Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UBX5 (FBLN5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibulin-5

Short name=FIBL-5
Alternative name(s):
Developmental arteries and neural crest EGF-like protein
Short name=Dance
Urine p50 protein
Short name=UP50
Gene names
Name:FBLN5
Synonyms:DANCE
ORF Names:UNQ184/PRO210
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Could be a vascular ligand for integrin receptors and may play a role in vascular development and remodeling.

Subunit structure

Homodimer. Ref.9

Subcellular location

Secreted.

Tissue specificity

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.13

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the fibulin family.

Contains 6 EGF-like domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentSecreted
   DiseaseAge-related macular degeneration
Disease mutation
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-matrix adhesion

Traceable author statement Ref.2. Source: ProtInc

elastic fiber assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

protein localization to cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

regulation of removal of superoxide radicals

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentelastic fiber

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

proteinaceous extracellular matrix

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

integrin binding

Traceable author statement Ref.2. Source: ProtInc

protein C-terminus binding

Inferred from physical interaction PubMed 15528465. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 17581631PubMed 19570982. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 448425Fibulin-5
PRO_0000007577

Regions

Domain42 – 8241EGF-like 1; calcium-binding Potential
Domain127 – 16741EGF-like 2; calcium-binding Potential
Domain168 – 20639EGF-like 3; calcium-binding Potential
Domain207 – 24640EGF-like 4; calcium-binding Potential
Domain247 – 28741EGF-like 5; calcium-binding Potential
Domain288 – 33346EGF-like 6; calcium-binding Potential
Motif54 – 563Cell attachment site Potential

Amino acid modifications

Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 59 By similarity
Disulfide bond53 ↔ 68 By similarity
Disulfide bond131 ↔ 144 By similarity
Disulfide bond138 ↔ 153 By similarity
Disulfide bond155 ↔ 166 By similarity
Disulfide bond172 ↔ 181 By similarity
Disulfide bond177 ↔ 190 By similarity
Disulfide bond192 ↔ 205 By similarity
Disulfide bond211 ↔ 221 By similarity
Disulfide bond217 ↔ 230 By similarity
Disulfide bond232 ↔ 245 By similarity
Disulfide bond251 ↔ 262 By similarity
Disulfide bond258 ↔ 271 By similarity
Disulfide bond273 ↔ 286 By similarity
Disulfide bond292 ↔ 305 By similarity
Disulfide bond299 ↔ 314 By similarity
Disulfide bond320 ↔ 332 By similarity

Natural variations

Natural variant601V → L in ARMD3. Ref.12
Corresponds to variant rs28939371 [ dbSNP | Ensembl ].
VAR_019814
Natural variant711R → Q in ARMD3. Ref.12
Corresponds to variant rs28939372 [ dbSNP | Ensembl ].
VAR_019815
Natural variant871P → S in ARMD3. Ref.12
Corresponds to variant rs28939373 [ dbSNP | Ensembl ].
VAR_019816
Natural variant1691I → T in ARMD3. Ref.12
Corresponds to variant rs28939072 [ dbSNP | Ensembl ].
VAR_019817
Natural variant2271S → P in ARCL1A. Ref.10 Ref.13
Corresponds to variant rs28939370 [ dbSNP | Ensembl ].
VAR_017153
Natural variant3511R → W in ARMD3. Ref.12
Corresponds to variant rs28939073 [ dbSNP | Ensembl ].
VAR_019818
Natural variant3631A → T in ARMD3. Ref.12
VAR_019819
Natural variant3641D → Y.
Corresponds to variant rs1802492 [ dbSNP | Ensembl ].
VAR_026986
Natural variant4121G → E in ARMD3. Ref.12
VAR_019820

Experimental info

Sequence conflict69 – 702IP → HS in AAC62107. Ref.3
Sequence conflict147 – 1482TE → MK in AAC62107. Ref.3
Sequence conflict2281F → L in AAQ89257. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9UBX5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 19FCA51FDA328003

FASTA44850,180
        10         20         30         40         50         60 
MPGIKRILTV TILALCLPSP GNAQAQCTNG FDLDRQSGQC LDIDECRTIP EACRGDMMCV 

        70         80         90        100        110        120 
NQNGGYLCIP RTNPVYRGPY SNPYSTPYSG PYPAAAPPLS APNYPTISRP LICRFGYQMD 

       130        140        150        160        170        180 
ESNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL 

       190        200        210        220        230        240 
CANVPGSYSC TCNPGFTLNE DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELEE 

       250        260        270        280        290        300 
DGVHCSDMDE CSFSEFLCQH ECVNQPGTYF CSCPPGYILL DDNRSCQDIN ECEHRNHTCN 

       310        320        330        340        350        360 
LQQTCYNLQG GFKCIDPIRC EEPYLRISDN RCMCPAENPG CRDQPFTILY RDMDVVSGRS 

       370        380        390        400        410        420 
VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPREIQLDL 

       430        440 
EMITVNTVIN FRGSSVIRLR IYVSQYPF 

« Hide

References

« Hide 'large scale' references
[1]Kostka G.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Melanoma.
[2]"DANCE, a novel secreted RGD protein expressed in developing, atherosclerotic, and balloon-injured arteries."
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.
J. Biol. Chem. 274:22476-22483(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Zemel R., Sholto O., Shaul Y.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Urine.
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
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. expand/collapse author list , 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.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
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. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[9]"Fibulin 5 forms a compact dimer in physiological solutions."
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.
J. Biol. Chem. 284:25938-25943(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[10]"Homozygosity for a missense mutation in fibulin-5 (FBLN5) results in a severe form of cutis laxa."
Loeys B., van Maldergem L., Mortier G., Coucke P., Gerniers S., Naeyaert J.-M., de Paepe A.
Hum. Mol. Genet. 11:2113-2118(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCL1A PRO-227.
[11]"Genetic heterogeneity of cutis laxa: a heterozygous tandem duplication within the fibulin-5 (FBLN5) gene."
Markova D., Zou Y., Ringpfeil F., Sasaki T., Kostka G., Timpl R., Uitto J., Chu M.-L.
Am. J. Hum. Genet. 72:998-1004(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ADCL2.
[12]"Missense variations in the fibulin 5 gene and age-related macular degeneration."
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.
N. Engl. J. Med. 351:346-353(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARMD3 LEU-60; GLN-71; SER-87; THR-169; TRP-351; THR-363 AND GLU-412.
[13]"Homozygous missense mutation in fibulin-5 in an Iranian autosomal recessive cutis laxa pedigree and associated haplotype."
Elahi E., Kalhor R., Banihosseini S.S., Torabi N., Pour-Jafari H., Houshmand M., Amini S.S.H., Ramezani A., Loeys B.
J. Invest. Dermatol. 126:1506-1509(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCL1A PRO-227.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ133490 mRNA. Translation: CAB38568.1.
AF112152 mRNA. Translation: AAD41768.1.
AF093118 mRNA. Translation: AAC62107.1.
AY358898 mRNA. Translation: AAQ89257.1.
CR457140 mRNA. Translation: CAG33421.1.
AK075147 mRNA. Translation: BAG52073.1.
CH471061 Genomic DNA. Translation: EAW81466.1.
BC022280 mRNA. Translation: AAH22280.1.
CCDSCCDS9898.1.
RefSeqNP_006320.2. NM_006329.3.
UniGeneHs.332708.

3D structure databases

ProteinModelPortalQ9UBX5.
SMRQ9UBX5. Positions 21-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115771. 7 interactions.
IntActQ9UBX5. 16 interactions.
MINTMINT-2868380.
STRING9606.ENSP00000345008.

Polymorphism databases

DMDM12643876.

2D gel databases

REPRODUCTION-2DPAGEIPI00294615.

Proteomic databases

PaxDbQ9UBX5.
PeptideAtlasQ9UBX5.
PRIDEQ9UBX5.

Protocols and materials databases

DNASU10516.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342058; ENSP00000345008; ENSG00000140092.
GeneID10516.
KEGGhsa:10516.
UCSCuc001xzx.4. human.

Organism-specific databases

CTD10516.
GeneCardsGC14M092335.
GeneReviewsFBLN5.
HGNCHGNC:3602. FBLN5.
HPACAB025843.
HPA000848.
HPA000868.
MIM219100. phenotype.
604580. gene.
608895. phenotype.
614434. phenotype.
neXtProtNX_Q9UBX5.
Orphanet279. Age-related macular degeneration.
90348. Autosomal dominant cutis laxa.
90349. Autosomal recessive cutis laxa type 1.
280598. Hereditary sensorimotor neuropathy with hyperelastic skin.
PharmGKBPA28015.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309650.
HOGENOMHOG000234337.
HOVERGENHBG051560.
KOK17340.
PhylomeDBQ9UBX5.
TreeFamTF317514.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9UBX5.
BgeeQ9UBX5.
CleanExHS_FBLN5.
GenevestigatorQ9UBX5.

Family and domain databases

InterProIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTSM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 3 hits.
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFBLN5.
GenomeRNAi10516.
NextBio39880.
PROQ9UBX5.
SOURCESearch...

Entry information

Entry nameFBLN5_HUMAN
AccessionPrimary (citable) accession number: Q9UBX5
Secondary accession number(s): O75966, Q6IAL4, Q6UWA3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM