FBLN2_MOUSE
ID FBLN2_MOUSE Reviewed; 1221 AA.
AC P37889; G5E8B3; Q9WUI2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Fibulin-2;
DE Short=FIBL-2;
DE Flags: Precursor;
GN Name=Fbln2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-35.
RC TISSUE=Fibroblast;
RX PubMed=8245130; DOI=10.1083/jcb.123.5.1269;
RA Pan T.-C., Sasaki T., Zhang R.-Z., Faessler R., Timpl R., Chu M.-L.;
RT "Structure and expression of fibulin-2, a novel extracellular matrix
RT protein with multiple EGF-like repeats and consensus motifs for calcium
RT binding.";
RL J. Cell Biol. 123:1269-1277(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10406956; DOI=10.1046/j.1432-1327.1999.00523.x;
RA Graessel S., Sicot F.-X., Gotta S., Chu M.-L.;
RT "Mouse fibulin-2 gene. Complete exon-intron organization and promoter
RT characterization.";
RL Eur. J. Biochem. 263:471-477(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8841408; DOI=10.1111/j.1432-1033.1996.0427h.x;
RA Sasaki T., Mann K., Murphy G., Chu M.-L., Timpl R.;
RT "Different susceptibilities of fibulin-1 and fibulin-2 to cleavage by
RT matrix metalloproteinases and other tissue proteases.";
RL Eur. J. Biochem. 240:427-434(1996).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=8850569;
RX DOI=10.1002/(sici)1097-0177(199603)205:3<348::aid-aja13>3.0.co;2-0;
RA Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.;
RT "Fibulin-1 and fibulin-2 expression during organogenesis in the developing
RT mouse embryo.";
RL Dev. Dyn. 205:348-364(1996).
RN [7]
RP INTERACTION WITH LAMA2.
RX PubMed=10022829; DOI=10.1093/emboj/18.4.863;
RA Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.;
RT "Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan
RT to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix
RT proteins.";
RL EMBO J. 18:863-870(1999).
RN [8]
RP DOWN-REGULATION BY GLUCOCORTICOIDS.
RX PubMed=11737251; DOI=10.1034/j.1600-0609.2001.5790528.x;
RA Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.;
RT "Glucocorticoids down-regulate the extracellular matrix proteins
RT fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma.";
RL Eur. J. Haematol. 67:176-184(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Its binding to fibronectin and some other ligands is calcium
CC dependent. May act as an adapter that mediates the interaction between
CC FBN1 and ELN. {ECO:0000250|UniProtKB:P98095}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Interacts with LAMA2
CC (PubMed:10022829). Interacts with FBN1 (via N-terminal domain). Forms a
CC ternary complex with ELN and FBN1 (By similarity).
CC {ECO:0000250|UniProtKB:P98095, ECO:0000269|PubMed:10022829}.
CC -!- INTERACTION:
CC P37889-1; Q62406-1: Irak1; NbExp=10; IntAct=EBI-645953, EBI-488313;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P37889-1; Sequence=Displayed;
CC Name=2; Synonyms=EGF3-less;
CC IsoId=P37889-2; Sequence=VSP_001391;
CC -!- TISSUE SPECIFICITY: Component of both basement membranes and other
CC connective tissues.
CC -!- DEVELOPMENTAL STAGE: The differential expression of the fibulin family
CC contributes to the formation of molecularly distinct extracellular
CC matrices already during early developmental stages of a large number of
CC tissues. {ECO:0000269|PubMed:8850569}.
CC -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC synthesis.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; X75285; CAA53040.1; -; mRNA.
DR EMBL; AF135253; AAD34456.1; -; Genomic_DNA.
DR EMBL; AF135239; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135240; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135241; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135242; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135243; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135244; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135245; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135246; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135247; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135248; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135249; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135250; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135251; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AF135252; AAD34456.1; JOINED; Genomic_DNA.
DR EMBL; AC121990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466523; EDK99296.1; -; Genomic_DNA.
DR CCDS; CCDS39566.1; -. [P37889-1]
DR CCDS; CCDS39567.1; -. [P37889-2]
DR PIR; A49457; A49457.
DR RefSeq; NP_032018.2; NM_007992.2. [P37889-1]
DR RefSeq; XP_006505593.1; XM_006505530.3. [P37889-1]
DR AlphaFoldDB; P37889; -.
DR BioGRID; 199606; 9.
DR IntAct; P37889; 5.
DR STRING; 10090.ENSMUSP00000048334; -.
DR GlyGen; P37889; 4 sites.
DR iPTMnet; P37889; -.
DR PhosphoSitePlus; P37889; -.
DR CPTAC; non-CPTAC-3981; -.
DR jPOST; P37889; -.
DR MaxQB; P37889; -.
DR PaxDb; P37889; -.
DR PeptideAtlas; P37889; -.
DR PRIDE; P37889; -.
DR ProteomicsDB; 267342; -. [P37889-1]
DR ProteomicsDB; 267343; -. [P37889-2]
DR Antibodypedia; 1165; 273 antibodies from 32 providers.
DR DNASU; 14115; -.
DR Ensembl; ENSMUST00000041544; ENSMUSP00000048334; ENSMUSG00000064080. [P37889-1]
DR Ensembl; ENSMUST00000113498; ENSMUSP00000109126; ENSMUSG00000064080. [P37889-2]
DR GeneID; 14115; -.
DR KEGG; mmu:14115; -.
DR UCSC; uc009cxw.1; mouse. [P37889-1]
DR CTD; 2199; -.
DR MGI; MGI:95488; Fbln2.
DR VEuPathDB; HostDB:ENSMUSG00000064080; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156047; -.
DR HOGENOM; CLU_268948_0_0_1; -.
DR InParanoid; P37889; -.
DR OMA; ICTRWTS; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; P37889; -.
DR TreeFam; TF317514; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 14115; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Fbln2; mouse.
DR PRO; PR:P37889; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P37889; protein.
DR Bgee; ENSMUSG00000064080; Expressed in stroma of bone marrow and 252 other tissues.
DR ExpressionAtlas; P37889; baseline and differential.
DR Genevisible; P37889; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR CDD; cd00017; ANATO; 2.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR037286; Fibulin-2.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24039:SF32; PTHR24039:SF32; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 6.
DR SMART; SM00104; ANATO; 3.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 10.
DR SUPFAM; SSF57184; SSF57184; 3.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 3.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:8245130"
FT CHAIN 27..1221
FT /note="Fibulin-2"
FT /id="PRO_0000007569"
FT DOMAIN 435..477
FT /note="Anaphylatoxin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 478..510
FT /note="Anaphylatoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 511..543
FT /note="Anaphylatoxin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 594..635
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 669..708
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 709..755
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 756..800
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 801..846
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 847..894
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 895..937
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 938..979
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 980..1018
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1019..1061
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1062..1106
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 27..434
FT /note="N"
FT REGION 27..176
FT /note="Subdomain NA (Cys-rich)"
FT REGION 177..434
FT /note="Subdomain NB (Cys-free)"
FT REGION 248..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1221
FT /note="Domain III"
FT MOTIF 421..423
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 354..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 435..462
FT /evidence="ECO:0000250"
FT DISULFID 436..469
FT /evidence="ECO:0000250"
FT DISULFID 449..470
FT /evidence="ECO:0000250"
FT DISULFID 479..508
FT /evidence="ECO:0000250"
FT DISULFID 492..509
FT /evidence="ECO:0000250"
FT DISULFID 511..535
FT /evidence="ECO:0000250"
FT DISULFID 512..542
FT /evidence="ECO:0000250"
FT DISULFID 525..543
FT /evidence="ECO:0000250"
FT DISULFID 598..610
FT /evidence="ECO:0000250"
FT DISULFID 606..619
FT /evidence="ECO:0000250"
FT DISULFID 621..634
FT /evidence="ECO:0000250"
FT DISULFID 673..683
FT /evidence="ECO:0000250"
FT DISULFID 679..692
FT /evidence="ECO:0000250"
FT DISULFID 694..707
FT /evidence="ECO:0000250"
FT DISULFID 713..726
FT /evidence="ECO:0000250"
FT DISULFID 720..735
FT /evidence="ECO:0000250"
FT DISULFID 742..754
FT /evidence="ECO:0000250"
FT DISULFID 805..818
FT /evidence="ECO:0000250"
FT DISULFID 812..827
FT /evidence="ECO:0000250"
FT DISULFID 833..845
FT /evidence="ECO:0000250"
FT DISULFID 899..912
FT /evidence="ECO:0000250"
FT DISULFID 906..921
FT /evidence="ECO:0000250"
FT DISULFID 923..936
FT /evidence="ECO:0000250"
FT DISULFID 942..954
FT /evidence="ECO:0000250"
FT DISULFID 950..963
FT /evidence="ECO:0000250"
FT DISULFID 965..978
FT /evidence="ECO:0000250"
FT DISULFID 984..993
FT /evidence="ECO:0000250"
FT DISULFID 989..1002
FT /evidence="ECO:0000250"
FT DISULFID 1004..1017
FT /evidence="ECO:0000250"
FT DISULFID 1023..1035
FT /evidence="ECO:0000250"
FT DISULFID 1031..1044
FT /evidence="ECO:0000250"
FT DISULFID 1046..1060
FT /evidence="ECO:0000250"
FT DISULFID 1066..1079
FT /evidence="ECO:0000250"
FT DISULFID 1073..1088
FT /evidence="ECO:0000250"
FT DISULFID 1093..1105
FT /evidence="ECO:0000250"
FT VAR_SEQ 709..755
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001391"
FT CONFLICT 140..159
FT /note="HSGRKYAAGHTVHLSSCRAC -> TVAVSICWPYRPPLILPGF (in Ref.
FT 2; AAD34456)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="L -> V (in Ref. 1; CAA53040 and 2; AAD34456)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="S -> L (in Ref. 2; AAD34456)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="K -> KQ (in Ref. 2; AAD34456)"
FT /evidence="ECO:0000305"
FT CONFLICT 1102
FT /note="E -> Q (in Ref. 1; CAA53040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1221 AA; 131834 MW; F74113CD292FF51C CRC64;
MLLQESAGVW LALALVTALT PSPSMAVPWQ DCTGAECPLL ENCIEEALEP GACCATCVQQ
GCACEGYQYY DCVQGGFVDG RVPAGQSYFV DFGSTECSCP PGGGKISCQF MLCPELPPNC
IEAVVVADSC PQCGQVGCVH SGRKYAAGHT VHLSSCRACH CPDAGGELIC YQLPGCHGNF
SDAEEGDSER QYEDPYSYDQ EVAEAEATTA IVNEVQAGAE GPPAALGGGN LPPSSIRVTP
WPVALPRPTA AAALGPPAPV QAKARRVTLD TEEDEEEEEE ETLVTEPPTA GSPGRLDSLP
TRSPARPGFP VQEKEAEAKA GPEENLIPDA QVTPRSVMQE GAAPLPRSGL AALSPSLATD
SSSEDPVKPS DHPTLSTLPP DRAQVSPSPE TPEEIPQHPQ LLPRFRAEED IDPNSVHSVP
RGDLDGSTKD LIETCCAAGQ QWAIDNDECQ EIPENGAQSD ICRIAQRQCC ISYLKEKSCV
AGVMGAKEGE TCGAEDNDTC GVSLYKQCCD CCGLGLRVRA EGQSCESNPN LGYPCNHVML
SCCEGEEPLI VPEVRRPPEP EAAPRRVSEM EMASREALSL GTEAELPNSL PGDDQDECLM
LPGELCQHLC INTVGSYRCA CFPGFELQGD GRTCRPDRGA PQLDTARESA PRSESAQVSP
NTIPLPVPQP NTCKDNGPCR QVCRVVGDTA MCSCFPGYAI MADGVSCEDQ DECLMGTHDC
SWKQFCVNTL GSFYCVNHTV LCAEGYILNA HRKCVDINEC VTDLHTCTRA EHCVNTPGSF
QCYKALTCEP GYVLTDGECT DVDECVTGTH NCQAGFSCQN TKGSFYCQAR QRCMDGFLQD
PEGNCVDINE CTSLLEPCRS GFSCINTVGS YTCQRNPLVC GRGYHANEEG SECVDVNECE
TGVHRCGEGQ LCYNLPGSYR CDCKPGFQRD AFGRTCIDVN ECWVSPGRLC QHTCENTPGS
YRCSCAAGFL LAADGKHCED VNECETRRCS QECANIYGSY QCYCRQGYQL AEDGHTCTDI
DECAQGAGIL CTFRCVNVPG SYQCACPEQG YTMMANGRSC KDLDECALGT HNCSEAETCH
NIQGSFRCLR FDCPPNYVRV SETKCERTTC QDITECQTSP ARITHYQLNF QTGLLVPAHI
FRIGPAPAFA GDTISLTITK GNEEGYFVTR RLNAYTGVVS LQRSVLEPRD FALDVEMKLW
RQGSVTTFLA KMYIFFTTFA P
