: Head and Urinary bladder.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
Tissue: Mammary tumor.
[4]"Structural and functional characterization of the human and mouse fibulin-1 gene promoters: role of Sp1 and Sp3."
Castoldi M., Chu M.-L.
Biochem. J. 362:41-50(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
[5]"Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum."
Kluge M., Mann K., Dziadek M., Timpl R.
Eur. J. Biochem. 193:651-659(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-53; 110-117; 231-243; 339-387; 434-439; 469-476; 553-563 AND 574-581.
[6]"Structural characterization of two variants of fibulin-1 that differ in nidogen affinity."
Sasaki T., Kostka G., Goehring W., Wiedemann H., Mann K., Chu M.-L., Timpl R.
J. Mol. Biol. 245:241-250(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF NID AFFINITY.
[7]"Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo."
Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.
Dev. Dyn. 205:348-364(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[8]"Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules."
Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.
J. Mol. Biol. 272:226-236(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NID-BINDING SITE.
Strain: 129/Sv.
[9]"Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins."
Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.
EMBO J. 18:863-870(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAMA2.
[10]"Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican."
Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.
J. Biol. Chem. 274:20444-20449(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACAN AND CSPG2.
[11]"Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies."
Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.
Eur. J. Biochem. 268:5119-5128(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NID.
[12]"Glucocorticoids down-regulate the extracellular matrix proteins fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma."
Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.
Eur. J. Haematol. 67:176-184(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DOWN-REGULATION BY GLUCOCORTICOIDS.
[13]"Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function."
Ohsawa I., Takamura C., Kohsaka S.
J. Neurochem. 76:1411-1420(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[14]"Interaction of oncogenic papillomavirus E6 proteins with fibulin-1."
Du M., Fan X., Hong E., Chen J.J.
Biochem. Biophys. Res. Commun. 296:962-969(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E6, INHIBITION OF E6-MEDIATED TRANSFORMATION.
[15]"The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with a complex type of synpolydactyly."
Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S., De Smet L., Fryns J.-P., Van De Ven W.J.M.
J. Med. Genet. 39:98-104(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[16]"TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding."
de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A., Fisher L.W., Fukumoto S., Yamada Y.
J. Biol. Chem. 282:30878-30888(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLN7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X70854 mRNA. Translation: CAA50207.1.
X70853 mRNA. Translation: CAA50206.1.
AK086451 mRNA. Translation: BAC39669.1.
AK035388 mRNA. Translation: BAC29054.1.
BC007140 mRNA. Translation: AAH07140.1.
AY040588 Genomic DNA. Translation: AAK82944.1.
IPIIPI00230432.
IPI00322748.
PIRS34968.
S78040.
RefSeqNP_034310.2. NM_010180.2.
UniGeneMm.297992.

3D structure databases

ProteinModelPortalQ08879.
SMRQ08879. Positions 186-564.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-245863.

PTM databases

PhosphoSiteQ08879.

Proteomic databases

PaxDbQ08879.
PRIDEQ08879.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057410; ENSMUSP00000054583; ENSMUSG00000006369.
ENSMUST00000109432; ENSMUSP00000105058; ENSMUSG00000006369.
GeneID14114.
KEGGmmu:14114.
UCSCuc007xdb.2. mouse.

Organism-specific databases

CTD2192.
MGIMGI:95487. Fbln1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00700000104154.
HOGENOMHOG000007079.
HOVERGENHBG051559.
InParanoidQ08879.
OMAMDSATEQ.
OrthoDBEOG4NGGM2.

Gene expression databases

ArrayExpressQ08879.
BgeeQ08879.
CleanExMM_FBLN1.
GenevestigatorQ08879.
GermOnlineENSMUSG00000006369. Mus musculus.

Family and domain databases

InterProIPR000020. Anaphylatoxin/fibulin.
IPR026823. cEGF.
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.
IPR017048. Fibulin-1.
[Graphical view]
PfamPF01821. ANATO. 2 hits.
PF12662. cEGF. 3 hits.
PF07645. EGF_CA. 4 hits.
[Graphical view]
PIRSFPIRSF036313. Fibulin-1. 1 hit.
SMARTSM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view]
PROSITEPS01177. ANAPHYLATOXIN_1. 3 hits.
PS01178. ANAPHYLATOXIN_2. 3 hits.
PS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBLN1. mouse.
NextBio285170.
SOURCESearch...

Entry information

Entry nameFBLN1_MOUSE
AccessionPrimary (citable) accession number: Q08879
Secondary accession number(s): Q08878 expand/collapse secondary AC list , Q8C3B1, Q91ZC9, Q922K8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 9, 2003
Last modified: May 1, 2013
This is version 133 of the entry and version 2 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents