FBLN5_MOUSE
ID FBLN5_MOUSE Reviewed; 448 AA.
AC Q9WVH9; Q541Z7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Fibulin-5;
DE Short=FIBL-5;
DE AltName: Full=Developmental arteries and neural crest EGF-like protein;
DE Short=Dance;
DE Flags: Precursor;
GN Name=Fbln5; Synonyms=Dance;
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].
RX PubMed=10428823; DOI=10.1074/jbc.274.32.22476;
RA Nakamura T., Ruiz-Lozano P., Lindner V., Yabe D., Taniwaki M., Furukawa Y.,
RA Kobuke K., Tashiro K., Lu Z., Andon N.L., Schaub R., Matsumori A.,
RA Sasayama S., Chien K.R., Honjo T.;
RT "DANCE, a novel secreted RGD protein expressed in developing,
RT atherosclerotic, and balloon-injured arteries.";
RL J. Biol. Chem. 274:22476-22483(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Lung;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ITGAV/ITGB3;
RP ITGAV/ITGB5 AND ITGA9/ITGB1.
RX PubMed=11805835; DOI=10.1038/415171a;
RA Nakamura T., Lozano P.R., Ikeda Y., Iwanaga Y., Hinek A., Minamisawa S.,
RA Cheng C.F., Kobuke K., Dalton N., Takada Y., Tashiro K., Ross J., Honjo T.,
RA Chien K.R.;
RT "Fibulin-5/DANCE is essential for elastogenesis in vivo.";
RL Nature 415:171-175(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, 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: Essential for elastic fiber formation, is involved in the
CC assembly of continuous elastin (ELN) polymer and promotes the
CC interaction of microfibrils and ELN (By similarity). Stabilizes and
CC organizes elastic fibers in the skin, lung and vasculature. Promotes
CC adhesion of endothelial cells through interaction of integrins and the
CC RGD motif. Vascular ligand for integrin receptors which may play a role
CC in vascular development and remodeling (PubMed:11805835). May act as an
CC adapter that mediates the interaction between FBN1 and ELN (By
CC similarity). {ECO:0000250|UniProtKB:Q9UBX5,
CC ECO:0000269|PubMed:11805835}.
CC -!- SUBUNIT: Homodimer. Monomer, homodimerizes in presence of Ca(2+).
CC Interacts with ELN (By similarity). Interacts (via N-terminus) with the
CC integrins ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1 (PubMed:11805835).
CC Interacts with FBN1 (via N-terminal domain). Forms a ternary complex
CC with ELN and FBN1 (By similarity). Interacts with EFEMP2 with moderate
CC affinity (By similarity). {ECO:0000250|UniProtKB:Q9UBX5,
CC ECO:0000269|PubMed:11805835}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9UBX5}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:Q9UBX5}. Note=co-localizes with ELN in elastic
CC fibers. {ECO:0000250|UniProtKB:Q9UBX5}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UBX5}.
CC -!- DISRUPTION PHENOTYPE: Mice survive to adulthood, but have a tortuous
CC aorta with loss of compliance, severe emphisema and loose skin. They
CC exhibit a severely disorganized elastic fiber system throughout the
CC body. {ECO:0000269|PubMed:11805835}.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AF112151; AAD41767.1; -; mRNA.
DR EMBL; AK085170; BAC39381.1; -; mRNA.
DR EMBL; AK090129; BAC41109.1; -; mRNA.
DR EMBL; AK159471; BAE35112.1; -; mRNA.
DR EMBL; AK159960; BAE35515.1; -; mRNA.
DR EMBL; AK165018; BAE38002.1; -; mRNA.
DR EMBL; BC006636; AAH06636.1; -; mRNA.
DR CCDS; CCDS36525.1; -.
DR RefSeq; NP_035942.1; NM_011812.4.
DR AlphaFoldDB; Q9WVH9; -.
DR BioGRID; 204769; 1.
DR IntAct; Q9WVH9; 2.
DR MINT; Q9WVH9; -.
DR STRING; 10090.ENSMUSP00000021603; -.
DR GlyConnect; 2315; 2 N-Linked glycans (1 site).
DR GlyGen; Q9WVH9; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9WVH9; -.
DR PhosphoSitePlus; Q9WVH9; -.
DR MaxQB; Q9WVH9; -.
DR PaxDb; Q9WVH9; -.
DR PeptideAtlas; Q9WVH9; -.
DR PRIDE; Q9WVH9; -.
DR ProteomicsDB; 272957; -.
DR Antibodypedia; 72; 457 antibodies from 38 providers.
DR DNASU; 23876; -.
DR Ensembl; ENSMUST00000021603; ENSMUSP00000021603; ENSMUSG00000021186.
DR GeneID; 23876; -.
DR KEGG; mmu:23876; -.
DR UCSC; uc007otp.2; mouse.
DR CTD; 10516; -.
DR MGI; MGI:1346091; Fbln5.
DR VEuPathDB; HostDB:ENSMUSG00000021186; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000158774; -.
DR HOGENOM; CLU_004826_0_1_1; -.
DR InParanoid; Q9WVH9; -.
DR OMA; ACRGDMV; -.
DR PhylomeDB; Q9WVH9; -.
DR TreeFam; TF317514; -.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 23876; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Fbln5; mouse.
DR PRO; PR:Q9WVH9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9WVH9; protein.
DR Bgee; ENSMUSG00000021186; Expressed in external carotid artery and 237 other tissues.
DR ExpressionAtlas; Q9WVH9; baseline and differential.
DR Genevisible; Q9WVH9; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0048251; P:elastic fiber assembly; IMP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0098867; P:intramembranous bone growth; IMP:CACAO.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:CACAO.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CACAO.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CACAO.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:BHF-UCL.
DR GO; GO:2000121; P:regulation of removal of superoxide radicals; IMP:BHF-UCL.
DR GO; GO:0046903; P:secretion; ISO:MGI.
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; IPR037288; Fibulin-5.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24050:SF21; PTHR24050:SF21; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 2.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 6.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..448
FT /note="Fibulin-5"
FT /id="PRO_0000007578"
FT DOMAIN 42..82
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 127..167
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 168..206
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 207..246
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 247..287
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 288..333
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOTIF 54..56
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 53..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 131..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 138..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 155..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 172..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 177..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 192..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 211..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 217..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 232..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 251..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 258..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 273..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 292..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 320..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 448 AA; 50193 MW; F15CC70CCFBFDC97 CRC64;
MPGLKRILTV TILALWLPHP GNAQQQCTNG FDLDRQSGQC LDIDECRTIP EACRGDMMCV
NQNGGYLCIP RTNPVYRGPY SNPYSTSYSG PYPAAAPPVP ASNYPTISRP LVCRFGYQMD
EGNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL
CANVPGSYSC TCNPGFTLND DGRSCQDVNE CETENPCVQT CVNTYGSFIC RCDPGYELEE
DGIHCSDMDE CSFSEFLCQH ECVNQPGSYF CSCPPGYVLL DDNRSCQDIN ECEHRNHTCT
SLQTCYNLQG GFKCIDPISC EEPYLLIGEN RCMCPAEHTS CRDQPFTILY RDMDVVSGRS
VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPRDIQLDL
EMITVNTVIN FRGSSVIRLR IYVSQYPF
