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P37889

- FBLN2_MOUSE

UniProt

P37889 - FBLN2_MOUSE

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Protein

Fibulin-2

Gene

Fbln2

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

Functioni

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

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. extracellular matrix binding Source: MGI

GO - Biological processi

  1. positive regulation of cell-substrate adhesion Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_198998. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibulin-2
Short name:
FIBL-2
Gene namesi
Name:Fbln2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:95488. Fbln2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 12211195Fibulin-2PRO_0000007569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi435 ↔ 462By similarity
Disulfide bondi436 ↔ 469By similarity
Disulfide bondi449 ↔ 470By similarity
Disulfide bondi479 ↔ 508By similarity
Disulfide bondi492 ↔ 509By similarity
Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi511 ↔ 535By similarity
Disulfide bondi512 ↔ 542By similarity
Disulfide bondi525 ↔ 543By similarity
Disulfide bondi598 ↔ 610By similarity
Disulfide bondi606 ↔ 619By similarity
Disulfide bondi621 ↔ 634By similarity
Disulfide bondi673 ↔ 683By similarity
Disulfide bondi679 ↔ 692By similarity
Disulfide bondi694 ↔ 707By similarity
Disulfide bondi713 ↔ 726By similarity
Disulfide bondi720 ↔ 735By similarity
Glycosylationi737 – 7371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi742 ↔ 754By similarity
Disulfide bondi805 ↔ 818By similarity
Disulfide bondi812 ↔ 827By similarity
Disulfide bondi833 ↔ 845By similarity
Disulfide bondi899 ↔ 912By similarity
Disulfide bondi906 ↔ 921By similarity
Disulfide bondi923 ↔ 936By similarity
Disulfide bondi942 ↔ 954By similarity
Disulfide bondi950 ↔ 963By similarity
Disulfide bondi965 ↔ 978By similarity
Disulfide bondi984 ↔ 993By similarity
Disulfide bondi989 ↔ 1002By similarity
Disulfide bondi1004 ↔ 1017By similarity
Disulfide bondi1023 ↔ 1035By similarity
Disulfide bondi1031 ↔ 1044By similarity
Disulfide bondi1046 ↔ 1060By similarity
Disulfide bondi1066 ↔ 1079By similarity
Glycosylationi1072 – 10721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1073 ↔ 1088By similarity
Disulfide bondi1093 ↔ 1105By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP37889.
PRIDEiP37889.

PTM databases

PhosphoSiteiP37889.

Miscellaneous databases

PMAP-CutDBP37889.

Expressioni

Tissue specificityi

Component of both basement membranes and other connective tissues.

Developmental stagei

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.1 Publication

Inductioni

Glucocorticoids suppressed mRNA expression and protein synthesis.

Gene expression databases

CleanExiMM_FBLN2.
ExpressionAtlasiP37889. baseline and differential.
GenevestigatoriP37889.

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. Interacts with LAMA2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Irak1Q62406-110EBI-645953,EBI-488313

Protein-protein interaction databases

IntActiP37889. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP37889.
SMRiP37889. Positions 594-1098.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini435 – 47743Anaphylatoxin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini478 – 51033Anaphylatoxin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini511 – 54333Anaphylatoxin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini594 – 63542EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini669 – 70840EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini709 – 75547EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini756 – 80045EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini801 – 84646EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini847 – 89448EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini895 – 93743EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini938 – 97942EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini980 – 101839EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1019 – 106143EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1062 – 110645EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 434408NAdd
BLAST
Regioni27 – 176150Subdomain NA (Cys-rich)Add
BLAST
Regioni177 – 434258Subdomain NB (Cys-free)Add
BLAST
Regioni1111 – 1221111Domain IIIAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi421 – 4233Cell attachment siteSequence Analysis

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 3 anaphylatoxin-like domains.PROSITE-ProRule annotation
Contains 11 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000007079.
HOVERGENiHBG051559.
InParanoidiP37889.
KOiK17307.
OMAiSETKCER.
OrthoDBiEOG7P5T0C.
TreeFamiTF317514.

Family and domain databases

InterProiIPR000020. 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]
PfamiPF01821. ANATO. 2 hits.
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 6 hits.
[Graphical view]
SMARTiSM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 9 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
PROSITEiPS01177. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P37889-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MLLQESAGVW LALALVTALT PSPSMAVPWQ DCTGAECPLL ENCIEEALEP
60 70 80 90 100
GACCATCVQQ GCACEGYQYY DCVQGGFVDG RVPAGQSYFV DFGSTECSCP
110 120 130 140 150
PGGGKISCQF MLCPELPPNC IEAVVVADSC PQCGQVGCVH SGRKYAAGHT
160 170 180 190 200
VHLSSCRACH CPDAGGELIC YQLPGCHGNF SDAEEGDSER QYEDPYSYDQ
210 220 230 240 250
EVAEAEATTA IVNEVQAGAE GPPAALGGGN LPPSSIRVTP WPVALPRPTA
260 270 280 290 300
AAALGPPAPV QAKARRVTLD TEEDEEEEEE ETLVTEPPTA GSPGRLDSLP
310 320 330 340 350
TRSPARPGFP VQEKEAEAKA GPEENLIPDA QVTPRSVMQE GAAPLPRSGL
360 370 380 390 400
AALSPSLATD SSSEDPVKPS DHPTLSTLPP DRAQVSPSPE TPEEIPQHPQ
410 420 430 440 450
LLPRFRAEED IDPNSVHSVP RGDLDGSTKD LIETCCAAGQ QWAIDNDECQ
460 470 480 490 500
EIPENGAQSD ICRIAQRQCC ISYLKEKSCV AGVMGAKEGE TCGAEDNDTC
510 520 530 540 550
GVSLYKQCCD CCGLGLRVRA EGQSCESNPN LGYPCNHVML SCCEGEEPLI
560 570 580 590 600
VPEVRRPPEP EAAPRRVSEM EMASREALSL GTEAELPNSL PGDDQDECLM
610 620 630 640 650
LPGELCQHLC INTVGSYRCA CFPGFELQGD GRTCRPDRGA PQLDTARESA
660 670 680 690 700
PRSESAQVSP NTIPLPVPQP NTCKDNGPCR QVCRVVGDTA MCSCFPGYAI
710 720 730 740 750
MADGVSCEDQ DECLMGTHDC SWKQFCVNTL GSFYCVNHTV LCAEGYILNA
760 770 780 790 800
HRKCVDINEC VTDLHTCTRA EHCVNTPGSF QCYKALTCEP GYVLTDGECT
810 820 830 840 850
DVDECVTGTH NCQAGFSCQN TKGSFYCQAR QRCMDGFLQD PEGNCVDINE
860 870 880 890 900
CTSLLEPCRS GFSCINTVGS YTCQRNPLVC GRGYHANEEG SECVDVNECE
910 920 930 940 950
TGVHRCGEGQ LCYNLPGSYR CDCKPGFQRD AFGRTCIDVN ECWVSPGRLC
960 970 980 990 1000
QHTCENTPGS YRCSCAAGFL LAADGKHCED VNECETRRCS QECANIYGSY
1010 1020 1030 1040 1050
QCYCRQGYQL AEDGHTCTDI DECAQGAGIL CTFRCVNVPG SYQCACPEQG
1060 1070 1080 1090 1100
YTMMANGRSC KDLDECALGT HNCSEAETCH NIQGSFRCLR FDCPPNYVRV
1110 1120 1130 1140 1150
SETKCERTTC QDITECQTSP ARITHYQLNF QTGLLVPAHI FRIGPAPAFA
1160 1170 1180 1190 1200
GDTISLTITK GNEEGYFVTR RLNAYTGVVS LQRSVLEPRD FALDVEMKLW
1210 1220
RQGSVTTFLA KMYIFFTTFA P
Length:1,221
Mass (Da):131,834
Last modified:October 3, 2012 - v2
Checksum:iF74113CD292FF51C
GO
Isoform 2 (identifier: P37889-2) [UniParc]FASTAAdd to Basket

Also known as: EGF3-less

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

Show »
Length:1,174
Mass (Da):126,497
Checksum:i041D8E5939A51B18
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 15920HSGRK…SCRAC → TVAVSICWPYRPPLILPGF in AAD34456. (PubMed:10406956)CuratedAdd
BLAST
Sequence conflicti345 – 3451L → V in CAA53040. (PubMed:8245130)Curated
Sequence conflicti345 – 3451L → V in AAD34456. (PubMed:10406956)Curated
Sequence conflicti348 – 3481S → L in AAD34456. (PubMed:10406956)Curated
Sequence conflicti506 – 5061K → KQ in AAD34456. (PubMed:10406956)Curated
Sequence conflicti1102 – 11021E → Q in CAA53040. (PubMed:8245130)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei709 – 75547Missing in isoform 2. CuratedVSP_001391Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75285 mRNA. Translation: CAA53040.1.
AF135253
, 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.
CCDSiCCDS39566.1. [P37889-1]
CCDS39567.1. [P37889-2]
PIRiA49457.
RefSeqiNP_032018.2. NM_007992.2. [P37889-1]
XP_006505593.1. XM_006505530.1. [P37889-1]
UniGeneiMm.249146.
Mm.410235.

Genome annotation databases

EnsembliENSMUST00000041544; ENSMUSP00000048334; ENSMUSG00000064080. [P37889-1]
ENSMUST00000113498; ENSMUSP00000109126; ENSMUSG00000064080. [P37889-2]
GeneIDi14115.
KEGGimmu:14115.
UCSCiuc009cxw.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75285 mRNA. Translation: CAA53040.1 .
AF135253
, 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 .
CCDSi CCDS39566.1. [P37889-1 ]
CCDS39567.1. [P37889-2 ]
PIRi A49457.
RefSeqi NP_032018.2. NM_007992.2. [P37889-1 ]
XP_006505593.1. XM_006505530.1. [P37889-1 ]
UniGenei Mm.249146.
Mm.410235.

3D structure databases

ProteinModelPortali P37889.
SMRi P37889. Positions 594-1098.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P37889. 2 interactions.

PTM databases

PhosphoSitei P37889.

Proteomic databases

PaxDbi P37889.
PRIDEi P37889.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000041544 ; ENSMUSP00000048334 ; ENSMUSG00000064080 . [P37889-1 ]
ENSMUST00000113498 ; ENSMUSP00000109126 ; ENSMUSG00000064080 . [P37889-2 ]
GeneIDi 14115.
KEGGi mmu:14115.
UCSCi uc009cxw.1. mouse.

Organism-specific databases

CTDi 2199.
MGIi MGI:95488. Fbln2.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118806.
HOGENOMi HOG000007079.
HOVERGENi HBG051559.
InParanoidi P37889.
KOi K17307.
OMAi SETKCER.
OrthoDBi EOG7P5T0C.
TreeFami TF317514.

Enzyme and pathway databases

Reactomei REACT_198998. Molecules associated with elastic fibres.

Miscellaneous databases

NextBioi 285174.
PMAP-CutDB P37889.
PROi P37889.
SOURCEi Search...

Gene expression databases

CleanExi MM_FBLN2.
ExpressionAtlasi P37889. baseline and differential.
Genevestigatori P37889.

Family and domain databases

InterProi IPR000020. 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 ]
Pfami PF01821. ANATO. 2 hits.
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 6 hits.
[Graphical view ]
SMARTi SM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 9 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 4 hits.
PROSITEi PS01177. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiFBLN2_MOUSE
AccessioniPrimary (citable) accession number: P37889
Secondary accession number(s): G5E8B3, Q9WUI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 3, 2012
Last modified: October 29, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3