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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.
13-FEB-2019, entry version 186.
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. Interacts with CCN3 (By
similarity). {ECO:0000250|UniProtKB:P23142,
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; ENSGT00940000156642; -.
HOGENOM; HOG000007079; -.
HOVERGEN; HBG051559; -.
InParanoid; Q08879; -.
KO; K17307; -.
OMA; CHENQEC; -.
OrthoDB; 1174178at2759; -.
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.
ExpressionAtlas; Q08879; baseline and differential.
Genevisible; Q08879; MM.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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:0005509; F:calcium ion binding; ISO:MGI.
GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
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; 3.
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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Gentaur; yes we can

Pathways :
WP1502: Mitochondrial biogenesis
WP1624: Bacterial secretion system
WP1665: Limonene and pinene degradation
WP1689: Porphyrin and chlorophyll metabolism
WP1692: Protein export
WP1713: Two-component system
WP1714: Tyrosine metabolism
WP2199: Seed Development
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1488: CFTR activity in the plasma membrane
WP1493: Carbon assimilation C4 pathway
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1616: ABC transporters
WP1625: Base excision repair
WP1626: Benzoate degradation via CoA ligation
WP1644: DNA replication
WP1646: Ethylbenzene degradation
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation

Related Genes :
[Fbln1] Fibulin-1 (FIBL-1) (Basement-membrane protein 90) (BM-90)
[EFEMP2 FBLN4 UNQ200/PRO226] EGF-containing fibulin-like extracellular matrix protein 2 (Fibulin-4) (FIBL-4) (Protein UPH1)
[FBLN5 DANCE UNQ184/PRO210] Fibulin-5 (FIBL-5) (Developmental arteries and neural crest EGF-like protein) (Dance) (Urine p50 protein) (UP50)
[FBLN2] Fibulin-2 (FIBL-2)
[icsA virG CP0182] Outer membrane protein IcsA autotransporter [Cleaved into: Outer membrane protein IcsA; Outer membrane protein IcsA translocator]
[SPARC ON] SPARC (Basement-membrane protein 40) (BM-40) (Osteonectin) (ON) (Secreted protein acidic and rich in cysteine)
[Sparc] SPARC (Basement-membrane protein 40) (BM-40) (Osteonectin) (ON) (Secreted protein acidic and rich in cysteine)
[HSP90AA1 HSP90A HSPC1 HSPCA] Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[Hsp90aa1 Hsp86 Hsp86-1 Hspca] Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Tumor-specific transplantation 86 kDa antigen) (TSTA)
[RPS6KA1 MAPKAPK1A RSK1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[Hsp90ab1 Hsp84 Hsp84-1 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84) (Tumor-specific transplantation 84 kDa antigen) (TSTA)
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[HSP90-5 CR88 EMB1956 HSP88-1 At2g04030] Heat shock protein 90-5, chloroplastic (AtHSP90.5) (AtHsp90-5) (Heat shock protein 88-1) (Hsp88-1) (Hsp90C) (Protein EMBRYO DEFECTIVE 1956) (Protein chlorate-resistance 88)
[TY1B-OR YORWTy1-2 POL YOR142W-B O3367 YOR3367W] Transposon Ty1-OR Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
[Rps6ka3 Mapkapk1b Rps6ka-rs1 Rsk2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[Rps6ka1 Mapkapk1a Rsk1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[hsp90a.1 hsp90 hsp90a hsp90aa1 zgc:86652] Heat shock protein HSP 90-alpha 1
[Sparc] SPARC (Basement-membrane protein 40) (BM-40) (Osteonectin) (ON) (Secreted protein acidic and rich in cysteine)
[T 90C4.150 NCU00776] Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase)
[HSPG2] Basement membrane-specific heparan sulfate proteoglycan core protein (HSPG) (Perlecan) (PLC) [Cleaved into: Endorepellin; LG3 peptide]
[HSP90AB1 HSP90B HSPC2 HSPCB] Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[ospF mkaD CP0010 pWR501_0013 SFLP011] Phosphothreonine lyase OspF (EC 4.2.3.-) (Effector protein OspF)
[RPS6KA2 MAPKAPK1C RSK3] Ribosomal protein S6 kinase alpha-2 (S6K-alpha-2) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 2) (p90-RSK 2) (p90RSK2) (MAP kinase-activated protein kinase 1c) (MAPK-activated protein kinase 1c) (MAPKAP kinase 1c) (MAPKAPK-1c) (Ribosomal S6 kinase 3) (RSK-3) (pp90RSK3)
[RPS6KA3 ISPK1 MAPKAPK1B RSK2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[HSP90-7 SHD At4g24190 T19F6.1 T22A6.20] Endoplasmin homolog (Glucose-regulated protein 94 homolog) (GRP-94 homolog) (Heat shock protein 90-7) (AtHSP90.7) (AtHsp90-7) (Protein SHEPHERD)
[CYP90D1 At3g13730 MMM17.15] 3-epi-6-deoxocathasterone 23-monooxygenase CYP90D1 (EC 1.14.14.147) (Cytochrome P450 90D1)
[B4GALT1 GALT GGTB2] Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1]

Bibliography :
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