FBLN1_CAEEL
ID FBLN1_CAEEL Reviewed; 728 AA.
AC O77469; O18026; O77474; Q20903; Q50JF9; Q5I5Q9; Q95NZ3; Q9TZS1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Fibulin-1;
DE Flags: Precursor;
GN Name=fbl-1; Synonyms=fbln1; ORFNames=F56H11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B).
RC STRAIN=CB1489;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-288 AND HIS-290.
RX PubMed=15556863; DOI=10.1016/j.cub.2004.10.047;
RA Kubota Y., Kuroki R., Nishiwaki K.;
RT "A fibulin-1 homolog interacts with an ADAM protease that controls cell
RT migration in C. elegans.";
RL Curr. Biol. 14:2011-2018(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16120639; DOI=10.1242/dev.02007;
RA Muriel J.M., Dong C., Hutter H., Vogel B.E.;
RT "Fibulin-1C and Fibulin-1D splice variants have distinct functions and
RT assemble in a hemicentin-dependent manner.";
RL Development 132:4223-4234(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15556862; DOI=10.1016/j.cub.2004.11.006;
RA Hesselson D., Newman C., Kim K.W., Kimble J.;
RT "GON-1 and fibulin have antagonistic roles in control of organ shape.";
RL Curr. Biol. 14:2005-2010(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17043142; DOI=10.1083/jcb.200608061;
RA Hesselson D., Kimble J.;
RT "Growth control by EGF repeats of the C. elegans Fibulin-1C isoform.";
RL J. Cell Biol. 175:217-223(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-288 AND HIS-290.
RX PubMed=19104038; DOI=10.1073/pnas.0804055106;
RA Kubota Y., Ohkura K., Tamai K.K., Nagata K., Nishiwaki K.;
RT "MIG-17/ADAMTS controls cell migration by recruiting nidogen to the
RT basement membrane in C. elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20804-20809(2008).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22298704; DOI=10.1534/genetics.111.133173;
RA Kubota Y., Nagata K., Sugimoto A., Nishiwaki K.;
RT "Tissue architecture in the Caenorhabditis elegans gonad depends on
RT interactions among fibulin-1, type IV collagen and the ADAMTS extracellular
RT protease.";
RL Genetics 190:1379-1388(2012).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-624, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers. Plays
CC a role in cell adhesion and migration along protein fibers within the
CC extracellular matrix (ECM). Important for certain developmental
CC processes and contributes to the supramolecular organization of ECM
CC architecture, in particular to those of basement membranes.
CC {ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:15556863,
CC ECO:0000269|PubMed:16120639, ECO:0000269|PubMed:17043142,
CC ECO:0000269|PubMed:19104038, ECO:0000269|PubMed:22298704}.
CC -!- FUNCTION: [Isoform a]: Involved in regulating the shape and adhesion of
CC cells in the developing pharynx, intestine, body-wall muscle and
CC gonadal tissue (PubMed:16120639). During gonadogenesis, regulates the
CC width of gonads and the migration of distal tip cells (DTC)
CC (PubMed:15556862, PubMed:17043142, PubMed:22298704). Together with type
CC IV collagen let-2 and downstream of metalloprotease mig-17, recruits
CC nidogen nid-1 to the gonad basement membrane thereby inducing basement
CC membrane remodeling required for the directional migration of DTCs
CC (PubMed:15556863, PubMed:19104038). Acts antagonistically with
CC metalloprotease gon-1 to maintain optimal levels of type IV collagen
CC emb-9 in the gonad basement membrane during gonadogenesis
CC (PubMed:15556862, PubMed:17043142, PubMed:22298704). Required for
CC larval development (PubMed:17043142). {ECO:0000269|PubMed:15556862,
CC ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:16120639,
CC ECO:0000269|PubMed:17043142, ECO:0000269|PubMed:19104038}.
CC -!- FUNCTION: [Isoform c]: Involved in the assembly of the flexible
CC hemicentin-containing tracks found joining the pharynx and body-wall-
CC muscle basement membranes. {ECO:0000269|PubMed:16120639}.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Secreted, extracellular space,
CC extracellular matrix, basement membrane {ECO:0000269|PubMed:15556862,
CC ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:17043142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c; Synonyms=Fibulin-1D;
CC IsoId=O77469-1; Sequence=Displayed;
CC Name=a; Synonyms=C, Fibulin-1C;
CC IsoId=O77469-2; Sequence=VSP_001388, VSP_001390;
CC Name=b; Synonyms=D;
CC IsoId=O77469-3; Sequence=VSP_001388;
CC -!- TISSUE SPECIFICITY: Expressed in head muscle cells, anterior and
CC posterior intestinal cells (PubMed:15556862). Isoform a: Expressed in
CC male and hermaphrodite gonad, anterior and posterior intestine and
CC pharyngeal basement membranes, body-wall muscle, GLR cells, uterine
CC attachment and mechanosensory neurons (PubMed:15556863,
CC PubMed:16120639, PubMed:17043142). Isoform c: Expressed on ALM/PLM
CC mechanosensory neuron attachments, in flexible tracks connecting the
CC pharyngeal, body-wall-muscle basement membranes and in uterine
CC attachments (PubMed:16120639). {ECO:0000269|PubMed:15556862,
CC ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:16120639,
CC ECO:0000269|PubMed:17043142}.
CC -!- DEVELOPMENTAL STAGE: Expressed from late embryonic stage onwards.
CC {ECO:0000269|PubMed:16120639}.
CC -!- DISRUPTION PHENOTYPE: Gonads have short and swollen arms. Pharyngeal
CC defects. Movement is lethargic. {ECO:0000269|PubMed:16120639,
CC ECO:0000269|PubMed:17043142, ECO:0000269|PubMed:22298704}.
CC -!- MISCELLANEOUS: Although involved in the same pathway as gon-1 and mig-
CC 17, it is probably not cleaved by these metalloproteases.
CC {ECO:0000305|PubMed:15556862}.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AB212860; BAD98165.1; -; mRNA.
DR EMBL; AY851363; AAW34127.1; -; mRNA.
DR EMBL; AF051401; AAC28321.1; -; mRNA.
DR EMBL; AF051402; AAC28322.1; -; mRNA.
DR EMBL; AF051403; AAC28323.1; -; Genomic_DNA.
DR EMBL; AF051403; AAC28324.1; -; Genomic_DNA.
DR EMBL; AF070477; AAC24035.1; -; Genomic_DNA.
DR EMBL; Z68749; CAA92962.2; -; Genomic_DNA.
DR EMBL; Z68219; CAA92962.2; JOINED; Genomic_DNA.
DR EMBL; Z68749; CAC35817.1; -; Genomic_DNA.
DR EMBL; Z68219; CAC35817.1; JOINED; Genomic_DNA.
DR EMBL; Z68749; CAC35818.1; -; Genomic_DNA.
DR EMBL; Z68219; CAC35818.1; JOINED; Genomic_DNA.
DR PIR; T22793; T22793.
DR PIR; T42760; T42760.
DR PIR; T42990; T42990.
DR PIR; T43210; T43210.
DR RefSeq; NP_001023236.1; NM_001028065.2. [O77469-2]
DR RefSeq; NP_001023237.1; NM_001028066.4. [O77469-3]
DR RefSeq; NP_501694.2; NM_069293.4. [O77469-1]
DR AlphaFoldDB; O77469; -.
DR BioGRID; 42893; 7.
DR DIP; DIP-26629N; -.
DR IntAct; O77469; 7.
DR MINT; O77469; -.
DR STRING; 6239.F56H11.1c; -.
DR iPTMnet; O77469; -.
DR EPD; O77469; -.
DR PaxDb; O77469; -.
DR PeptideAtlas; O77469; -.
DR EnsemblMetazoa; F56H11.1a.1; F56H11.1a.1; WBGene00001403. [O77469-2]
DR EnsemblMetazoa; F56H11.1b.1; F56H11.1b.1; WBGene00001403. [O77469-3]
DR EnsemblMetazoa; F56H11.1c.1; F56H11.1c.1; WBGene00001403. [O77469-1]
DR GeneID; 177788; -.
DR KEGG; cel:CELE_F56H11.1; -.
DR UCSC; F56H11.1a.1; c. elegans. [O77469-1]
DR CTD; 177788; -.
DR WormBase; F56H11.1a; CE26701; WBGene00001403; fbl-1. [O77469-2]
DR WormBase; F56H11.1b; CE26702; WBGene00001403; fbl-1. [O77469-3]
DR WormBase; F56H11.1c; CE38374; WBGene00001403; fbl-1. [O77469-1]
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156642; -.
DR InParanoid; O77469; -.
DR OMA; LRITHYH; -.
DR PhylomeDB; O77469; -.
DR Reactome; R-CEL-2129379; Molecules associated with elastic fibres.
DR PRO; PR:O77469; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001403; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O77469; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:WormBase.
DR GO; GO:0016504; F:peptidase activator activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
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; 1.
DR Pfam; PF07645; EGF_CA; 6.
DR PIRSF; PIRSF036313; Fibulin-1; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Developmental protein;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..728
FT /note="Fibulin-1"
FT /id="PRO_0000007567"
FT DOMAIN 23..64
FT /note="Anaphylatoxin-like 1"
FT DOMAIN 65..96
FT /note="Anaphylatoxin-like 2"
FT DOMAIN 97..129
FT /note="Anaphylatoxin-like 3"
FT DOMAIN 155..194
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 195..280
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 281..344
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 343..389
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 390..429
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 430..473
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 474..514
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 515..559
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 560..610
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 23..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 24..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 37..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 66..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 79..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 97..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 98..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 111..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 159..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 164..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 180..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 285..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 292..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 347..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 353..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 375..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 394..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 399..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 415..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 434..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 442..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 459..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 478..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 485..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 500..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 519..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 530..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 545..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 564..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 569..585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 196..280
FT /note="RNECLTRQSPCTQSEDCVNTIGGYICQRRISRLVPHRHRANRIGNAPRRMRD
FT DPYSRAGEYREASQANTEFGCPMGWLFQHGHCV -> IDECATLMDDCLESQRCLNTPG
FT SFKCIRTLSCGTGYAMDSETERCR (in isoform a and isoform b)"
FT /evidence="ECO:0000303|PubMed:15556863,
FT ECO:0000303|PubMed:16120639, ECO:0000303|PubMed:9923656"
FT /id="VSP_001388"
FT VAR_SEQ 603..728
FT /note="QIADGYSCIKVCSTEDTECLGNHTREVLYQFRAVPSLKTIISPIEVSRIVTH
FT MGVPFSVDYNLDYVGQRHFRIVQERNIGIVQLVKPISGPTVETIKVNIHTKSRTGVILA
FT FNEAIIEISVSKYPF -> RCNRQPSACGLPEECSKVPLFLTYQFISLARAVPISSHRP
FT AITLFKVSAPNHADTEVNFELQLKTTIVGAPNVLPAIRANFLLQKGEKRNSAVVTLRDS
FT LDGPQTVKLQLLLRMSKKGKNFNTYAANLIVDVAAHKRHNTVHPPLMKIR (in
FT isoform a)"
FT /evidence="ECO:0000303|PubMed:15556863,
FT ECO:0000303|PubMed:16120639, ECO:0000303|PubMed:9923656"
FT /id="VSP_001390"
FT MUTAGEN 288
FT /note="G->E: In k201/tk51; slight defect in posterior DTC
FT migration. In a let-2 (k196) mutant background, partially
FT prevents anterior DTC migration. Restores normal DTC
FT migration and nid-1 basement membrane localization in a
FT mig-17 (k174) mutant background but not in a mig-17 (k174)
FT and nid-1 (cg119) mutant background. Restores nid-1
FT basement membrane localization in a mig-17 (k174) mutant
FT background."
FT /evidence="ECO:0000269|PubMed:15556863,
FT ECO:0000269|PubMed:19104038"
FT MUTAGEN 290
FT /note="H->Y: In k206; No defect in DTC migration. In a let-
FT 2 (k196) mutant background, partially prevents anterior DTC
FT migration. Restores normal DTC migration and nid-1 basement
FT membrane localization in a mig-17 (k174) mutant background
FT but not in a mig-17 (k174) and nid-1 (cg119) mutant
FT background."
FT /evidence="ECO:0000269|PubMed:15556863,
FT ECO:0000269|PubMed:19104038"
FT CONFLICT 195
FT /note="D -> DH (in Ref. 1; AAC24035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 79321 MW; DBD2484CC6FD53A9 CRC64;
MRICFLLLAF LVAETFANEL TRCCAGGTRH FKNSNTCSSI KSEGTSMTCQ RAASICCLRS
LLDNACDSGT DIAKEEESCP SNINILGGGL KKECCDCCLL AKDLLNRNEP CVAPVGFSAG
CLRSFNKCCN GDIEITHASE IITGRPLNDP HVLHLGDRCA SSHCEHLCHD RGGEKVECSC
RSGFDLAPDG MACVDRNECL TRQSPCTQSE DCVNTIGGYI CQRRISRLVP HRHRANRIGN
APRRMRDDPY SRAGEYREAS QANTEFGCPM GWLFQHGHCV DVDECNLGSH DCGPLYQCRN
TQGSYRCDAK KCGDGELQNP MTGECTSITC PNGYYPKNGM CNDIDECVTG HNCGAGEECV
NTPGSFRCQQ KGNLCAHGYE VNGATGFCED VNECQQGVCG SMECINLPGT YKCKCGPGYE
FNDAKKRCED VDECIKFAGH VCDLSAECIN TIGSFECKCK PGFQLASDGR RCEDVNECTT
GIAACEQKCV NIPGSYQCIC DRGFALGPDG TKCEDIDECS IWAGSGNDLC MGGCINTKGS
YLCQCPPGYK IQPDGRTCVD VDECAMGECA GSDKVCVNTL GSFKCHSIDC PTNYIHDSLN
KNQIADGYSC IKVCSTEDTE CLGNHTREVL YQFRAVPSLK TIISPIEVSR IVTHMGVPFS
VDYNLDYVGQ RHFRIVQERN IGIVQLVKPI SGPTVETIKV NIHTKSRTGV ILAFNEAIIE
ISVSKYPF
