FBLN1_DANRE
ID FBLN1_DANRE Reviewed; 681 AA.
AC O42182; O42183;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Fibulin-1;
DE Short=FIBL-1;
DE Flags: Precursor;
GN Name=fbln1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D).
RA Zhang H.-Y., Lardelli M., Ekblom P.;
RT "Sequence of zebrafish fibulin-1 and its expression in developing heart and
RT other embryonic organs.";
RL Dev. Genes Evol. 207:340-351(1997).
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 such as FN1, LAMA1, NID, AGC1 and CSPG2.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D;
CC IsoId=O42182-1; Sequence=Displayed;
CC Name=C;
CC IsoId=O42182-2; Sequence=VSP_007379;
CC -!- DEVELOPMENTAL STAGE: Isoform C is detected in the later blastula
CC period, 4 hours after fertilization. Isoform D is not detected at this
CC stage, it first appears during the gastrula period in 8 hours old
CC embryos. Expression of both isoforms is then maintained throughout
CC development. During later developmental stages, prominent expression is
CC seen in regions where tissue compartments are continuously moving in
CC relation to each other.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AF013751; AAB80944.1; -; mRNA.
DR EMBL; AF013752; AAB80945.1; -; mRNA.
DR AlphaFoldDB; O42182; -.
DR STRING; 7955.ENSDARP00000108375; -.
DR PaxDb; O42182; -.
DR ZFIN; ZDB-GENE-990415-73; fbln1.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; O42182; -.
DR PhylomeDB; O42182; -.
DR PRO; PR:O42182; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0035122; P:embryonic medial fin morphogenesis; IGI:ZFIN.
DR GO; GO:0030198; P:extracellular matrix organization; IGI:ZFIN.
DR GO; GO:0090497; P:mesenchymal cell migration; IGI:ZFIN.
DR GO; GO:0043589; P:skin morphogenesis; IGI:ZFIN.
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; 2.
DR SMART; SM00181; EGF; 8.
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; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 6.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..681
FT /note="Fibulin-1"
FT /id="PRO_0000007566"
FT DOMAIN 29..63
FT /note="Anaphylatoxin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 68..107
FT /note="Anaphylatoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 108..139
FT /note="Anaphylatoxin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 158..192
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 193..238
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 239..284
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 285..331
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 332..373
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 374..415
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 416..455
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 456..499
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 500..554
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..55
FT /evidence="ECO:0000250"
FT DISULFID 30..62
FT /evidence="ECO:0000250"
FT DISULFID 43..63
FT /evidence="ECO:0000250"
FT DISULFID 72..103
FT /evidence="ECO:0000250"
FT DISULFID 85..104
FT /evidence="ECO:0000250"
FT DISULFID 106..125
FT /evidence="ECO:0000250"
FT DISULFID 107..138
FT /evidence="ECO:0000250"
FT DISULFID 114..139
FT /evidence="ECO:0000250"
FT DISULFID 162..171
FT /evidence="ECO:0000250"
FT DISULFID 167..176
FT /evidence="ECO:0000250"
FT DISULFID 178..191
FT /evidence="ECO:0000250"
FT DISULFID 197..210
FT /evidence="ECO:0000250"
FT DISULFID 204..219
FT /evidence="ECO:0000250"
FT DISULFID 225..237
FT /evidence="ECO:0000250"
FT DISULFID 243..256
FT /evidence="ECO:0000250"
FT DISULFID 250..265
FT /evidence="ECO:0000250"
FT DISULFID 271..283
FT /evidence="ECO:0000250"
FT DISULFID 289..301
FT /evidence="ECO:0000250"
FT DISULFID 317..330
FT /evidence="ECO:0000250"
FT DISULFID 336..348
FT /evidence="ECO:0000250"
FT DISULFID 343..357
FT /evidence="ECO:0000250"
FT DISULFID 359..372
FT /evidence="ECO:0000250"
FT DISULFID 378..390
FT /evidence="ECO:0000250"
FT DISULFID 386..399
FT /evidence="ECO:0000250"
FT DISULFID 401..414
FT /evidence="ECO:0000250"
FT DISULFID 420..429
FT /evidence="ECO:0000250"
FT DISULFID 440..454
FT /evidence="ECO:0000250"
FT DISULFID 460..473
FT /evidence="ECO:0000250"
FT DISULFID 469..482
FT /evidence="ECO:0000250"
FT DISULFID 484..498
FT /evidence="ECO:0000250"
FT DISULFID 504..517
FT /evidence="ECO:0000250"
FT DISULFID 511..526
FT /evidence="ECO:0000250"
FT DISULFID 531..553
FT /evidence="ECO:0000250"
FT VAR_SEQ 542..681
FT /note="RPRVDRADIIRCVKSCQHNDISCVLNPILSHSHTAISLPTFREFNKPEEIVF
FT LRSPTPTHLPHMDSPEIVYDILEGNIQNSFDIIKRLDHGMIVGVVKQVRPLVGPVRTVL
FT KLAMNYVTNGVVSHRNIINVRIYVSEFWF -> RCERLSCNESNECMAFTRRITYYQLT
FT FPAKIPVPTDLFRMGPSNTALGDDIEVAIVDGNRDGFFAAKRLDHGGVLVLQKPIAWPQ
FT DFQIALEMKLKRFGHLSIYLFKIRPVRHARRHQQRY (in isoform C)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_007379"
SQ SEQUENCE 681 AA; 74460 MW; 175C966305A46699 CRC64;
MDLYMIVLLS LCGLLRAQET TDTISLDNCC EDGKKRGLES QDCSSLPLIS ESTTCRVVQE
QCCSAVLEDS ICTSGINMAK DQSSCDALLS GSSTCETKTT KMCCECCLLG SSRCRIRVSP
VSSVCRWSIS RGPGVRSCCV DKQPAHGVQP SKGDAQNTED QCRAAGCAQR CLNGTCSCLD
GFKLKTDGKH CEDINECLLG PHHCVTGERC INTLGSYRCQ REISCGTGYE LTDNNKCKDI
DECDLGTHNC AAEMECQNTA GSFRCRPRMQ CAAGFIQDAL GSCIDINECV SVTALSRGQM
CFNTVGSFIC QRHSVTCGRG YHLNAEGTRC VDIDECAGPD NSCDGHGCIN LVGSYRCECR
TGFIFNSISR SCEDIDECRN YPGRLCAHKC ENILGSYKCS CTAGFKLADD GRNCDDVNEC
ESSPCSQGCA NVYGSYQSYC RRGYQLSDAD GITCEDIDEC ALPTGGHICS YRCHNTPGSF
HCTCPASGYT LAANGRSCQD IDECLTGTHS CSESESCFNI QGGFRCLSFD CPANYRRSGD
TRPRVDRADI IRCVKSCQHN DISCVLNPIL SHSHTAISLP TFREFNKPEE IVFLRSPTPT
HLPHMDSPEI VYDILEGNIQ NSFDIIKRLD HGMIVGVVKQ VRPLVGPVRT VLKLAMNYVT
NGVVSHRNII NVRIYVSEFW F
