FBLN1_CHICK
ID FBLN1_CHICK Reviewed; 704 AA.
AC O73775; O73774;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Fibulin-1;
DE Short=FIBL-1;
DE Flags: Precursor;
GN Name=FBLN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D).
RC TISSUE=Embryo;
RX PubMed=9923656; DOI=10.1016/s0945-053x(98)90114-7;
RA Barth J.L., Argraves K.M., Roark E.F., Little C.D., Argraves W.S.;
RT "Identification of chicken and C. elegans fibulin-1 homologs and
RT characterization of the C. elegans fibulin-1 gene.";
RL Matrix Biol. 17:635-646(1998).
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.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D;
CC IsoId=O73775-2; Sequence=Displayed;
CC Name=C;
CC IsoId=O73775-1; Sequence=VSP_007378;
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AF051399; AAC05387.1; -; mRNA.
DR EMBL; AF051400; AAC05388.1; -; mRNA.
DR RefSeq; NP_989496.1; NM_204165.1. [O73775-2]
DR AlphaFoldDB; O73775; -.
DR STRING; 9031.ENSGALP00000022972; -.
DR PaxDb; O73775; -.
DR PRIDE; O73775; -.
DR GeneID; 373979; -.
DR KEGG; gga:373979; -.
DR CTD; 2192; -.
DR VEuPathDB; HostDB:geneid_373979; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; O73775; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; O73775; -.
DR PRO; PR:O73775; -.
DR Proteomes; UP000000539; Unplaced.
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; PF01821; ANATO; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 6.
DR PIRSF; PIRSF036313; Fibulin-1; 1.
DR SMART; SM00104; ANATO; 3.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 9.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 8.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..704
FT /note="Fibulin-1"
FT /id="PRO_0000007565"
FT DOMAIN 33..74
FT /note="Anaphylatoxin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 75..109
FT /note="Anaphylatoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 110..142
FT /note="Anaphylatoxin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 177..216
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..262
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 263..308
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 309..356
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 357..399
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 400..441
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 442..481
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 482..525
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 526..579
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 357..441
FT /note="Self-association and FN1-binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..59
FT /evidence="ECO:0000250"
FT DISULFID 34..66
FT /evidence="ECO:0000250"
FT DISULFID 47..67
FT /evidence="ECO:0000250"
FT DISULFID 76..107
FT /evidence="ECO:0000250"
FT DISULFID 89..108
FT /evidence="ECO:0000250"
FT DISULFID 110..134
FT /evidence="ECO:0000250"
FT DISULFID 111..141
FT /evidence="ECO:0000250"
FT DISULFID 124..142
FT /evidence="ECO:0000250"
FT DISULFID 181..191
FT /evidence="ECO:0000250"
FT DISULFID 187..200
FT /evidence="ECO:0000250"
FT DISULFID 202..215
FT /evidence="ECO:0000250"
FT DISULFID 221..234
FT /evidence="ECO:0000250"
FT DISULFID 228..243
FT /evidence="ECO:0000250"
FT DISULFID 249..261
FT /evidence="ECO:0000250"
FT DISULFID 267..280
FT /evidence="ECO:0000250"
FT DISULFID 274..289
FT /evidence="ECO:0000250"
FT DISULFID 295..307
FT /evidence="ECO:0000250"
FT DISULFID 313..326
FT /evidence="ECO:0000250"
FT DISULFID 320..335
FT /evidence="ECO:0000250"
FT DISULFID 342..355
FT /evidence="ECO:0000250"
FT DISULFID 361..374
FT /evidence="ECO:0000250"
FT DISULFID 368..383
FT /evidence="ECO:0000250"
FT DISULFID 385..398
FT /evidence="ECO:0000250"
FT DISULFID 404..416
FT /evidence="ECO:0000250"
FT DISULFID 412..425
FT /evidence="ECO:0000250"
FT DISULFID 427..440
FT /evidence="ECO:0000250"
FT DISULFID 446..455
FT /evidence="ECO:0000250"
FT DISULFID 451..464
FT /evidence="ECO:0000250"
FT DISULFID 466..480
FT /evidence="ECO:0000250"
FT DISULFID 486..499
FT /evidence="ECO:0000250"
FT DISULFID 495..508
FT /evidence="ECO:0000250"
FT DISULFID 510..524
FT /evidence="ECO:0000250"
FT DISULFID 530..543
FT /evidence="ECO:0000250"
FT DISULFID 537..552
FT /evidence="ECO:0000250"
FT DISULFID 557..578
FT /evidence="ECO:0000250"
FT VAR_SEQ 568..704
FT /note="VRLEKTDTIRCIKSCRPNDVNCVLDPVHTISHTVISLPTFREFTRPEEIIFL
FT RAITPTYPANQADIIFDITEGNLRESFDIIKRYMDGMTVGVVRQVRPIVGPFHAILKLE
FT MNYVMGGVVSHRNIVNVHIFVSEYWF -> RCERLPCNENKECQSLPLRITYYHLSFPT
FT NIQVPTDIFRMGPSNAVPGDKILLSIISGNQEGFFTTKKVNNHSGIVVMQRQITEPRDL
FT LLTIQMQLTRHGTVNTFIAKLFVFVSAQL (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9923656"
FT /id="VSP_007378"
SQ SEQUENCE 704 AA; 78138 MW; D47D5A30D5E42932 CRC64;
MDKLRGARPL RLLLLLLALL PALRGQDLSM EECCDKGVEW ANKNRICTSL PLISESRECS
MTQVQCCRSK LEEHYCSDGI EFASVHEECD SHNGENSTCE AEYFKKCCYC CLLGKTAQVQ
GQSCEPNLKI GYQCGIVFRA CCVKGQEGTD VSISDDAPKK EQVEISKEEL DQEDPYLHDG
CRGGGPCSQQ CRDTGSSYVC SCFVGYQLQP DGVNCEDINE CITGTHSCGI GQTCVNTLGS
FRCQRDTSCG TGYELTDDSR CKDIDECETG THNCPPDFIC QNTPGSFRCR PKLQCMNGFI
QDALGNCIDI NECLSTNMPC PAGQICINTD GSYTCQRISP SCGRGYHLNE DGTRCVDVDE
CSSSDQPCGE GHVCINGPGN YRCECKSGYS FDVISRTCID INECRRYPGR LCAHKCENTP
GSYYCTCTMG FKLSSDGRSC EDLNECESSP CSQECANVYG SYQCYCRRGF QLSDIDGISC
EDIDECALPT GGHICSFRCI NIPGSFQCTC PSTGYRLAPN ARNCQDIDEC VAETHNCSFN
ETCFNIQGGF RCLSLECPEN YRKSGDTVRL EKTDTIRCIK SCRPNDVNCV LDPVHTISHT
VISLPTFREF TRPEEIIFLR AITPTYPANQ ADIIFDITEG NLRESFDIIK RYMDGMTVGV
VRQVRPIVGP FHAILKLEMN YVMGGVVSHR NIVNVHIFVS EYWF
