FBLN3_MOUSE
ID FBLN3_MOUSE Reviewed; 493 AA.
AC Q8BPB5; Q6Y3N6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=EGF-containing fibulin-like extracellular matrix protein 1;
DE AltName: Full=Fibulin-3;
DE Short=FIBL-3;
DE Flags: Precursor;
GN Name=Efemp1; Synonyms=Fbln3;
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].
RC STRAIN=C57BL/6J;
RX PubMed=12915309; DOI=10.1016/s1567-133x(03)00084-x;
RA Ehlermann J., Weber S., Pfisterer P., Schorle H.;
RT "Cloning, expression and characterization of the murine Efemp1, a gene
RT mutated in Doyne-Honeycomb retinal dystrophy.";
RL Gene Expr. Patterns 3:441-447(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Xiphoid cartilage;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 DISRUPTION PHENOTYPE.
RX PubMed=17872905; DOI=10.1093/hmg/ddm264;
RA McLaughlin P.J., Bakall B., Choi J., Liu Z., Sasaki T., Davis E.C.,
RA Marmorstein A.D., Marmorstein L.Y.;
RT "Lack of fibulin-3 causes early aging and herniation, but not macular
RT degeneration in mice.";
RL Hum. Mol. Genet. 16:3059-3070(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
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: Binds EGFR, the EGF receptor, inducing EGFR
CC autophosphorylation and the activation of downstream signaling
CC pathways. May play a role in cell adhesion and migration. May function
CC as a negative regulator of chondrocyte differentiation. In the
CC olfactory epithelium, it may regulate glial cell migration,
CC differentiation and the ability of glial cells to support neuronal
CC neurite outgrowth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ECM1. Interacts with TIMP3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC Secreted, extracellular space, extracellular matrix {ECO:0000250}.
CC Note=Localizes to the lamina propria underneath the olfactory
CC epithelium. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and have no overt phenotype at
CC birth. However, they exhibit reduced reproductivity and an early onset
CC of aging-associated phenotypes including reduced lifespan, decreased
CC body mass, lordokyphosis, reduced hair growth and generalized fat,
CC muscle and organ atrophy. They also display multiple hernias associated
CC with a reduction of elastic fibers in facia, the thin layer of
CC connective tissue maintaining and protecting structures throughout the
CC body. However, there is no apparent macular degeneration.
CC {ECO:0000269|PubMed:17872905}.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AY251056; AAP79577.1; -; mRNA.
DR EMBL; AY185605; AAO37642.1; -; mRNA.
DR EMBL; AK077302; BAC36738.1; -; mRNA.
DR EMBL; AL954346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48761.1; -.
DR RefSeq; NP_666127.2; NM_146015.2.
DR RefSeq; XP_006514723.1; XM_006514660.1.
DR AlphaFoldDB; Q8BPB5; -.
DR BioGRID; 229766; 3.
DR IntAct; Q8BPB5; 2.
DR STRING; 10090.ENSMUSP00000020759; -.
DR GlyGen; Q8BPB5; 1 site.
DR iPTMnet; Q8BPB5; -.
DR PhosphoSitePlus; Q8BPB5; -.
DR CPTAC; non-CPTAC-3805; -.
DR CPTAC; non-CPTAC-5606; -.
DR MaxQB; Q8BPB5; -.
DR PaxDb; Q8BPB5; -.
DR PeptideAtlas; Q8BPB5; -.
DR PRIDE; Q8BPB5; -.
DR ProteomicsDB; 271874; -.
DR Antibodypedia; 30453; 395 antibodies from 36 providers.
DR DNASU; 216616; -.
DR Ensembl; ENSMUST00000020759; ENSMUSP00000020759; ENSMUSG00000020467.
DR GeneID; 216616; -.
DR KEGG; mmu:216616; -.
DR UCSC; uc007ign.2; mouse.
DR CTD; 2202; -.
DR MGI; MGI:1339998; Efemp1.
DR VEuPathDB; HostDB:ENSMUSG00000020467; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000157837; -.
DR HOGENOM; CLU_004826_0_1_1; -.
DR InParanoid; Q8BPB5; -.
DR OMA; HKYMSIR; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q8BPB5; -.
DR TreeFam; TF317514; -.
DR BioGRID-ORCS; 216616; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8BPB5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BPB5; protein.
DR Bgee; ENSMUSG00000020467; Expressed in ciliary body and 240 other tissues.
DR ExpressionAtlas; Q8BPB5; baseline and differential.
DR Genevisible; Q8BPB5; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005006; F:epidermal growth factor receptor activity; ISS:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0031346; P:positive regulation of cell projection organization; ISO:MGI.
DR GO; GO:0048050; P:post-embryonic eye morphogenesis; IEA:Ensembl.
DR GO; GO:1903975; P:regulation of glial cell migration; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR032973; EFEMP1.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24034:SF102; PTHR24034:SF102; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 3.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 6.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Growth factor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..493
FT /note="EGF-containing fibulin-like extracellular matrix
FT protein 1"
FT /id="PRO_0000007572"
FT DOMAIN 26..71
FT /note="EGF-like 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 173..213
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..253
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 254..293
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 294..333
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 334..378
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 259..493
FT /note="Mediates interaction with TIMP3"
FT /evidence="ECO:0000250"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 184..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 201..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 218..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 224..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 239..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 258..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 264..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 279..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 298..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 305..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 320..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 338..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 344..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 365..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 493 AA; 54953 MW; 9CEDC7BF2FF9430F CRC64;
MLQTLFLTML TLALVKSQYT EETITYTQCT DGYEWDPIRQ QCKDIDECDI VPDACKGGMK
CVNHYGGYLC LPKTAQIIVN NEHPQQETPA AEASSGATTG TVAARSMATS GVVPGGGFMA
SATAVAGPEV QTGRNNFVIR RNPADPQRIP SNPSHRIQCA AGYEQSEHNV CQDIDECTSG
THNCRTDQVC INLRGSFTCQ CLPGYQKRGE QCVDIDECTV PPYCHQRCVN TPGSFYCQCS
PGFQLAANNY TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT
SSYLCQYQCV NEPGKFSCMC PQGYEVVRSR TCQDINECET TNECREDEMC WNYHGGFRCY
PRNPCQDHYV LTSENRCVCP VSNTMCRELP QSIVYKYMSI RSDRSVPSDI FQIQATMIYA
NTINTFRIKS GNENGEFYLR QTSPVSAMLV LVKSLSGPRE YIVDLEMLTV SSIGTFRTSS
VLRLTIIVGP FSF
