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Database: UniProt
Entry: Q5EA62
LinkDB: Q5EA62
Original site: Q5EA62 
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   16-JAN-2019, entry version 87.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
CC       the assembly of continuous elastin (ELN) polymer and promotes the
CC       interaction of microfibrils and ELN. Stabilizes and organizes
CC       elastic fibers in the skin, lung and vasculature. Promotes
CC       adhesion of endothelial cells through interaction of integrins and
CC       the RGD motif. Vascular ligand for integrin receptors which may
CC       play a role in vascular development and remodeling. May act as an
CC       adapter that 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
CC       N-terminal domain). Forms a ternary complex with ELN and FBN1.
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
CC       elastic fibers. {ECO:0000250|UniProtKB:Q9UBX5}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UBX5}.
CC   -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
DR   EMBL; BT020707; AAX08724.1; -; mRNA.
DR   RefSeq; NP_001014946.1; NM_001014946.1.
DR   UniGene; Bt.44183; -.
DR   ProteinModelPortal; Q5EA62; -.
DR   SMR; Q5EA62; -.
DR   IntAct; Q5EA62; 2.
DR   STRING; 9913.ENSBTAP00000024122; -.
DR   PaxDb; Q5EA62; -.
DR   PeptideAtlas; Q5EA62; -.
DR   PRIDE; Q5EA62; -.
DR   GeneID; 535185; -.
DR   KEGG; bta:535185; -.
DR   CTD; 10516; -.
DR   eggNOG; ENOG410IR76; Eukaryota.
DR   eggNOG; ENOG41104WD; LUCA.
DR   HOGENOM; HOG000234337; -.
DR   HOVERGEN; HBG051560; -.
DR   InParanoid; Q5EA62; -.
DR   KO; K17340; -.
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; IPR013032; EGF-like_CS.
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; IPR037287; Fibulin_3/4/5.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   PANTHER; PTHR44074; PTHR44074; 1.
DR   PANTHER; PTHR44074:SF4; PTHR44074:SF4; 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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    448       Fibulin-5.
FT                                /FTId=PRO_0000236272.
FT   DOMAIN       42     82       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      127    167       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      168    206       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      207    246       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      247    287       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      288    333       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MOTIF        54     56       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    283    283       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     46     59       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     53     68       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    131    144       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    138    153       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    155    166       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    172    181       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    177    190       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    192    205       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    211    221       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    217    230       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    232    245       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    251    262       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    258    271       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    273    286       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    292    305       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    299    314       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    320    332       {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
//
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