FBLN5_RAT
ID FBLN5_RAT Reviewed; 448 AA.
AC Q9WVH8; Q9R284;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Fibulin-5;
DE Short=FIBL-5;
DE AltName: Full=Developmental arteries and neural crest EGF-like protein;
DE Short=Dance;
DE AltName: Full=Embryonic vascular EGF repeat-containing protein;
DE Short=EVEC;
DE Flags: Precursor;
GN Name=Fbln5; Synonyms=Dance;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
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 [MRNA].
RX PubMed=10347091; DOI=10.1161/01.res.84.10.1166;
RA Kowal R.C., Richardson J.A., Miano J.M., Olson E.N.;
RT "EVEC, a novel epidermal growth factor-like repeat-containing protein
RT upregulated in embryonic and diseased adult vasculature.";
RL Circ. Res. 84:1166-1176(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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. Stabilizes and organizes elastic
CC fibers in the skin, lung and vasculature. Promotes adhesion of
CC endothelial cells through interaction of integrins and the RGD motif.
CC Vascular ligand for integrin receptors which may play a role in
CC vascular development and remodeling. May act as an adapter that
CC mediates the interaction between FBN1 and ELN.
CC {ECO:0000250|UniProtKB:Q9UBX5, ECO:0000250|UniProtKB:Q9WVH9}.
CC -!- SUBUNIT: Homodimer. Monomer, homodimerizes in presence of Ca(2+).
CC Interacts with ELN. Interacts (via N-terminus) with the integrins
CC ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1. Interacts with FBN1 (via N-
CC terminal domain). Forms a ternary complex with ELN and FBN1. Interacts
CC with EFEMP2 with moderate affinity (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBX5, ECO:0000250|UniProtKB:Q9WVH9}.
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 -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AF112153; AAD41769.1; -; mRNA.
DR EMBL; AF137350; AAD25101.1; -; mRNA.
DR EMBL; BC078845; AAH78845.1; -; mRNA.
DR RefSeq; NP_062026.2; NM_019153.3.
DR AlphaFoldDB; Q9WVH8; -.
DR BioGRID; 247841; 3.
DR IntAct; Q9WVH8; 1.
DR STRING; 10116.ENSRNOP00000007004; -.
DR GlyGen; Q9WVH8; 2 sites.
DR PaxDb; Q9WVH8; -.
DR PRIDE; Q9WVH8; -.
DR GeneID; 29158; -.
DR KEGG; rno:29158; -.
DR UCSC; RGD:2594; rat.
DR CTD; 10516; -.
DR RGD; 2594; Fbln5.
DR VEuPathDB; HostDB:ENSRNOG00000050539; -.
DR eggNOG; KOG1217; Eukaryota.
DR HOGENOM; CLU_004826_0_1_1; -.
DR InParanoid; Q9WVH8; -.
DR OMA; ACRGDMV; -.
DR OrthoDB; 1174178at2759; -.
DR Reactome; R-RNO-1566948; Elastic fibre formation.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR PRO; PR:Q9WVH8; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000050539; Expressed in spleen and 18 other tissues.
DR Genevisible; Q9WVH8; RN.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0098867; P:intramembranous bone growth; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; IEP:RGD.
DR GO; GO:2000121; P:regulation of removal of superoxide radicals; ISO:RGD.
DR GO; GO:0046903; P:secretion; ISO:RGD.
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 2: Evidence at transcript 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_0000007579"
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"
FT CONFLICT 238
FT /note="L -> P (in Ref. 2; AAD25101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 50160 MW; E6BC68F7BF14B714 CRC64;
MPGLKRILTV TILALWLPHP GNAQQQCTNG FDLDRQTGQC LDIDECRTIP EACRGDMMCV
NQNGGYLCIP RTNPVYRGPY SNPYSTSYSG PYPAAAPPVP ASNYPTISRP LVCRFGYQMD
EGNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL
CANVPGSYSC TCNPGFTLND DGRSCQDVNE CETENPCVQT CVNTYGSFIC RCDPGYELEE
DGIHCSDMDE CSFSEFLCQH ECVNQPGSYF CSCPPGYVLL EDNRSCQDIN ECEHRNHTCT
PLQTCYNLQG GFKCIDPIVC EEPYLLIGDN RCMCPAENTG CRDQPFTILF RDMDVVSGRS
VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPRDIQLDL
EMITVNTVIN FRGSSVIRLR IYVSQYPF
