FBLN1_CHLAE
ID FBLN1_CHLAE Reviewed; 598 AA.
AC Q8MJJ9;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Fibulin-1;
DE Short=FIBL-1;
DE Flags: Fragment;
GN Name=FBLN1;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH DTR.
RX PubMed=11846885; DOI=10.1186/1471-2121-3-2;
RA Brooke J.S., Cha J.-H., Eidels L.;
RT "Latent transforming growth factor beta-binding protein-3 and fibulin-1C
RT interact with the extracellular domain of the heparin-binding EGF-like
RT growth factor precursor.";
RL BMC Cell Biol. 3:2-2(2002).
CC -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers. May
CC play a role in cell adhesion and migration along protein fibers within
CC the extracellular matrix (ECM). Could be important for certain
CC developmental processes and contribute to the supramolecular
CC organization of ECM architecture, in particular to those of basement
CC membranes. May serve to anchor the mature/soluble form of DTR to its
CC fibers as it migrates through the extracellular matrix. The direct
CC physical association with DTR may be useful in such tissue
CC developmental processes as wound healing.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components. Interacts with FBLN7 (By similarity). Interacts with
CC the mature/soluble form of DTR. Interacts with CCN3 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P23142,
CC ECO:0000269|PubMed:11846885}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AF395659; AAM90567.1; -; mRNA.
DR AlphaFoldDB; Q8MJJ9; -.
DR PRIDE; Q8MJJ9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00017; ANATO; 1.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
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; IPR017048; Fibulin-1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF07645; EGF_CA; 4.
DR PIRSF; PIRSF036313; Fibulin-1; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 7.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Repeat; Secreted.
FT CHAIN <1..598
FT /note="Fibulin-1"
FT /id="PRO_0000007562"
FT DOMAIN <1..27
FT /note="Anaphylatoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 28..60
FT /note="Anaphylatoxin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 92..131
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 132..177
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 178..223
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 224..270
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 271..313
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 314..355
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 356..395
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 396..439
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 440..484
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 271..355
FT /note="Self-association and FN1-binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID <1..25
FT /evidence="ECO:0000250"
FT DISULFID 7..26
FT /evidence="ECO:0000250"
FT DISULFID 28..52
FT /evidence="ECO:0000250"
FT DISULFID 29..59
FT /evidence="ECO:0000250"
FT DISULFID 42..60
FT /evidence="ECO:0000250"
FT DISULFID 96..106
FT /evidence="ECO:0000250"
FT DISULFID 102..115
FT /evidence="ECO:0000250"
FT DISULFID 117..130
FT /evidence="ECO:0000250"
FT DISULFID 136..149
FT /evidence="ECO:0000250"
FT DISULFID 143..158
FT /evidence="ECO:0000250"
FT DISULFID 164..176
FT /evidence="ECO:0000250"
FT DISULFID 182..195
FT /evidence="ECO:0000250"
FT DISULFID 189..204
FT /evidence="ECO:0000250"
FT DISULFID 210..222
FT /evidence="ECO:0000250"
FT DISULFID 228..242
FT /evidence="ECO:0000250"
FT DISULFID 257..270
FT /evidence="ECO:0000250"
FT DISULFID 275..288
FT /evidence="ECO:0000250"
FT DISULFID 282..297
FT /evidence="ECO:0000250"
FT DISULFID 299..312
FT /evidence="ECO:0000250"
FT DISULFID 318..330
FT /evidence="ECO:0000250"
FT DISULFID 326..339
FT /evidence="ECO:0000250"
FT DISULFID 341..354
FT /evidence="ECO:0000250"
FT DISULFID 360..369
FT /evidence="ECO:0000250"
FT DISULFID 365..378
FT /evidence="ECO:0000250"
FT DISULFID 380..394
FT /evidence="ECO:0000250"
FT DISULFID 400..413
FT /evidence="ECO:0000250"
FT DISULFID 409..422
FT /evidence="ECO:0000250"
FT DISULFID 424..438
FT /evidence="ECO:0000250"
FT DISULFID 444..457
FT /evidence="ECO:0000250"
FT DISULFID 451..466
FT /evidence="ECO:0000250"
FT DISULFID 471..483
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 598 AA; 65517 MW; 849BF018DF452B02 CRC64;
ANEQDHCAAP RGDNASLEAT FVKRCCHCCL LGRAAQAQGQ SCEYNLMVGY QCGQVFRACC
VKSQETGDLD VRSLQETDKI TEVEEEQEDP YLNDRCRGGG PCKQQCRDTG DEVVCSCFVG
YQLLSDGVSC EDVNECITGS HSCRLGESCI NTVGSFRCQR DSSCGTGYEL TEDNSCKDID
QCESGIHNCL PDFICQNTLG SFRCRPKLQC KNGFIQDALA NCIDINECLS IVSAPCPTGH
TCINTEGSYT QKNVPNCGRG YHLNEEGTRC DVNECAPPAE PCGKGHRCVN SPGSFRCECK
TGYYFDGISR MCVDVNECQR YPGRLCGHKC ENTLGSYVCS CSVGFRLSVD GRSCEDINEC
SSSPCSQECA NVYGSYQCYC RRGYQLSDVD GVTCEDIDEC ALPTGGHICS YRCINIPGSF
QCSCPASGYR LAPNGRNCQD IDECVTGIHN CSINETCFNI QGGFRCLAFE CPENYRRSAA
TRCERLPCHE NRECSKLPLR ITYYHLSFPT NIQAPAVVFR MGPSSAVPGD SMQLAITGGN
EEGFFTTRKV SPHSGVVALT KPVPEPRDLL LTVKMDLYRH GTVSSFVAKL FIFVSAEL
