ID A0A452F2R0_CAPHI Unreviewed; 713 AA.
AC A0A452F2R0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Fibulin-1 {ECO:0000256|ARBA:ARBA00021554, ECO:0000256|PIRNR:PIRNR036313};
GN Name=FBLN1 {ECO:0000313|Ensembl:ENSCHIP00000018671.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000018671.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000018671.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000018671.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components. {ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SIMILARITY: Belongs to the fibulin family.
CC {ECO:0000256|ARBA:ARBA00006127, ECO:0000256|PIRNR:PIRNR036313}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; LWLT01000005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452F2R0; -.
DR STRING; 9925.ENSCHIP00000018671; -.
DR Ensembl; ENSCHIT00000026486.1; ENSCHIP00000018671.1; ENSCHIG00000017977.1.
DR GeneTree; ENSGT00940000156642; -.
DR Proteomes; UP000291000; Chromosome 5.
DR Bgee; ENSCHIG00000017977; Expressed in uterus and 17 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0071953; C:elastic fiber; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR CDD; cd00017; ANATO; 2.
DR CDD; cd00054; EGF_CA; 5.
DR Gene3D; 2.10.25.10; Laminin; 9.
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 PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF07645; EGF_CA; 4.
DR PIRSF; PIRSF036313; Fibulin-1; 1.
DR SMART; SM00104; ANATO; 3.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW ECO:0000256|PIRNR:PIRNR036313};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036313}.
FT DOMAIN 43..76
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 84..117
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 119..151
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 366..408
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 451..490
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 491..534
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
SQ SEQUENCE 713 AA; 78503 MW; 9BDBA2B2AA4EF1F2 CRC64;
PSPRVPSPWV PSPWVFTFHS PGKPSLVVPV RGTPGADVSM EACCADGHRM ATEHRACSLP
YASESKECRM VQEQCCHNQL EELHCATGIN LANEQDSCTA PRGDNTSLEA MFVKRCCHCC
LLGRAAQAQG QSCEYSLMVG YQCGLVFRAC CVKGQETAEF APGDGGDLQE TAKVSEIEEE
QEDPYLNDRC RGGGPCKQQC RDTGEEVVCS CFVGYQLLPD GVSCEDVNEC IRGSQNCRLG
ETCINTVGSF RCQRDSSCGT GYELTEDNDC KDIDECESGI HNCLPDFICQ NTLGSFRCRP
KLQCKSGFIQ DALGNCIDIN ECLSISAPCP VGQTCINTEG SYTCQKNVPN CGRGYHLNEE
GTRCVDVDEC SPPSEPCGPG HLCVNSPGSF RCECKAGYYF DGISRTCVDI NECRRYPGRL
CGHKCENTPG SYYCSCTIGF RLSSDGRSCE DVNECNSSPC SQECANVYGS YQCYCRRGYQ
LSDVDGVTCE DIDECALPTG GHICSYRCIN IPGSFQCSCP STGYRLAPNG RNCQDIDECV
TGIHNCSINE TCFNIQGGFR CLAFECPENY RRSTDTLRQE KTDTVRCIKS CRPNDVACVL
DPVHTVSHTV VSLPTFREFT RPEEIIFLRA ITPAYPANHA DIIFDITDGN LRDSFDIIKR
YMDGMTVGVV RQVRPIVGPF HAVLKLEMNY VVGGVVSHRN VVNVHIFVSE YWF
//
