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Fibulin-5 (FIBL-5) (Developmental arteries and neural crest EGF-like protein) (Dance) (Urine p50 protein) (UP50)

 FBLN5_HUMAN             Reviewed;         448 AA.
Q9UBX5; O75966; Q6IAL4; Q6UWA3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-DEC-2017, entry version 172.
RecName: Full=Fibulin-5;
Short=FIBL-5;
AltName: Full=Developmental arteries and neural crest EGF-like protein;
Short=Dance;
AltName: Full=Urine p50 protein;
Short=UP50;
Flags: Precursor;
Name=FBLN5; Synonyms=DANCE; ORFNames=UNQ184/PRO210;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Melanoma;
Kostka G.;
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10428823; DOI=10.1074/jbc.274.32.22476;
Nakamura T., Ruiz-Lozano P., Lindner V., Yabe D., Taniwaki M.,
Furukawa Y., Kobuke K., Tashiro K., Lu Z., Andon N.L., Schaub R.,
Matsumori A., Sasayama S., Chien K.R., Honjo T.;
"DANCE, a novel secreted RGD protein expressed in developing,
atherosclerotic, and balloon-injured arteries.";
J. Biol. Chem. 274:22476-22483(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Urine;
Zemel R., Sholto O., Shaul Y.;
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[9]
INTERACTION WITH FBN1 AND ELN, SUBUNIT, AND GLYCOSYLATION.
PubMed=15790312; DOI=10.1042/BJ20050368;
Freeman L.J., Lomas A., Hodson N., Sherratt M.J., Mellody K.T.,
Weiss A.S., Shuttleworth A., Kielty C.M.;
"Fibulin-5 interacts with fibrillin-1 molecules and microfibrils.";
Biochem. J. 388:1-5(2005).
[10]
FUNCTION, AND INTERACTION WITH FBN1 AND ELN.
PubMed=17255108; DOI=10.1074/jbc.M608204200;
El-Hallous E., Sasaki T., Hubmacher D., Getie M., Tiedemann K.,
Brinckmann J., Baetge B., Davis E.C., Reinhardt D.P.;
"Fibrillin-1 interactions with fibulins depend on the first hybrid
domain and provide an adaptor function to tropoelastin.";
J. Biol. Chem. 282:8935-8946(2007).
[11]
SUBUNIT, AND GLYCOSYLATION.
PubMed=19617354; DOI=10.1074/jbc.M109.011627;
Jones R.P., Wang M.C., Jowitt T.A., Ridley C., Mellody K.T.,
Howard M., Wang T., Bishop P.N., Lotery A.J., Kielty C.M., Baldock C.,
Trump D.;
"Fibulin 5 forms a compact dimer in physiological solutions.";
J. Biol. Chem. 284:25938-25943(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
VARIANT ARCL1A PRO-227.
PubMed=12189163; DOI=10.1093/hmg/11.18.2113;
Loeys B., van Maldergem L., Mortier G., Coucke P., Gerniers S.,
Naeyaert J.-M., de Paepe A.;
"Homozygosity for a missense mutation in fibulin-5 (FBLN5) results in
a severe form of cutis laxa.";
Hum. Mol. Genet. 11:2113-2118(2002).
[14]
INVOLVEMENT IN ADCL2.
PubMed=12618961; DOI=10.1086/373940;
Markova D., Zou Y., Ringpfeil F., Sasaki T., Kostka G., Timpl R.,
Uitto J., Chu M.-L.;
"Genetic heterogeneity of cutis laxa: a heterozygous tandem
duplication within the fibulin-5 (FBLN5) gene.";
Am. J. Hum. Genet. 72:998-1004(2003).
[15]
VARIANTS ARMD3 LEU-60; GLN-71; SER-87; THR-169; TRP-351; THR-363 AND
GLU-412.
PubMed=15269314; DOI=10.1056/NEJMoa040833;
Stone E.M., Braun T.A., Russell S.R., Kuehn M.H., Lotery A.J.,
Moore P.A., Eastman C.G., Casavant T.L., Sheffield V.C.;
"Missense variations in the fibulin 5 gene and age-related macular
degeneration.";
N. Engl. J. Med. 351:346-353(2004).
[16]
VARIANTS ARCL1A ARG-217 AND PRO-227, CHARACTERIZATION OF VARIANTS
ARCL1A ARG-217 AND PRO-227, FUNCTION, INTERACTION WITH ELN,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17035250; DOI=10.1093/hmg/ddl414;
Hu Q., Loeys B.L., Coucke P.J., De Paepe A., Mecham R.P., Choi J.,
Davis E.C., Urban Z.;
"Fibulin-5 mutations: mechanisms of impaired elastic fiber formation
in recessive cutis laxa.";
Hum. Mol. Genet. 15:3379-3386(2006).
[17]
VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267;
TRP-351; THR-363 AND GLU-412, CHARACTERIZATION OF VARIANTS ARMD3
LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267; TRP-351; THR-363
AND GLU-412, VARIANTS ARCL1A ARG-217 AND PRO-227, CHARACTERIZATION OF
VARIANTS ARCL1A ARG-217 AND PRO-227, VARIANTS MET-126 AND ARG-202, AND
SUBCELLULAR LOCATION.
PubMed=16652333; DOI=10.1002/humu.20344;
Lotery A.J., Baas D., Ridley C., Jones R.P., Klaver C.C., Stone E.,
Nakamura T., Luff A., Griffiths H., Wang T., Bergen A.A., Trump D.;
"Reduced secretion of fibulin 5 in age-related macular degeneration
and cutis laxa.";
Hum. Mutat. 27:568-574(2006).
[18]
VARIANT ARCL1A PRO-227.
PubMed=16691202; DOI=10.1038/sj.jid.5700247;
Elahi E., Kalhor R., Banihosseini S.S., Torabi N., Pour-Jafari H.,
Houshmand M., Amini S.S.H., Ramezani A., Loeys B.;
"Homozygous missense mutation in fibulin-5 in an Iranian autosomal
recessive cutis laxa pedigree and associated haplotype.";
J. Invest. Dermatol. 126:1506-1509(2006).
[19]
VARIANT ARCL1A ARG-217, CHARACTERIZATION OF VARIANT ARCL1A ARG-217,
AND FUNCTION.
PubMed=18185537; DOI=10.1038/sj.jid.5701211;
Claus S., Fischer J., Megarbane H., Megarbane A., Jobard F.,
Debret R., Peyrol S., Saker S., Devillers M., Sommer P., Damour O.;
"A p.C217R mutation in fibulin-5 from cutis laxa patients is
associated with incomplete extracellular matrix formation in a skin
equivalent model.";
J. Invest. Dermatol. 128:1442-1450(2008).
[20]
VARIANT MET-301.
PubMed=19194475; DOI=10.1038/jid.2008.450;
Megarbane H., Florence J., Sass J.O., Schwonbeck S., Foglio M.,
de Cid R., Cure S., Saker S., Megarbane A., Fischer J.;
"An autosomal-recessive form of cutis laxa is due to homozygous
elastin mutations, and the phenotype may be modified by a heterozygous
fibulin 5 polymorphism.";
J. Invest. Dermatol. 129:1650-1655(2009).
[21]
CHARACTERIZATION OF VARIANTS MET-126 AND ARG-202, CHARACTERIZATION OF
VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267;
TRP-351 AND GLU-412, CHARACTERIZATION OF VARIANTS ARCL1A ARG-217 AND
PRO-227, AND SUBUNIT.
PubMed=20007835; DOI=10.1167/iovs.09-4620;
Jones R.P., Ridley C., Jowitt T.A., Wang M.C., Howard M., Bobola N.,
Wang T., Bishop P.N., Kielty C.M., Baldock C., Lotery A.J., Trump D.;
"Structural effects of fibulin 5 missense mutations associated with
age-related macular degeneration and cutis laxa.";
Invest. Ophthalmol. Vis. Sci. 51:2356-2362(2010).
[22]
CHARACTERIZATION OF VARIANTS ARCL1A PRO-227 AND SER-267,
CHARACTERIZATION OF VARIANT ARMD3 THR-169, CHARACTERIZATION OF VARIANT
ARG-202, AND SUBCELLULAR LOCATION.
PubMed=20599547; DOI=10.1016/j.jmb.2010.06.039;
Schneider R., Jensen S.A., Whiteman P., McCullagh J.S., Redfield C.,
Handford P.A.;
"Biophysical characterisation of fibulin-5 proteins associated with
disease.";
J. Mol. Biol. 401:605-617(2010).
[23]
VARIANTS HNARMD ILE-48; SER-90; SER-267 AND CYS-373, AND VARIANT
MET-126.
PubMed=21576112; DOI=10.1093/brain/awr076;
Auer-Grumbach M., Weger M., Fink-Puches R., Papic L., Froehlich E.,
Auer-Grumbach P., El Shabrawi-Caelen L., Schabhuettl M.,
Windpassinger C., Senderek J., Budka H., Trajanoski S., Janecke A.R.,
Haas A., Metze D., Pieber T.R., Guelly C.;
"Fibulin-5 mutations link inherited neuropathies, age-related macular
degeneration and hyperelastic skin.";
Brain 134:1839-1852(2011).
[24]
VARIANT HNARMD CYS-373.
PubMed=23328402; DOI=10.1093/brain/aws333;
Safka Brozkova D., Lassuthova P., Neupauerova J., Krutova M.,
Haberlova J., Stejskal D., Seeman P.;
"Czech family confirms the link between FBLN5 and Charcot-Marie-Tooth
type 1 neuropathy.";
Brain 136:E232-E232(2013).
-!- FUNCTION: Essential for elastic fiber formation, is involved in
the assembly of continuous elastin (ELN) polymer and promotes the
interaction of microfibrils and ELN (PubMed:18185537). Stabilizes
and organizes elastic fibers in the skin, lung and vasculature (By
similarity). Promotes adhesion of endothelial cells through
interaction of integrins and the RGD motif. Vascular ligand for
integrin receptors which may play a role in vascular development
and remodeling (PubMed:10428823). May act as an adapter that
mediates the interaction between FBN1 and ELN (PubMed:17255108).
{ECO:0000250|UniProtKB:Q9WVH9, ECO:0000269|PubMed:10428823,
ECO:0000269|PubMed:17255108, ECO:0000269|PubMed:18185537}.
-!- SUBUNIT: Homodimer (PubMed:20007835). Monomer (PubMed:15790312,
PubMed:19617354), homodimerizes in presence of Ca(2+)
(PubMed:19617354). Interacts with ELN (PubMed:17035250,
PubMed:15790312). Interacts (via N-terminus) with the integrins
ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1 (By similarity).
Interacts with FBN1 (via N-terminal domain). Forms a ternary
complex with ELN and FBN1 (PubMed:17255108).
{ECO:0000250|UniProtKB:Q9WVH9, ECO:0000269|PubMed:15790312,
ECO:0000269|PubMed:17035250, ECO:0000269|PubMed:17255108,
ECO:0000269|PubMed:19617354, ECO:0000269|PubMed:20007835}.
-!- INTERACTION:
O95967:EFEMP2; NbExp=3; IntAct=EBI-947897, EBI-743414;
P15502:ELN; NbExp=3; IntAct=EBI-947897, EBI-1222108;
P35555:FBN1; NbExp=3; IntAct=EBI-947897, EBI-2505934;
P28300:LOX; NbExp=2; IntAct=EBI-947897, EBI-3893481;
Q14767:LTBP2; NbExp=2; IntAct=EBI-947897, EBI-1546118;
P50222:MEOX2; NbExp=3; IntAct=EBI-947897, EBI-748397;
P32242:OTX1; NbExp=3; IntAct=EBI-947897, EBI-740446;
Q15645:TRIP13; NbExp=3; IntAct=EBI-947897, EBI-358993;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:17035250, ECO:0000269|PubMed:20599547}.
Secreted, extracellular space, extracellular matrix
{ECO:0000269|PubMed:17035250}. Note=co-localizes with ELN in
elastic fibers. {ECO:0000269|PubMed:17035250}.
-!- TISSUE SPECIFICITY: Expressed in skin fibroblasts (at protein
level)(PubMed:17035250). Expressed predominantly in heart, ovary,
and colon but also in kidney, pancreas, testis, lung and placenta.
Not detectable in brain, liver, thymus, prostate, or peripheral
blood leukocytes (PubMed:10428823). {ECO:0000269|PubMed:10428823,
ECO:0000269|PubMed:17035250}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15790312,
ECO:0000269|PubMed:19617354}.
-!- DISEASE: Neuropathy, hereditary, with or without age-related
macular degeneration (HNARMD) [MIM:608895]: An autosomal dominant
neuropathy of the Charcot-Marie-Tooth disease group, characterized
by distal muscle weakness and atrophy variably affecting the lower
and upper limbs. Distal sensory impairment and decreased nerve
conduction velocities are present in most but not all patients.
Additional variable features are age-related macular degeneration,
joint hypermobility, and hyperelastic skin.
{ECO:0000269|PubMed:21576112, ECO:0000269|PubMed:23328402}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Cutis laxa, autosomal dominant, 2 (ADCL2) [MIM:614434]: A
connective tissue disorder characterized by loose, hyperextensible
skin with decreased resilience and elasticity leading to a
premature aged appearance. Face, hands, feet, joints, and torso
may be differentially affected. Additional variable clinical
features are gastrointestinal diverticula, hernia, and genital
prolapse. Rare manifestations are pulmonary artery stenosis,
aortic aneurysm, bronchiectasis, and emphysema.
{ECO:0000269|PubMed:12618961}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cutis laxa, autosomal recessive, 1A (ARCL1A)
[MIM:219100]: A connective tissue disorder characterized by loose,
hyperextensible skin with decreased resilience and elasticity
leading to a premature aged appearance. Face, hands, feet, joints,
and torso may be differentially affected. The clinical spectrum of
autosomal recessive cutis laxa is highly heterogeneous with
respect to organ involvement and severity. Type I autosomal
recessive cutis laxa is a specific, life-threatening disorder with
organ involvement, lung atelectasis and emphysema, diverticula of
the gastrointestinal and genitourinary systems, and vascular
anomalies. Associated cranial anomalies, late closure of the
fontanel, joint laxity, hip dislocation, and inguinal hernia have
been observed but are uncommon. {ECO:0000269|PubMed:12189163,
ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:16691202,
ECO:0000269|PubMed:17035250, ECO:0000269|PubMed:18185537,
ECO:0000269|PubMed:20007835, ECO:0000269|PubMed:20599547}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. Mutations affecting this gene can
modify the phenotype of diseases caused by ELN mutations.
{ECO:0000269|PubMed:19194475}.
-!- DISEASE: Macular degeneration, age-related, 3 (ARMD3)
[MIM:608895]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:20007835,
ECO:0000269|PubMed:20599547}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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EMBL; AJ133490; CAB38568.1; -; mRNA.
EMBL; AF112152; AAD41768.1; -; mRNA.
EMBL; AF093118; AAC62107.1; -; mRNA.
EMBL; AY358898; AAQ89257.1; -; mRNA.
EMBL; CR457140; CAG33421.1; -; mRNA.
EMBL; AK075147; BAG52073.1; -; mRNA.
EMBL; CH471061; EAW81466.1; -; Genomic_DNA.
EMBL; BC022280; AAH22280.1; -; mRNA.
CCDS; CCDS9898.1; -.
RefSeq; NP_006320.2; NM_006329.3.
UniGene; Hs.332708; -.
ProteinModelPortal; Q9UBX5; -.
SMR; Q9UBX5; -.
BioGrid; 115771; 16.
DIP; DIP-44301N; -.
IntAct; Q9UBX5; 22.
MINT; MINT-2868380; -.
STRING; 9606.ENSP00000345008; -.
iPTMnet; Q9UBX5; -.
PhosphoSitePlus; Q9UBX5; -.
BioMuta; FBLN5; -.
DMDM; 12643876; -.
REPRODUCTION-2DPAGE; IPI00294615; -.
PaxDb; Q9UBX5; -.
PeptideAtlas; Q9UBX5; -.
PRIDE; Q9UBX5; -.
DNASU; 10516; -.
Ensembl; ENST00000342058; ENSP00000345008; ENSG00000140092.
GeneID; 10516; -.
KEGG; hsa:10516; -.
UCSC; uc001xzx.5; human.
CTD; 10516; -.
DisGeNET; 10516; -.
EuPathDB; HostDB:ENSG00000140092.14; -.
GeneCards; FBLN5; -.
GeneReviews; FBLN5; -.
HGNC; HGNC:3602; FBLN5.
HPA; CAB025843; -.
HPA; HPA000848; -.
HPA; HPA000868; -.
MalaCards; FBLN5; -.
MIM; 219100; phenotype.
MIM; 604580; gene.
MIM; 608895; phenotype.
MIM; 614434; phenotype.
neXtProt; NX_Q9UBX5; -.
OpenTargets; ENSG00000140092; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 90348; Autosomal dominant cutis laxa.
Orphanet; 90349; Autosomal recessive cutis laxa type 1.
Orphanet; 280598; Hereditary sensorimotor neuropathy with hyperelastic skin.
PharmGKB; PA28015; -.
eggNOG; ENOG410IR76; Eukaryota.
eggNOG; ENOG41104WD; LUCA.
GeneTree; ENSGT00760000118806; -.
HOGENOM; HOG000234337; -.
HOVERGEN; HBG051560; -.
InParanoid; Q9UBX5; -.
KO; K17340; -.
PhylomeDB; Q9UBX5; -.
TreeFam; TF317514; -.
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
SIGNOR; Q9UBX5; -.
GeneWiki; FBLN5; -.
GenomeRNAi; 10516; -.
PRO; PR:Q9UBX5; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000140092; -.
CleanEx; HS_FBLN5; -.
ExpressionAtlas; Q9UBX5; baseline and differential.
Genevisible; Q9UBX5; HS.
GO; GO:0071953; C:elastic fiber; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:ProtInc.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
GO; GO:0048251; P:elastic fiber assembly; IMP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:2000121; P:regulation of removal of superoxide radicals; ISS:BHF-UCL.
GO; GO:0046903; P:secretion; IDA:UniProtKB.
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; IPR037288; Fibulin-5.
InterPro; IPR037287; Fibulin_3/4/5.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
PANTHER; PTHR44074; PTHR44074; 1.
PANTHER; PTHR44074:SF4; PTHR44074:SF4; 1.
Pfam; PF12662; cEGF; 3.
Pfam; PF07645; EGF_CA; 2.
SMART; SM00181; EGF; 5.
SMART; SM00179; EGF_CA; 6.
SUPFAM; SSF57184; SSF57184; 3.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS50026; EGF_3; 5.
PROSITE; PS01187; EGF_CA; 6.
1: Evidence at protein level;
Age-related macular degeneration; Calcium; Cell adhesion;
Charcot-Marie-Tooth disease; Complete proteome; Disease mutation;
Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
Neuropathy; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 448 Fibulin-5.
/FTId=PRO_0000007577.
DOMAIN 42 82 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 127 167 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 168 206 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 207 246 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 247 287 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 288 333 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
MOTIF 54 56 Cell attachment site. {ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 59 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 53 68 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 131 144 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 138 153 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 155 166 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 172 181 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 177 190 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 192 205 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 211 221 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 217 230 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 232 245 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 251 262 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 258 271 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 273 286 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 292 305 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 299 314 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 320 332 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VARIANT 48 48 T -> I (in HNARMD; dbSNP:rs141200859).
{ECO:0000269|PubMed:21576112}.
/FTId=VAR_076289.
VARIANT 60 60 V -> L (in ARMD3; no effect on secretion;
no effect on homodimerization;
dbSNP:rs121434299).
{ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835}.
/FTId=VAR_019814.
VARIANT 71 71 R -> Q (in ARMD3; no effect on secretion;
no effect on homodimerization;
dbSNP:rs121434300).
{ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835}.
/FTId=VAR_019815.
VARIANT 87 87 P -> S (in ARMD3; no effect on secretion;
slightly increases homodimerization in
absence of Ca(2+); dbSNP:rs121434301).
{ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835}.
/FTId=VAR_019816.
VARIANT 90 90 G -> S (in HNARMD; dbSNP:rs144288844).
{ECO:0000269|PubMed:21576112}.
/FTId=VAR_076290.
VARIANT 124 124 Q -> P (in ARMD3; almost abolishes
secretion; no effect on
homodimerization).
{ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835}.
/FTId=VAR_072389.
VARIANT 126 126 V -> M (polymorphism; no effect on
secretion; slightly increases
homodimerization in absence of Ca(2+);
dbSNP:rs61734479).
{ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835,
ECO:0000269|PubMed:21576112}.
/FTId=VAR_072390.
VARIANT 169 169 I -> T (in ARMD3; decreases secretion;
slightly increases homodimerization in
absence of Ca(2+); no effect on protein
folding; dbSNP:rs28939072).
{ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835,
ECO:0000269|PubMed:20599547}.
/FTId=VAR_019817.
VARIANT 202 202 G -> R (polymorphism; slightly increases
homodimerization in absence of Ca(2+); no
effect on protein folding; no effect on
secretion; dbSNP:rs80338765).
{ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835,
ECO:0000269|PubMed:20599547}.
/FTId=VAR_072391.
VARIANT 217 217 C -> R (in ARCL1A; formation of
extracellular globular aggregates;
decreases cell growth; reduces
interaction with ELN; abolishes
secretion; increases homodimerization;
dbSNP:rs80338766).
{ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:17035250,
ECO:0000269|PubMed:18185537,
ECO:0000269|PubMed:20007835}.
/FTId=VAR_072392.
VARIANT 227 227 S -> P (in ARCL1A; decreases expression;
produces protein misfolding; abolishes
secretion; reduces interaction with ELN;
increases homodimerization; impairs
elastic fiber development;
dbSNP:rs28939370).
{ECO:0000269|PubMed:12189163,
ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:16691202,
ECO:0000269|PubMed:17035250,
ECO:0000269|PubMed:20007835,
ECO:0000269|PubMed:20599547}.
/FTId=VAR_017153.
VARIANT 267 267 G -> S (in ARMD3, ARCL1A and HNARMD;
produces protein misolding; decreases
secretion; no effect on homodimerization;
dbSNP:rs149396611).
{ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835,
ECO:0000269|PubMed:20599547,
ECO:0000269|PubMed:21576112}.
/FTId=VAR_072393.
VARIANT 301 301 L -> M (found in a patient with autosomal
recessive cutis laxa also carrying a
mutation in ELN; unknown pathological
significance; dbSNP:rs377360782).
{ECO:0000269|PubMed:19194475}.
/FTId=VAR_072394.
VARIANT 351 351 R -> W (in ARMD3; no effect on secretion;
slightly increases homodimerization in
absence of Ca(2+); dbSNP:rs28939073).
{ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835}.
/FTId=VAR_019818.
VARIANT 363 363 A -> T (in ARMD3; no effect on secretion;
dbSNP:rs121434302).
{ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333}.
/FTId=VAR_019819.
VARIANT 364 364 D -> Y (in dbSNP:rs1802492).
/FTId=VAR_026986.
VARIANT 373 373 R -> C (in HNARMD; dbSNP:rs864309526).
{ECO:0000269|PubMed:21576112,
ECO:0000269|PubMed:23328402}.
/FTId=VAR_076291.
VARIANT 412 412 G -> E (in ARMD3; decreases secretion;
slightly increases homodimerization in
absence of Ca(2+); dbSNP:rs121434303).
{ECO:0000269|PubMed:15269314,
ECO:0000269|PubMed:16652333,
ECO:0000269|PubMed:20007835}.
/FTId=VAR_019820.
CONFLICT 69 70 IP -> HS (in Ref. 3; AAC62107).
{ECO:0000305}.
CONFLICT 147 148 TE -> MK (in Ref. 3; AAC62107).
{ECO:0000305}.
CONFLICT 228 228 F -> L (in Ref. 4; AAQ89257).
{ECO:0000305}.
SEQUENCE 448 AA; 50180 MW; 19FCA51FDA328003 CRC64;
MPGIKRILTV TILALCLPSP GNAQAQCTNG FDLDRQSGQC LDIDECRTIP EACRGDMMCV
NQNGGYLCIP RTNPVYRGPY SNPYSTPYSG PYPAAAPPLS APNYPTISRP LICRFGYQMD
ESNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL
CANVPGSYSC TCNPGFTLNE DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELEE
DGVHCSDMDE CSFSEFLCQH ECVNQPGTYF CSCPPGYILL DDNRSCQDIN ECEHRNHTCN
LQQTCYNLQG GFKCIDPIRC EEPYLRISDN RCMCPAENPG CRDQPFTILY RDMDVVSGRS
VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPREIQLDL
EMITVNTVIN FRGSSVIRLR IYVSQYPF


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