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Q9WVH9 (FBLN5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:Fbln5
Synonyms:Dance
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the fibulin family.

Contains 6 EGF-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 448425Fibulin-5
PRO_0000007578

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

Sequences

Sequence LengthMass (Da)Tools
Q9WVH9 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F15CC70CCFBFDC97

FASTA44850,193
        10         20         30         40         50         60 
MPGLKRILTV TILALWLPHP GNAQQQCTNG FDLDRQSGQC LDIDECRTIP EACRGDMMCV 

        70         80         90        100        110        120 
NQNGGYLCIP RTNPVYRGPY SNPYSTSYSG PYPAAAPPVP ASNYPTISRP LVCRFGYQMD 

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

       190        200        210        220        230        240 
CANVPGSYSC TCNPGFTLND DGRSCQDVNE CETENPCVQT CVNTYGSFIC RCDPGYELEE 

       250        260        270        280        290        300 
DGIHCSDMDE CSFSEFLCQH ECVNQPGSYF CSCPPGYVLL DDNRSCQDIN ECEHRNHTCT 

       310        320        330        340        350        360 
SLQTCYNLQG GFKCIDPISC EEPYLLIGEN RCMCPAEHTS CRDQPFTILY RDMDVVSGRS 

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

       430        440 
EMITVNTVIN FRGSSVIRLR IYVSQYPF

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye and Lung.
[3]"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].
Strain: C57BL/6J.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF112151 mRNA. Translation: AAD41767.1.
AK085170 mRNA. Translation: BAC39381.1.
AK090129 mRNA. Translation: BAC41109.1.
AK159471 mRNA. Translation: BAE35112.1.
AK159960 mRNA. Translation: BAE35515.1.
AK165018 mRNA. Translation: BAE38002.1.
BC006636 mRNA. Translation: AAH06636.1.
IPIIPI00323035.
RefSeqNP_035942.1. NM_011812.4.
UniGeneMm.288381.
Mm.465863.

3D structure databases

ProteinModelPortalQ9WVH9.
SMRQ9WVH9. Positions 42-326.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4094993.

Proteomic databases

PaxDbQ9WVH9.
PRIDEQ9WVH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021603; ENSMUSP00000021603; ENSMUSG00000021186.
GeneID23876.
KEGGmmu:23876.
UCSCuc007otp.1. mouse.

Organism-specific databases

CTD10516.
MGIMGI:1346091. Fbln5.

Phylogenomic databases

eggNOGNOG309650.
GeneTreeENSGT00700000104291.
HOGENOMHOG000234337.
HOVERGENHBG051560.
InParanoidQ9WVH9.
OMAIKGPRDI.
OrthoDBEOG4W6NVQ.

Gene expression databases

BgeeQ9WVH9.
CleanExMM_FBLN5.
GenevestigatorQ9WVH9.
GermOnlineENSMUSG00000021186. Mus musculus.

Family and domain databases

InterProIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
[Graphical view]
PfamPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view]
SMARTSM00179. EGF_CA. 4 hits.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBLN5. mouse.
NextBio303595.
SOURCESearch...

Entry information

Entry nameFBLN5_MOUSE
AccessionPrimary (citable) accession number: Q9WVH9
Secondary accession number(s): Q541Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents