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Database: UniProt
Entry: B5X3N0_SALSA
LinkDB: B5X3N0_SALSA
Original site: B5X3N0_SALSA 
ID   B5X3N0_SALSA            Unreviewed;       693 AA.
AC   B5X3N0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Fibulin-1 {ECO:0000256|ARBA:ARBA00021554, ECO:0000256|PIRNR:PIRNR036313};
GN   Name=FBLN1 {ECO:0000313|EMBL:ACI33911.1};
GN   Synonyms=fbln1 {ECO:0000313|RefSeq:NP_001133794.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI33911.1};
RN   [1] {ECO:0000313|EMBL:ACI33911.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33911.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RA   Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI33911.1, ECO:0000313|RefSeq:NP_001133794.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33911.1};
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
RN   [3] {ECO:0000313|EMBL:ACI33911.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33911.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001133794.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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; BT045649; ACI33911.1; -; mRNA.
DR   RefSeq; NP_001133794.1; NM_001140322.1.
DR   STRING; 8030.ENSSSAP00000018414; -.
DR   PaxDb; 8030-ENSSSAP00000018414; -.
DR   GeneID; 100195293; -.
DR   KEGG; sasa:100195293; -.
DR   OrthoDB; 19806at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa10.
DR   Bgee; ENSSSAG00000007086; Expressed in nose and 15 other cell types or tissues.
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:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 4.
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:SF97; FIBULIN-1; 1.
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; 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; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 3.
PE   2: Evidence at transcript level;
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   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036313};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001133794.1}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..693
FT                   /note="Fibulin-1"
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001133794.1"
FT                   /id="PRO_5009732187"
FT   DOMAIN          28..62
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01178"
FT   DOMAIN          428..467
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          468..511
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
SQ   SEQUENCE   693 AA;  75392 MW;  FC8F5CBE01C07A62 CRC64;
     MGPGIVILFS LFGVLNGQGG KQISMDECCK DGRARGIDNQ DCTAIPLISE STTCRIVQEQ
     CCAAVLEDNI CTSGINMAKD QGACDTQFTG STCETKTAKM CCDCCLLGRA AREQGLTCDH
     SLSLGYQCGL VSRACCDDRA PDVETKISQV SDKDNKTLTE KENPLPNNMC SSGVATCAQE
     CVGNSTCACF KGYKLKPDGK NCEDINECLL GASNCRGGEH CINTVGSFRC QREVSCGTGY
     ELMDSNNCKD IDECESGTHN CSPDFECQNT QGSFRCLPKN QCGDGYIQDA MGSCIDINEC
     LAQTEPCRPG QLCMNTMGSF TCQRNSINCG RGYHLNDGGN RCVDIDECKG PDGACAGHGC
     INLVGSFRCE CKIGFIFNSI SRVCEDINEC RHYPGRLCAH KCENVLGSYK CSCTQGFKLA
     SDGRNCDDLN ECESSPCSQE CANVYGSYQC YCRRGYQLSD IDGINCEDID ECALPTGGHI
     CSYRCNNTPG SFYCTCPATG YTLAPNGRSC QDVDECVTGT HTCSVTESCF NVQGGFRCLS
     FECPPNYRQA GEIRARVERS DTIRCVKSCQ PNDIGCVLDP VHSVSHTVIS LPTFREFTKP
     EEIVFLRTMS PAHSSPQLSS DIVFDILEGN VQNSFDIVKR QEHGMIVGVV RQVKPLIGSL
     NMVLKLAMNY VTSGVVSHRN IVNVHIFVSE FWF
//
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