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P37889 (FBLN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibulin-2

Short name=FIBL-2
Gene names
Name:Fbln2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Its binding to fibronectin and some other ligands is calcium dependent.

Subunit structure

Homotrimer; disulfide-linked. Interacts with LAMA2. Ref.7

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Component of both basement membranes and other connective tissues.

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. Ref.6

Induction

Glucocorticoids suppressed mRNA expression and protein synthesis. Ref.8

Sequence similarities

Belongs to the fibulin family.

Contains 3 anaphylatoxin-like domains.

Contains 11 EGF-like domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Irak1Q62406-110EBI-645953,EBI-488313

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P37889-1)

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 2 (identifier: P37889-2)

Also known as: EGF3-less;

The sequence of this isoform differs from the canonical sequence as follows:
     709-755: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.1
Chain27 – 12211195Fibulin-2
PRO_0000007569

Regions

Domain435 – 47743Anaphylatoxin-like 1
Domain478 – 51033Anaphylatoxin-like 2
Domain511 – 54333Anaphylatoxin-like 3
Domain594 – 63542EGF-like 1; calcium-binding Potential
Domain669 – 70840EGF-like 2
Domain709 – 75547EGF-like 3; calcium-binding Potential
Domain756 – 80045EGF-like 4; calcium-binding Potential
Domain801 – 84646EGF-like 5; calcium-binding Potential
Domain847 – 89448EGF-like 6; calcium-binding Potential
Domain895 – 93743EGF-like 7; calcium-binding Potential
Domain938 – 97942EGF-like 8; calcium-binding Potential
Domain980 – 101839EGF-like 9; calcium-binding Potential
Domain1019 – 106143EGF-like 10; calcium-binding Potential
Domain1062 – 110645EGF-like 11; calcium-binding Potential
Region27 – 434408N
Region27 – 176150Subdomain NA (Cys-rich)
Region177 – 434258Subdomain NB (Cys-free)
Region1111 – 1221111Domain III
Motif421 – 4233Cell attachment site Potential

Amino acid modifications

Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Glycosylation7371N-linked (GlcNAc...) Potential
Glycosylation10721N-linked (GlcNAc...) Potential
Disulfide bond435 ↔ 462 By similarity
Disulfide bond436 ↔ 469 By similarity
Disulfide bond449 ↔ 470 By similarity
Disulfide bond479 ↔ 508 By similarity
Disulfide bond492 ↔ 509 By similarity
Disulfide bond511 ↔ 535 By similarity
Disulfide bond512 ↔ 542 By similarity
Disulfide bond525 ↔ 543 By similarity
Disulfide bond598 ↔ 610 By similarity
Disulfide bond606 ↔ 619 By similarity
Disulfide bond621 ↔ 634 By similarity
Disulfide bond673 ↔ 683 By similarity
Disulfide bond679 ↔ 692 By similarity
Disulfide bond694 ↔ 707 By similarity
Disulfide bond713 ↔ 726 By similarity
Disulfide bond720 ↔ 735 By similarity
Disulfide bond742 ↔ 754 By similarity
Disulfide bond805 ↔ 818 By similarity
Disulfide bond812 ↔ 827 By similarity
Disulfide bond833 ↔ 845 By similarity
Disulfide bond899 ↔ 912 By similarity
Disulfide bond906 ↔ 921 By similarity
Disulfide bond923 ↔ 936 By similarity
Disulfide bond942 ↔ 954 By similarity
Disulfide bond950 ↔ 963 By similarity
Disulfide bond965 ↔ 978 By similarity
Disulfide bond984 ↔ 993 By similarity
Disulfide bond989 ↔ 1002 By similarity
Disulfide bond1004 ↔ 1017 By similarity
Disulfide bond1023 ↔ 1035 By similarity
Disulfide bond1031 ↔ 1044 By similarity
Disulfide bond1046 ↔ 1060 By similarity
Disulfide bond1066 ↔ 1079 By similarity
Disulfide bond1073 ↔ 1088 By similarity
Disulfide bond1093 ↔ 1105 By similarity

Natural variations

Alternative sequence709 – 75547Missing in isoform 2.
VSP_001391

Experimental info

Sequence conflict140 – 15920HSGRK…SCRAC → TVAVSICWPYRPPLILPGF in AAD34456. Ref.2
Sequence conflict3451L → V in CAA53040. Ref.1
Sequence conflict3451L → V in AAD34456. Ref.2
Sequence conflict3481S → L in AAD34456. Ref.2
Sequence conflict5061K → KQ in AAD34456. Ref.2
Sequence conflict11021E → Q in CAA53040. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: F74113CD292FF51C

FASTA1,221131,834
        10         20         30         40         50         60 
MLLQESAGVW LALALVTALT PSPSMAVPWQ DCTGAECPLL ENCIEEALEP GACCATCVQQ 

        70         80         90        100        110        120 
GCACEGYQYY DCVQGGFVDG RVPAGQSYFV DFGSTECSCP PGGGKISCQF MLCPELPPNC 

       130        140        150        160        170        180 
IEAVVVADSC PQCGQVGCVH SGRKYAAGHT VHLSSCRACH CPDAGGELIC YQLPGCHGNF 

       190        200        210        220        230        240 
SDAEEGDSER QYEDPYSYDQ EVAEAEATTA IVNEVQAGAE GPPAALGGGN LPPSSIRVTP 

       250        260        270        280        290        300 
WPVALPRPTA AAALGPPAPV QAKARRVTLD TEEDEEEEEE ETLVTEPPTA GSPGRLDSLP 

       310        320        330        340        350        360 
TRSPARPGFP VQEKEAEAKA GPEENLIPDA QVTPRSVMQE GAAPLPRSGL AALSPSLATD 

       370        380        390        400        410        420 
SSSEDPVKPS DHPTLSTLPP DRAQVSPSPE TPEEIPQHPQ LLPRFRAEED IDPNSVHSVP 

       430        440        450        460        470        480 
RGDLDGSTKD LIETCCAAGQ QWAIDNDECQ EIPENGAQSD ICRIAQRQCC ISYLKEKSCV 

       490        500        510        520        530        540 
AGVMGAKEGE TCGAEDNDTC GVSLYKQCCD CCGLGLRVRA EGQSCESNPN LGYPCNHVML 

       550        560        570        580        590        600 
SCCEGEEPLI VPEVRRPPEP EAAPRRVSEM EMASREALSL GTEAELPNSL PGDDQDECLM 

       610        620        630        640        650        660 
LPGELCQHLC INTVGSYRCA CFPGFELQGD GRTCRPDRGA PQLDTARESA PRSESAQVSP 

       670        680        690        700        710        720 
NTIPLPVPQP NTCKDNGPCR QVCRVVGDTA MCSCFPGYAI MADGVSCEDQ DECLMGTHDC 

       730        740        750        760        770        780 
SWKQFCVNTL GSFYCVNHTV LCAEGYILNA HRKCVDINEC VTDLHTCTRA EHCVNTPGSF 

       790        800        810        820        830        840 
QCYKALTCEP GYVLTDGECT DVDECVTGTH NCQAGFSCQN TKGSFYCQAR QRCMDGFLQD 

       850        860        870        880        890        900 
PEGNCVDINE CTSLLEPCRS GFSCINTVGS YTCQRNPLVC GRGYHANEEG SECVDVNECE 

       910        920        930        940        950        960 
TGVHRCGEGQ LCYNLPGSYR CDCKPGFQRD AFGRTCIDVN ECWVSPGRLC QHTCENTPGS 

       970        980        990       1000       1010       1020 
YRCSCAAGFL LAADGKHCED VNECETRRCS QECANIYGSY QCYCRQGYQL AEDGHTCTDI 

      1030       1040       1050       1060       1070       1080 
DECAQGAGIL CTFRCVNVPG SYQCACPEQG YTMMANGRSC KDLDECALGT HNCSEAETCH 

      1090       1100       1110       1120       1130       1140 
NIQGSFRCLR FDCPPNYVRV SETKCERTTC QDITECQTSP ARITHYQLNF QTGLLVPAHI 

      1150       1160       1170       1180       1190       1200 
FRIGPAPAFA GDTISLTITK GNEEGYFVTR RLNAYTGVVS LQRSVLEPRD FALDVEMKLW 

      1210       1220 
RQGSVTTFLA KMYIFFTTFA P 

« Hide

Isoform 2 (EGF3-less) [UniParc].

Checksum: 041D8E5939A51B18
Show »

FASTA1,174126,497

References

« Hide 'large scale' references
[1]"Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding."
Pan T.-C., Sasaki T., Zhang R.-Z., Faessler R., Timpl R., Chu M.-L.
J. Cell Biol. 123:1269-1277(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-35.
Tissue: Fibroblast.
[2]"Mouse fibulin-2 gene. Complete exon-intron organization and promoter characterization."
Graessel S., Sicot F.-X., Gotta S., Chu M.-L.
Eur. J. Biochem. 263:471-477(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[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]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Different susceptibilities of fibulin-1 and fibulin-2 to cleavage by matrix metalloproteinases and other tissue proteases."
Sasaki T., Mann K., Murphy G., Chu M.-L., Timpl R.
Eur. J. Biochem. 240:427-434(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[6]"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.
[7]"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.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75285 mRNA. Translation: CAA53040.1.
AF135253 expand/collapse EMBL AC list , AF135239, AF135240, AF135241, AF135242, AF135243, AF135244, AF135245, AF135246, AF135247, AF135248, AF135249, AF135250, AF135251, AF135252 Genomic DNA. Translation: AAD34456.1.
AC121990 Genomic DNA. No translation available.
AC131764 Genomic DNA. No translation available.
CH466523 Genomic DNA. Translation: EDK99296.1.
CCDSCCDS39566.1. [P37889-1]
CCDS39567.1. [P37889-2]
PIRA49457.
RefSeqNP_032018.2. NM_007992.2. [P37889-1]
XP_006505593.1. XM_006505530.1. [P37889-1]
UniGeneMm.249146.
Mm.410235.

3D structure databases

ProteinModelPortalP37889.
SMRP37889. Positions 594-627, 672-1107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP37889. 2 interactions.

PTM databases

PhosphoSiteP37889.

Proteomic databases

PaxDbP37889.
PRIDEP37889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041544; ENSMUSP00000048334; ENSMUSG00000064080. [P37889-1]
ENSMUST00000113498; ENSMUSP00000109126; ENSMUSG00000064080. [P37889-2]
GeneID14115.
KEGGmmu:14115.
UCSCuc009cxw.1. mouse.

Organism-specific databases

CTD2199.
MGIMGI:95488. Fbln2.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00750000117498.
HOGENOMHOG000007079.
HOVERGENHBG051559.
InParanoidP37889.
KOK17307.
OMASETKCER.
OrthoDBEOG7P5T0C.
TreeFamTF317514.

Gene expression databases

CleanExMM_FBLN2.
GenevestigatorP37889.

Family and domain databases

InterProIPR000020. Anaphylatoxin/fibulin.
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]
PfamPF01821. ANATO. 2 hits.
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 6 hits.
[Graphical view]
SMARTSM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 9 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 4 hits.
PROSITEPS01177. ANAPHYLATOXIN_1. 3 hits.
PS01178. ANAPHYLATOXIN_2. 3 hits.
PS00010. ASX_HYDROXYL. 5 hits.
PS01186. EGF_2. 5 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio285174.
PMAP-CutDBP37889.
PROP37889.
SOURCESearch...

Entry information

Entry nameFBLN2_MOUSE
AccessionPrimary (citable) accession number: P37889
Secondary accession number(s): G5E8B3, Q9WUI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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