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P37889

- FBLN2_MOUSE

UniProt

P37889 - FBLN2_MOUSE

Protein

Fibulin-2

Gene

Fbln2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    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

    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

    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.
    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.
    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.
    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

    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 594-627, 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

    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 1, 2014
    This is version 136 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