FBLN5_PONAB
ID FBLN5_PONAB Reviewed; 448 AA.
AC Q5RC26;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Fibulin-5;
DE Short=FIBL-5;
DE Flags: Precursor;
GN Name=FBLN5;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858456; CAH90684.1; -; mRNA.
DR RefSeq; NP_001125375.1; NM_001131903.1.
DR AlphaFoldDB; Q5RC26; -.
DR STRING; 9601.ENSPPYP00000006903; -.
DR GeneID; 100172278; -.
DR KEGG; pon:100172278; -.
DR CTD; 10516; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q5RC26; -.
DR OrthoDB; 1174178at2759; -.
DR Proteomes; UP000001595; 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_0000317126"
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; 50280 MW; 5805D418AB8980B1 CRC64;
MPGIKRILTV TILALCLPSP GNAQAQCTNG FDLDRQSGQC LDIDECRTIP EACRGDMMCV
NQNGRYLCIP RTNPVYRGPY SNPYSTPYSG PYPAAAPPLS APNYPTISRP LICRFGYQMD
ESNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL
CANVPGSYSC TCNPGFTLNE DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELEE
DGVHCSDMDE CSFSEFLCQH ECVNQPGTYF CSCPPGYILL DDNRSCQDIN ECEHRNHTCN
LQQTCYNLQG GFKCIDPIRC EEPYLRISDN RCMCPAENPG CRDQPFTILY RDMDVVSGRS
VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPREIQLDL
EMITVNTVIN FRGSSVIRLR IYVSQYPF
