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Fibulin-1 (FIBL-1) (Basement-membrane protein 90) (BM-90)

 FBLN1_MOUSE             Reviewed;         705 AA.
Q08879; Q08878; Q8C3B1; Q91ZC9; Q922K8;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
09-MAY-2003, sequence version 2.
12-SEP-2018, entry version 182.
RecName: Full=Fibulin-1;
Short=FIBL-1;
AltName: Full=Basement-membrane protein 90;
Short=BM-90;
Flags: Precursor;
Name=Fbln1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), AND LIGANDS
INTERACTION.
PubMed=8354280; DOI=10.1111/j.1432-1033.1993.tb18086.x;
Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.;
"Sequence of extracellular mouse protein BM-90/fibulin and its
calcium-dependent binding to other basement-membrane ligands.";
Eur. J. Biochem. 215:733-740(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
STRAIN=C57BL/6J; TISSUE=Head, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
PubMed=11829738; DOI=10.1042/0264-6021:3620041;
Castoldi M., Chu M.-L.;
"Structural and functional characterization of the human and mouse
fibulin-1 gene promoters: role of Sp1 and Sp3.";
Biochem. J. 362:41-50(2002).
[5]
PROTEIN SEQUENCE OF 30-53; 110-117; 231-243; 339-387; 434-439;
469-476; 553-563 AND 574-581.
PubMed=2249686; DOI=10.1111/j.1432-1033.1990.tb19383.x;
Kluge M., Mann K., Dziadek M., Timpl R.;
"Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-
90) shared by basement membranes and serum.";
Eur. J. Biochem. 193:651-659(1990).
[6]
CHARACTERIZATION OF NID AFFINITY.
PubMed=7844816; DOI=10.1006/jmbi.1994.0020;
Sasaki T., Kostka G., Goehring W., Wiedemann H., Mann K., Chu M.-L.,
Timpl R.;
"Structural characterization of two variants of fibulin-1 that differ
in nidogen affinity.";
J. Mol. Biol. 245:241-250(1995).
[7]
DEVELOPMENTAL STAGE.
PubMed=8850569;
DOI=10.1002/(SICI)1097-0177(199603)205:3<348::AID-AJA13>3.0.CO;2-0;
Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.;
"Fibulin-1 and fibulin-2 expression during organogenesis in the
developing mouse embryo.";
Dev. Dyn. 205:348-364(1996).
[8]
NID-BINDING SITE.
STRAIN=129/Sv;
PubMed=9299350; DOI=10.1006/jmbi.1997.1244;
Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.;
"Binding of fibulin-1 to nidogen depends on its C-terminal globular
domain and a specific array of calcium-binding epidermal growth
factor-like (EG) modules.";
J. Mol. Biol. 272:226-236(1997).
[9]
INTERACTION WITH LAMA2.
PubMed=10022829; DOI=10.1093/emboj/18.4.863;
Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.;
"Binding of the G domains of laminin alpha1 and alpha2 chains and
perlecan to heparin, sulfatides, alpha-dystroglycan and several
extracellular matrix proteins.";
EMBO J. 18:863-870(1999).
[10]
INTERACTION WITH ACAN AND CSPG2.
PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
"Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
versican.";
J. Biol. Chem. 274:20444-20449(1999).
[11]
INTERACTION WITH NID.
PubMed=11589703; DOI=10.1046/j.0014-2956.2001.02437.x;
Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.;
"Recombinant domains of mouse nidogen-1 and their binding to basement
membrane proteins and monoclonal antibodies.";
Eur. J. Biochem. 268:5119-5128(2001).
[12]
DOWN-REGULATION BY GLUCOCORTICOIDS.
PubMed=11737251; DOI=10.1034/j.1600-0609.2001.5790528.x;
Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.;
"Glucocorticoids down-regulate the extracellular matrix proteins
fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma.";
Eur. J. Haematol. 67:176-184(2001).
[13]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11238726; DOI=10.1046/j.1471-4159.2001.00144.x;
Ohsawa I., Takamura C., Kohsaka S.;
"Fibulin-1 binds the amino-terminal head of beta-amyloid precursor
protein and modulates its physiological function.";
J. Neurochem. 76:1411-1420(2001).
[14]
DEVELOPMENTAL STAGE.
PubMed=11836357; DOI=10.1136/jmg.39.2.98;
Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S.,
De Smet L., Fryns J.-P., Van De Ven W.J.M.;
"The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with
a complex type of synpolydactyly.";
J. Med. Genet. 39:98-104(2002).
[15]
INTERACTION WITH FBLN7.
PubMed=17699513; DOI=10.1074/jbc.M705847200;
de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A.,
Fisher L.W., Fukumoto S., Yamada Y.;
"TM14 is a new member of the fibulin family (fibulin-7) that interacts
with extracellular matrix molecules and is active for cell binding.";
J. Biol. Chem. 282:30878-30888(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Incorporated into fibronectin-containing matrix fibers.
May play a role in cell adhesion and migration along protein
fibers within the extracellular matrix (ECM). Could be important
for certain developmental processes and contribute to the
supramolecular organization of ECM architecture, in particular to
those of basement membranes.
-!- SUBUNIT: Homomultimerizes and interacts with various extracellular
matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and
type IV collagen. Binding analysis demonstrated for isoform C a
100-fold stronger binding to the basement membrane protein NID
than for isoform D. Interacts with FBLN7.
{ECO:0000269|PubMed:10022829, ECO:0000269|PubMed:10400671,
ECO:0000269|PubMed:11589703, ECO:0000269|PubMed:17699513}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=D;
IsoId=Q08879-1; Sequence=Displayed;
Name=A;
IsoId=Q08879-3; Sequence=Not described;
Name=B;
IsoId=Q08879-4; Sequence=Not described;
Name=C;
IsoId=Q08879-2; Sequence=VSP_001386;
Note=Ref.1 (CAA50206) sequence is in conflict in position:
571:E->A.;
-!- TISSUE SPECIFICITY: Detected in most organs (brain, heart, lung,
spleen, liver and kidney). Neurons are the predominant source of
production in the brain. Not expressed significantly by astrocytes
or microglia. {ECO:0000269|PubMed:11238726}.
-!- DEVELOPMENTAL STAGE: The differential expression of the fibulin
family contributes to the formation of molecularly distinct
extracellular matrices already during early developmental stages
of a large number of tissues. Increase expression at neonate stage
in the brain. Expressed in interdigital regions of the handplate
of a 12 dpc embryo and in the lateral perichondrial region.
Similar expression persists in the 13 dpc handplate particularly
in the perichondrial regions and apical aspects of the developing
digits. {ECO:0000269|PubMed:11238726, ECO:0000269|PubMed:11836357,
ECO:0000269|PubMed:8850569}.
-!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
synthesis.
-!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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EMBL; X70854; CAA50207.1; -; mRNA.
EMBL; X70853; CAA50206.1; -; mRNA.
EMBL; AK086451; BAC39669.1; -; mRNA.
EMBL; AK035388; BAC29054.1; -; mRNA.
EMBL; BC007140; AAH07140.1; -; mRNA.
EMBL; AY040588; AAK82944.1; -; Genomic_DNA.
CCDS; CCDS27719.1; -. [Q08879-1]
CCDS; CCDS84186.1; -. [Q08879-2]
PIR; S34968; S34968.
PIR; S78040; S78040.
RefSeq; NP_001334017.1; NM_001347088.1. [Q08879-2]
RefSeq; NP_034310.2; NM_010180.2. [Q08879-1]
UniGene; Mm.297992; -.
ProteinModelPortal; Q08879; -.
SMR; Q08879; -.
BioGrid; 199605; 1.
IntAct; Q08879; 2.
MINT; Q08879; -.
STRING; 10090.ENSMUSP00000054583; -.
PhosphoSitePlus; Q08879; -.
PaxDb; Q08879; -.
PeptideAtlas; Q08879; -.
PRIDE; Q08879; -.
Ensembl; ENSMUST00000057410; ENSMUSP00000054583; ENSMUSG00000006369. [Q08879-1]
Ensembl; ENSMUST00000109432; ENSMUSP00000105058; ENSMUSG00000006369. [Q08879-2]
GeneID; 14114; -.
KEGG; mmu:14114; -.
UCSC; uc007xdb.2; mouse. [Q08879-2]
UCSC; uc011zxk.1; mouse. [Q08879-1]
CTD; 2192; -.
MGI; MGI:95487; Fbln1.
eggNOG; ENOG410IR7F; Eukaryota.
eggNOG; ENOG410Y194; LUCA.
GeneTree; ENSGT00760000118806; -.
HOGENOM; HOG000007079; -.
HOVERGEN; HBG051559; -.
InParanoid; Q08879; -.
KO; K17307; -.
OMA; GHLCVNS; -.
OrthoDB; EOG091G02LJ; -.
PhylomeDB; Q08879; -.
TreeFam; TF317514; -.
Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
PRO; PR:Q08879; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000006369; Expressed in 297 organ(s), highest expression level in ear vesicle.
CleanEx; MM_FBLN1; -.
ExpressionAtlas; Q08879; baseline and differential.
Genevisible; Q08879; MM.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0071953; C:elastic fiber; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; ISO:MGI.
GO; GO:0005201; F:extracellular matrix structural constituent; ISO:MGI.
GO; GO:0070051; F:fibrinogen binding; ISO:MGI.
GO; GO:0001968; F:fibronectin binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:MGI.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
GO; GO:2000647; P:negative regulation of stem cell proliferation; ISO:MGI.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:1904188; P:negative regulation of transformation of host cell by virus; ISO:MGI.
GO; GO:2001202; P:negative regulation of transforming growth factor-beta secretion; ISO:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; ISO:MGI.
CDD; cd00017; ANATO; 2.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR026823; cEGF.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR017048; Fibulin-1.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
Pfam; PF12662; cEGF; 3.
Pfam; PF07645; EGF_CA; 4.
PIRSF; PIRSF036313; Fibulin-1; 1.
SMART; SM00104; ANATO; 3.
SMART; SM00181; EGF; 9.
SMART; SM00179; EGF_CA; 8.
SUPFAM; SSF57184; SSF57184; 4.
PROSITE; PS01177; ANAPHYLATOXIN_1; 3.
PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 8.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 29 {ECO:0000269|PubMed:2249686}.
CHAIN 30 705 Fibulin-1.
/FTId=PRO_0000007564.
DOMAIN 36 76 Anaphylatoxin-like 1.
{ECO:0000255|PROSITE-ProRule:PRU00022}.
DOMAIN 77 111 Anaphylatoxin-like 2.
{ECO:0000255|PROSITE-ProRule:PRU00022}.
DOMAIN 112 144 Anaphylatoxin-like 3.
{ECO:0000255|PROSITE-ProRule:PRU00022}.
DOMAIN 178 217 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 218 263 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 264 309 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 310 357 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 358 400 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 401 442 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 443 482 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 483 526 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 527 580 EGF-like 9; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REGION 358 442 Self-association and FN1-binding.
{ECO:0000250}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 537 537 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 61 {ECO:0000250}.
DISULFID 37 68 {ECO:0000250}.
DISULFID 50 69 {ECO:0000250}.
DISULFID 78 109 {ECO:0000250}.
DISULFID 91 110 {ECO:0000250}.
DISULFID 112 136 {ECO:0000250}.
DISULFID 113 143 {ECO:0000250}.
DISULFID 126 144 {ECO:0000250}.
DISULFID 182 192 {ECO:0000250}.
DISULFID 188 201 {ECO:0000250}.
DISULFID 203 216 {ECO:0000250}.
DISULFID 222 235 {ECO:0000250}.
DISULFID 229 244 {ECO:0000250}.
DISULFID 250 262 {ECO:0000250}.
DISULFID 268 281 {ECO:0000250}.
DISULFID 275 290 {ECO:0000250}.
DISULFID 296 308 {ECO:0000250}.
DISULFID 314 327 {ECO:0000250}.
DISULFID 321 336 {ECO:0000250}.
DISULFID 343 356 {ECO:0000250}.
DISULFID 362 375 {ECO:0000250}.
DISULFID 369 384 {ECO:0000250}.
DISULFID 386 399 {ECO:0000250}.
DISULFID 405 417 {ECO:0000250}.
DISULFID 413 426 {ECO:0000250}.
DISULFID 428 441 {ECO:0000250}.
DISULFID 447 456 {ECO:0000250}.
DISULFID 452 465 {ECO:0000250}.
DISULFID 467 481 {ECO:0000250}.
DISULFID 487 500 {ECO:0000250}.
DISULFID 496 509 {ECO:0000250}.
DISULFID 511 525 {ECO:0000250}.
DISULFID 531 544 {ECO:0000250}.
DISULFID 538 553 {ECO:0000250}.
DISULFID 558 579 {ECO:0000250}.
VAR_SEQ 569 705 FRQEKTDTVRCIKSCRPNDEACVRDPVHTVSHTVISLPTFR
EFTRPEEIIFLRAVTPLYPANQADIIFDITEGNLRDSFDII
KRYEDGMTVGVVRQVRPIVGPFYAVLKLEMNYVLGGVVSHR
NVVNVHIFVSEYWF -> RCERLPCHENQECPRLPLRITYY
HLSFPTNIQVPAVVFRMGPSSAVPGDSMQLAITAGNEEGFF
TTRKVSHHSGVVALTKPIPEPRDLLLTVKMDLYRHGTVSSF
VAKLFIFVSAEL (in isoform C).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:8354280}.
/FTId=VSP_001386.
CONFLICT 30 30 D -> N (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 40 40 G -> P (in Ref. 1; CAA50207).
{ECO:0000305}.
CONFLICT 363 363 S -> A (in Ref. 1; CAA50207).
{ECO:0000305}.
CONFLICT 385 385 E -> K (in Ref. 2; BAC39669).
{ECO:0000305}.
CONFLICT 553 553 C -> Q (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 558 558 C -> Q (in Ref. 5; AA sequence).
{ECO:0000305}.
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


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E0136m ELISA Basement-membrane protein 90,BM-90,Fbln1,FIBL-1,Fibulin-1,Mouse,Mus musculus 96T
U0136m CLIA Basement-membrane protein 90,BM-90,Fbln1,FIBL-1,Fibulin-1,Mouse,Mus musculus 96T
E0136m ELISA kit Basement-membrane protein 90,BM-90,Fbln1,FIBL-1,Fibulin-1,Mouse,Mus musculus 96T
EIAAB14479 Efemp1,EGF-containing fibulin-like extracellular matrix protein 1,Fbln3,FIBL-3,Fibulin-3,Mouse,Mus musculus
EIAAB14478 Efemp1,EGF-containing fibulin-like extracellular matrix protein 1,Fbln3,FIBL-3,Fibulin-3,Rat,Rattus norvegicus,T16 protein
EIAAB14482 EFEMP2,EGF-containing fibulin-like extracellular matrix protein 2,FBLN4,FIBL-4,Fibulin-4,Homo sapiens,Human,Protein UPH1,UNQ200_PRO226
EIAAB14481 Efemp2,EGF-containing fibulin-like extracellular matrix protein 2,Fbln4,FIBL-4,Fibulin-4,Mbp1,Mouse,Mus musculus,Mutant p53-binding protein 1
EIAAB14480 EFEMP1,EGF-containing fibulin-like extracellular matrix protein 1,Extracellular protein S1-5,FBLN3,FBNL,FIBL-3,Fibrillin-like protein,Fibulin-3,Homo sapiens,Human
EIAAB14487 Fbln7,FIBL-7,Fibulin-7,Mouse,Mus musculus,Protein TM14,Tm14
EIAAB14484 Bos taurus,Bovine,FBLN5,FIBL-5,Fibulin-5
EIAAB14477 Fbln2,FIBL-2,Fibulin-2,Mouse,Mus musculus
EIAAB14485 Dance,DANCE,Developmental arteries and neural crest EGF-like protein,FBLN5,FIBL-5,Fibulin-5,Homo sapiens,Human,UNQ184_PRO210,UP50,Urine p50 protein
EIAAB14486 Dance,Dance,Developmental arteries and neural crest EGF-like protein,Embryonic vascular EGF repeat-containing protein,EVEC,Fbln5,FIBL-5,Fibulin-5,Rat,Rattus norvegicus
EIAAB14483 Dance,Dance,Developmental arteries and neural crest EGF-like protein,Fbln5,FIBL-5,Fibulin-5,Mouse,Mus musculus
EIAAB14476 FBLN2,FIBL-2,Fibulin-2,Homo sapiens,Human
EIAAB14488 FBLN7,FIBL-7,Fibulin-7,Homo sapiens,Human,TM14
E0136h ELISA FBLN1,FIBL-1,Fibulin-1,Homo sapiens,Human,PP213 96T
E0136h ELISA kit FBLN1,FIBL-1,Fibulin-1,Homo sapiens,Human,PP213 96T
U0136h CLIA FBLN1,FIBL-1,Fibulin-1,Homo sapiens,Human,PP213 96T
E0136c ELISA Chicken,FBLN1,FIBL-1,Fibulin-1,Gallus gallus 96T
E0136c ELISA kit Chicken,FBLN1,FIBL-1,Fibulin-1,Gallus gallus 96T
U0136c CLIA Chicken,FBLN1,FIBL-1,Fibulin-1,Gallus gallus 96T
gen11509 SPRC_MOUSE Basement-membrane protein 40 ELISA tesk kit 1
gen11523 SPRC_RABIT Basement-membrane protein 40 ELISA tesk kit 1
gen11530 SPRC_RAT Basement-membrane protein 40 ELISA tesk kit 1


 

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