ID   FBLN1_MOUSE             Reviewed;         705 AA.
AC   Q08879; Q08878; Q8C3B1; Q91ZC9; Q922K8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=Fibulin-1;
DE            Short=FIBL-1;
DE   AltName: Full=Basement-membrane protein 90;
DE            Short=BM-90;
DE   Flags: Precursor;
GN   Name=Fbln1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), AND LIGANDS INTERACTION.
RX   PubMed=8354280; DOI=10.1111/j.1432-1033.1993.tb18086.x;
RA   Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.;
RT   "Sequence of extracellular mouse protein BM-90/fibulin and its calcium-
RT   dependent binding to other basement-membrane ligands.";
RL   Eur. J. Biochem. 215:733-740(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX   PubMed=11829738; DOI=10.1042/0264-6021:3620041;
RA   Castoldi M., Chu M.-L.;
RT   "Structural and functional characterization of the human and mouse fibulin-
RT   1 gene promoters: role of Sp1 and Sp3.";
RL   Biochem. J. 362:41-50(2002).
RN   [5]
RP   PROTEIN SEQUENCE OF 30-53; 110-117; 231-243; 339-387; 434-439; 469-476;
RP   553-563 AND 574-581.
RX   PubMed=2249686; DOI=10.1111/j.1432-1033.1990.tb19383.x;
RA   Kluge M., Mann K., Dziadek M., Timpl R.;
RT   "Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90)
RT   shared by basement membranes and serum.";
RL   Eur. J. Biochem. 193:651-659(1990).
RN   [6]
RP   CHARACTERIZATION OF NID AFFINITY.
RX   PubMed=7844816; DOI=10.1006/jmbi.1994.0020;
RA   Sasaki T., Kostka G., Goehring W., Wiedemann H., Mann K., Chu M.-L.,
RA   Timpl R.;
RT   "Structural characterization of two variants of fibulin-1 that differ in
RT   nidogen affinity.";
RL   J. Mol. Biol. 245:241-250(1995).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8850569;
RX   DOI=10.1002/(sici)1097-0177(199603)205:3<348::aid-aja13>3.0.co;2-0;
RA   Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.;
RT   "Fibulin-1 and fibulin-2 expression during organogenesis in the developing
RT   mouse embryo.";
RL   Dev. Dyn. 205:348-364(1996).
RN   [8]
RP   NID-BINDING SITE.
RC   STRAIN=129/Sv;
RX   PubMed=9299350; DOI=10.1006/jmbi.1997.1244;
RA   Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.;
RT   "Binding of fibulin-1 to nidogen depends on its C-terminal globular domain
RT   and a specific array of calcium-binding epidermal growth factor-like (EG)
RT   modules.";
RL   J. Mol. Biol. 272:226-236(1997).
RN   [9]
RP   INTERACTION WITH LAMA2.
RX   PubMed=10022829; DOI=10.1093/emboj/18.4.863;
RA   Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.;
RT   "Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan
RT   to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix
RT   proteins.";
RL   EMBO J. 18:863-870(1999).
RN   [10]
RP   INTERACTION WITH ACAN AND CSPG2.
RX   PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
RA   Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
RT   "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
RT   versican.";
RL   J. Biol. Chem. 274:20444-20449(1999).
RN   [11]
RP   INTERACTION WITH NID.
RX   PubMed=11589703; DOI=10.1046/j.0014-2956.2001.02437.x;
RA   Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.;
RT   "Recombinant domains of mouse nidogen-1 and their binding to basement
RT   membrane proteins and monoclonal antibodies.";
RL   Eur. J. Biochem. 268:5119-5128(2001).
RN   [12]
RP   DOWN-REGULATION BY GLUCOCORTICOIDS.
RX   PubMed=11737251; DOI=10.1034/j.1600-0609.2001.5790528.x;
RA   Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.;
RT   "Glucocorticoids down-regulate the extracellular matrix proteins
RT   fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma.";
RL   Eur. J. Haematol. 67:176-184(2001).
RN   [13]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11238726; DOI=10.1046/j.1471-4159.2001.00144.x;
RA   Ohsawa I., Takamura C., Kohsaka S.;
RT   "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein
RT   and modulates its physiological function.";
RL   J. Neurochem. 76:1411-1420(2001).
RN   [14]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11836357; DOI=10.1136/jmg.39.2.98;
RA   Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S., De Smet L.,
RA   Fryns J.-P., Van De Ven W.J.M.;
RT   "The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with a
RT   complex type of synpolydactyly.";
RL   J. Med. Genet. 39:98-104(2002).
RN   [15]
RP   INTERACTION WITH FBLN7.
RX   PubMed=17699513; DOI=10.1074/jbc.m705847200;
RA   de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A., Fisher L.W.,
RA   Fukumoto S., Yamada Y.;
RT   "TM14 is a new member of the fibulin family (fibulin-7) that interacts with
RT   extracellular matrix molecules and is active for cell binding.";
RL   J. Biol. Chem. 282:30878-30888(2007).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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, LMA2, NID, ACAN, CSPG2 and type
CC       IV collagen. Binding analysis demonstrated for isoform C a 100-fold
CC       stronger binding to the basement membrane protein NID than for isoform
CC       D. Interacts with FBLN7. Interacts with CCN3 (By similarity).
CC       {ECO:0000250|UniProtKB:P23142, ECO:0000269|PubMed:10022829,
CC       ECO:0000269|PubMed:10400671, ECO:0000269|PubMed:11589703,
CC       ECO:0000269|PubMed:17699513}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=D;
CC         IsoId=Q08879-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q08879-3; Sequence=Not described;
CC       Name=B;
CC         IsoId=Q08879-4; Sequence=Not described;
CC       Name=C;
CC         IsoId=Q08879-2; Sequence=VSP_001386;
CC   -!- TISSUE SPECIFICITY: Detected in most organs (brain, heart, lung,
CC       spleen, liver and kidney). Neurons are the predominant source of
CC       production in the brain. Not expressed significantly by astrocytes or
CC       microglia. {ECO:0000269|PubMed:11238726}.
CC   -!- DEVELOPMENTAL STAGE: The differential expression of the fibulin family
CC       contributes to the formation of molecularly distinct extracellular
CC       matrices already during early developmental stages of a large number of
CC       tissues. Increased expression at neonate stage in the brain. Expressed
CC       in interdigital regions of the handplate of a 12 dpc embryo and in the
CC       lateral perichondrial region. Similar expression persists in the 13 dpc
CC       handplate particularly in the perichondrial regions and apical aspects
CC       of the developing digits. {ECO:0000269|PubMed:11238726,
CC       ECO:0000269|PubMed:11836357, ECO:0000269|PubMed:8850569}.
CC   -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC       synthesis.
CC   -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR   EMBL; X70854; CAA50207.1; -; mRNA.
DR   EMBL; X70853; CAA50206.1; -; mRNA.
DR   EMBL; AK086451; BAC39669.1; -; mRNA.
DR   EMBL; AK035388; BAC29054.1; -; mRNA.
DR   EMBL; BC007140; AAH07140.1; -; mRNA.
DR   EMBL; AY040588; AAK82944.1; -; Genomic_DNA.
DR   CCDS; CCDS27719.1; -. [Q08879-1]
DR   CCDS; CCDS84186.1; -. [Q08879-2]
DR   PIR; S34968; S34968.
DR   PIR; S78040; S78040.
DR   RefSeq; NP_001334017.1; NM_001347088.1. [Q08879-2]
DR   RefSeq; NP_034310.2; NM_010180.2. [Q08879-1]
DR   AlphaFoldDB; Q08879; -.
DR   BioGRID; 199605; 7.
DR   IntAct; Q08879; 1.
DR   MINT; Q08879; -.
DR   STRING; 10090.ENSMUSP00000054583; -.
DR   GlyCosmos; Q08879; 3 sites, No reported glycans.
DR   GlyGen; Q08879; 3 sites.
DR   PhosphoSitePlus; Q08879; -.
DR   MaxQB; Q08879; -.
DR   PaxDb; 10090-ENSMUSP00000054583; -.
DR   PeptideAtlas; Q08879; -.
DR   ProteomicsDB; 271872; -. [Q08879-1]
DR   ProteomicsDB; 271873; -. [Q08879-2]
DR   Antibodypedia; 886; 365 antibodies from 34 providers.
DR   DNASU; 14114; -.
DR   Ensembl; ENSMUST00000057410.14; ENSMUSP00000054583.8; ENSMUSG00000006369.15. [Q08879-1]
DR   Ensembl; ENSMUST00000109432.4; ENSMUSP00000105058.4; ENSMUSG00000006369.15. [Q08879-2]
DR   GeneID; 14114; -.
DR   KEGG; mmu:14114; -.
DR   UCSC; uc007xdb.2; mouse. [Q08879-2]
DR   UCSC; uc011zxk.1; mouse. [Q08879-1]
DR   AGR; MGI:95487; -.
DR   CTD; 2192; -.
DR   MGI; MGI:95487; Fbln1.
DR   VEuPathDB; HostDB:ENSMUSG00000006369; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00940000156642; -.
DR   HOGENOM; CLU_004826_1_1_1; -.
DR   InParanoid; Q08879; -.
DR   OMA; KCAEGEL; -.
DR   OrthoDB; 19806at2759; -.
DR   PhylomeDB; Q08879; -.
DR   TreeFam; TF317514; -.
DR   BioGRID-ORCS; 14114; 0 hits in 76 CRISPR screens.
DR   ChiTaRS; Fbln1; mouse.
DR   PRO; PR:Q08879; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q08879; Protein.
DR   Bgee; ENSMUSG00000006369; Expressed in aortic valve and 270 other cell types or tissues.
DR   ExpressionAtlas; Q08879; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0071953; C:elastic fiber; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; ISO:MGI.
DR   GO; GO:0070051; F:fibrinogen binding; ISO:MGI.
DR   GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:MGI.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR   GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:2000647; P:negative regulation of stem cell proliferation; ISO:MGI.
DR   GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:1904188; P:negative regulation of transformation of host cell by virus; ISO:MGI.
DR   GO; GO:0071635; P:negative regulation of transforming growth factor beta production; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; ISO:MGI.
DR   CDD; cd00017; ANATO; 2.
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:SF198; RE68558P; 1.
DR   Pfam; PF01821; ANATO; 2.
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; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 3.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 8.
DR   Genevisible; Q08879; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:2249686"
FT   CHAIN           30..705
FT                   /note="Fibulin-1"
FT                   /id="PRO_0000007564"
FT   DOMAIN          36..76
FT                   /note="Anaphylatoxin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DOMAIN          77..111
FT                   /note="Anaphylatoxin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DOMAIN          112..144
FT                   /note="Anaphylatoxin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DOMAIN          178..217
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          218..263
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          264..309
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          310..357
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          358..400
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          401..442
FT                   /note="EGF-like 6; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          443..482
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          483..526
FT                   /note="EGF-like 8; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          527..580
FT                   /note="EGF-like 9; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          156..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..442
FT                   /note="Self-association and FN1-binding"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        537
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        541
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        112..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        113..143
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        182..192
FT                   /evidence="ECO:0000250"
FT   DISULFID        188..201
FT                   /evidence="ECO:0000250"
FT   DISULFID        203..216
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..235
FT                   /evidence="ECO:0000250"
FT   DISULFID        229..244
FT                   /evidence="ECO:0000250"
FT   DISULFID        250..262
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..281
FT                   /evidence="ECO:0000250"
FT   DISULFID        275..290
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..308
FT                   /evidence="ECO:0000250"
FT   DISULFID        314..327
FT                   /evidence="ECO:0000250"
FT   DISULFID        321..336
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..356
FT                   /evidence="ECO:0000250"
FT   DISULFID        362..375
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..384
FT                   /evidence="ECO:0000250"
FT   DISULFID        386..399
FT                   /evidence="ECO:0000250"
FT   DISULFID        405..417
FT                   /evidence="ECO:0000250"
FT   DISULFID        413..426
FT                   /evidence="ECO:0000250"
FT   DISULFID        428..441
FT                   /evidence="ECO:0000250"
FT   DISULFID        447..456
FT                   /evidence="ECO:0000250"
FT   DISULFID        452..465
FT                   /evidence="ECO:0000250"
FT   DISULFID        467..481
FT                   /evidence="ECO:0000250"
FT   DISULFID        487..500
FT                   /evidence="ECO:0000250"
FT   DISULFID        496..509
FT                   /evidence="ECO:0000250"
FT   DISULFID        511..525
FT                   /evidence="ECO:0000250"
FT   DISULFID        531..544
FT                   /evidence="ECO:0000250"
FT   DISULFID        538..553
FT                   /evidence="ECO:0000250"
FT   DISULFID        558..579
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         569..705
FT                   /note="FRQEKTDTVRCIKSCRPNDEACVRDPVHTVSHTVISLPTFREFTRPEEIIFL
FT                   RAVTPLYPANQADIIFDITEGNLRDSFDIIKRYEDGMTVGVVRQVRPIVGPFYAVLKLE
FT                   MNYVLGGVVSHRNVVNVHIFVSEYWF -> RCERLPCHENQECPRLPLRITYYHLSFPT
FT                   NIQVPAVVFRMGPSSAVPGDSMQLAITAGNEEGFFTTRKVSHHSGVVALTKPIPEPRDL
FT                   LLTVKMDLYRHGTVSSFVAKLFIFVSAEL (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8354280"
FT                   /id="VSP_001386"
FT   CONFLICT        30
FT                   /note="D -> N (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="G -> P (in Ref. 1; CAA50207)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="S -> A (in Ref. 1; CAA50207)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="E -> K (in Ref. 2; BAC39669)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        553
FT                   /note="C -> Q (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        558
FT                   /note="C -> Q (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q08879-2:571
FT                   /note="E -> A (in Ref. 1; CAA50206)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   705 AA;  78033 MW;  76C527A12E97D0E1 CRC64;
     MERPVPSRLV PLPLLLLSSL SLLAARANAD ISMEACCTDG NQMANQHRDC SLPYTSESKE
     CRMVQEQCCH NQLEELHCAT GINLASEPEG CASLHSYNSS LETIFIKRCC HCCMLGKASL
     ARDQTCEPIV MISYQCGLVF RACCVKAREN SDFVQGNGAD LQDPAKIPDE EDQEDPYLND
     RCRGGGPCKQ QCRDTGDEVI CSCFVGYQLQ SDGVSCEDIN ECITGSHNCR LGESCINTVG
     SFRCQRDSSC GTGYELTEDN NCKDIDECET GIHNCPPDFI CQNTLGSFRC RPKLQCKSGF
     IQDALGNCID INECLSISAP CPVGQTCINT EGSYTCQKNV PNCGRGYHLN EEGTRCVDVD
     ECSPPAEPCG KGHHCLNSPG SFRCECKAGF YFDGISRTCV DINECQRYPG RLCGHKCENT
     PGSFHCSCSA GFRLSVDGRS CEDVNECLNS PCSQECANVY GSYQCYCRRG YQLSDVDGVT
     CEDIDECALP TGGHICSYRC INIPGSFQCS CPSSGYRLAP NGRNCQDIDE CVTGIHNCSI
     NETCFNIQGS FRCLSFECPE NYRRSADTFR QEKTDTVRCI KSCRPNDEAC VRDPVHTVSH
     TVISLPTFRE FTRPEEIIFL RAVTPLYPAN QADIIFDITE GNLRDSFDII KRYEDGMTVG
     VVRQVRPIVG PFYAVLKLEM NYVLGGVVSH RNVVNVHIFV SEYWF
//