FBLN5_BOVIN
ID FBLN5_BOVIN Reviewed; 448 AA.
AC Q5EA62;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Fibulin-5;
DE Short=FIBL-5;
DE Flags: Precursor;
GN Name=FBLN5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; BT020707; AAX08724.1; -; mRNA.
DR RefSeq; NP_001014946.1; NM_001014946.1.
DR AlphaFoldDB; Q5EA62; -.
DR IntAct; Q5EA62; 2.
DR STRING; 9913.ENSBTAP00000024122; -.
DR PaxDb; Q5EA62; -.
DR PeptideAtlas; Q5EA62; -.
DR GeneID; 535185; -.
DR KEGG; bta:535185; -.
DR CTD; 10516; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q5EA62; -.
DR OrthoDB; 1174178at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
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 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; 3.
DR Pfam; PF07645; EGF_CA; 2.
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; 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_0000236272"
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; 50164 MW; A8C61DA1121A47FB CRC64;
MPGFKRILTV TVLALCLPTP GNAQQQCTNG FDLDRSSGQC LDVDECRTIP EACRGDMMCV
NQNGGYLCIP RTNPVYRGPY SNPYSNPYSA SYPAAAPPLS APNYPTISRP LICRFGYQMD
ESNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL
CANVPGSYSC TCNPGFTLNE DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELED
DGVHCSDMDE CSFSEFLCQH ECVNQPGTYF CSCPAGYILL DDNRSCQDIN ECEHRNHTCI
LQQTCYNLQG GFKCIDPIRC EEPYLRISDN RCMCPAENPG CRDQPFTILY RDMDVVSGRS
VPADIFQMQA TTRYPGAYYI FQIKSGNDGR EFYMRQTGPI SATLVMTRPI KGPRDIQLDL
EMITVNTVIN FRGSSVIRLR IYVSQYPF
