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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
  3. protein binding Source: IntAct

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. 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 – 26261 Publication
Add
BLAST
Chaini27 – 12211195Fibulin-2
PRO_0000007569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi179 – 1791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi435 ↔ 462 By similarity
Disulfide bondi436 ↔ 469 By similarity
Disulfide bondi449 ↔ 470 By similarity
Disulfide bondi479 ↔ 508 By similarity
Disulfide bondi492 ↔ 509 By similarity
Glycosylationi497 – 4971N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi511 ↔ 535 By similarity
Disulfide bondi512 ↔ 542 By similarity
Disulfide bondi525 ↔ 543 By similarity
Disulfide bondi598 ↔ 610 By similarity
Disulfide bondi606 ↔ 619 By similarity
Disulfide bondi621 ↔ 634 By similarity
Disulfide bondi673 ↔ 683 By similarity
Disulfide bondi679 ↔ 692 By similarity
Disulfide bondi694 ↔ 707 By similarity
Disulfide bondi713 ↔ 726 By similarity
Disulfide bondi720 ↔ 735 By similarity
Glycosylationi737 – 7371N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi742 ↔ 754 By similarity
Disulfide bondi805 ↔ 818 By similarity
Disulfide bondi812 ↔ 827 By similarity
Disulfide bondi833 ↔ 845 By similarity
Disulfide bondi899 ↔ 912 By similarity
Disulfide bondi906 ↔ 921 By similarity
Disulfide bondi923 ↔ 936 By similarity
Disulfide bondi942 ↔ 954 By similarity
Disulfide bondi950 ↔ 963 By similarity
Disulfide bondi965 ↔ 978 By similarity
Disulfide bondi984 ↔ 993 By similarity
Disulfide bondi989 ↔ 1002 By similarity
Disulfide bondi1004 ↔ 1017 By similarity
Disulfide bondi1023 ↔ 1035 By similarity
Disulfide bondi1031 ↔ 1044 By similarity
Disulfide bondi1046 ↔ 1060 By similarity
Disulfide bondi1066 ↔ 1079 By similarity
Glycosylationi1072 – 10721N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1073 ↔ 1088 By similarity
Disulfide bondi1093 ↔ 1105 By 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.1 Publication

Gene expression databases

CleanExiMM_FBLN2.
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 594-627, 672-1107.

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi421 – 4233Cell attachment site Reviewed prediction

Sequence similaritiesi

Belongs to the fibulin family.
Contains 11 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00750000117498.
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

MLLQESAGVW LALALVTALT PSPSMAVPWQ DCTGAECPLL ENCIEEALEP     50
GACCATCVQQ GCACEGYQYY DCVQGGFVDG RVPAGQSYFV DFGSTECSCP 100
PGGGKISCQF MLCPELPPNC IEAVVVADSC PQCGQVGCVH SGRKYAAGHT 150
VHLSSCRACH CPDAGGELIC YQLPGCHGNF SDAEEGDSER QYEDPYSYDQ 200
EVAEAEATTA IVNEVQAGAE GPPAALGGGN LPPSSIRVTP WPVALPRPTA 250
AAALGPPAPV QAKARRVTLD TEEDEEEEEE ETLVTEPPTA GSPGRLDSLP 300
TRSPARPGFP VQEKEAEAKA GPEENLIPDA QVTPRSVMQE GAAPLPRSGL 350
AALSPSLATD SSSEDPVKPS DHPTLSTLPP DRAQVSPSPE TPEEIPQHPQ 400
LLPRFRAEED IDPNSVHSVP RGDLDGSTKD LIETCCAAGQ QWAIDNDECQ 450
EIPENGAQSD ICRIAQRQCC ISYLKEKSCV AGVMGAKEGE TCGAEDNDTC 500
GVSLYKQCCD CCGLGLRVRA EGQSCESNPN LGYPCNHVML SCCEGEEPLI 550
VPEVRRPPEP EAAPRRVSEM EMASREALSL GTEAELPNSL PGDDQDECLM 600
LPGELCQHLC INTVGSYRCA CFPGFELQGD GRTCRPDRGA PQLDTARESA 650
PRSESAQVSP NTIPLPVPQP NTCKDNGPCR QVCRVVGDTA MCSCFPGYAI 700
MADGVSCEDQ DECLMGTHDC SWKQFCVNTL GSFYCVNHTV LCAEGYILNA 750
HRKCVDINEC VTDLHTCTRA EHCVNTPGSF QCYKALTCEP GYVLTDGECT 800
DVDECVTGTH NCQAGFSCQN TKGSFYCQAR QRCMDGFLQD PEGNCVDINE 850
CTSLLEPCRS GFSCINTVGS YTCQRNPLVC GRGYHANEEG SECVDVNECE 900
TGVHRCGEGQ LCYNLPGSYR CDCKPGFQRD AFGRTCIDVN ECWVSPGRLC 950
QHTCENTPGS YRCSCAAGFL LAADGKHCED VNECETRRCS QECANIYGSY 1000
QCYCRQGYQL AEDGHTCTDI DECAQGAGIL CTFRCVNVPG SYQCACPEQG 1050
YTMMANGRSC KDLDECALGT HNCSEAETCH NIQGSFRCLR FDCPPNYVRV 1100
SETKCERTTC QDITECQTSP ARITHYQLNF QTGLLVPAHI FRIGPAPAFA 1150
GDTISLTITK GNEEGYFVTR RLNAYTGVVS LQRSVLEPRD FALDVEMKLW 1200
RQGSVTTFLA KMYIFFTTFA P 1221
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei709 – 75547Missing in isoform 2.
VSP_001391Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 15920HSGRK…SCRAC → TVAVSICWPYRPPLILPGF in AAD34456. 1 Publication
Add
BLAST
Sequence conflicti345 – 3451L → V in CAA53040. 1 Publication
Sequence conflicti345 – 3451L → V in AAD34456. 1 Publication
Sequence conflicti348 – 3481S → L in AAD34456. 1 Publication
Sequence conflicti506 – 5061K → KQ in AAD34456. 1 Publication
Sequence conflicti1102 – 11021E → Q in CAA53040. 1 Publication

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 594-627, 672-1107.
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 ENSGT00750000117498.
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.
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: September 3, 2014
This is version 135 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

Similar proteinsi