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Q9CZQ9 (BBS5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bardet-Biedl syndrome 5 protein homolog
Gene names
Name:Bbs5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for BBSome complex ciliary localization but not for the proper complex assembly By similarity.

Subunit structure

PPart of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Binds to phosphoinositides. Interacts with CCDC28B. Interacts with SMO; the interaction is indicative for the association of SMO with the BBsome complex to facilitate ciliary localization of SMO. Ref.5

Subcellular location

Cell projectioncilium membrane By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletoncilium basal body. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite By similarity. Note: Localizes to basal bodies. Ref.4

Sequence similarities

Belongs to the BBS5 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Bardet-Biedl syndrome 5 protein homolog
PRO_0000223256

Sequences

Sequence LengthMass (Da)Tools
Q9CZQ9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8FD2BF5943F72325

FASTA34138,862
        10         20         30         40         50         60 
MSVLDVLWED RDVRFDVSSQ QMKTRPGEVL IDCLDSIEDT KGNNGDRGRL LVTNLRIIWH 

        70         80         90        100        110        120 
SLALPRVNLS IGYNCILNIT TRTANSKLRG QTEALYILTK CNTTRFEFIF TNLVPGSPRL 

       130        140        150        160        170        180 
FTSVIAVHRA YETSKMYRDF KLRSAVIQNK QLRLLPQEHV YDKINGVWNL SSDQGNLGTF 

       190        200        210        220        230        240 
FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV 

       250        260        270        280        290        300 
EKLQESVKEI NSLHKVYSAS PIFGVNYEME EKPQPLEALT VEQIQDDVEI DSDDHTDAFV 

       310        320        330        340 
AYFADGNKQQ DREPVFSEEL GLAIEKLKDG FTLQGLWEVM S 

« Hide

References

« Hide 'large scale' references
[1]"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: Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Tissue: Testis.
[4]"Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene."
Li J.B., Gerdes J.M., Haycraft C.J., Fan Y., Teslovich T.M., May-Simera H., Li H., Blacque O.E., Li L., Leitch C.C., Lewis R.A., Green J.S., Parfrey P.S., Leroux M.R., Davidson W.S., Beales P.L., Guay-Woodford L.M., Yoder B.K. expand/collapse author list , Stormo G.D., Katsanis N., Dutcher S.K.
Cell 117:541-552(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened."
Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., Sheffield V.C.
PLoS Genet. 7:E1002358-E1002358(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BBSOME COMPLEX, INTERACTION WITH SMO.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK012283 mRNA. Translation: BAB28141.1.
AL929083 Genomic DNA. Translation: CAM24291.1.
BC061031 mRNA. Translation: AAH61031.1.
CCDSCCDS16094.1.
RefSeqNP_082560.1. NM_028284.2.
UniGeneMm.252136.

3D structure databases

ProteinModelPortalQ9CZQ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9CZQ9. 4 interactions.
STRING10090.ENSMUSP00000074494.

PTM databases

PhosphoSiteQ9CZQ9.

Proteomic databases

PaxDbQ9CZQ9.
PRIDEQ9CZQ9.

Protocols and materials databases

DNASU72569.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074963; ENSMUSP00000074494; ENSMUSG00000063145.
GeneID72569.
KEGGmmu:72569.
UCSCuc008jyf.1. mouse.

Organism-specific databases

CTD129880.
MGIMGI:1919819. Bbs5.

Phylogenomic databases

eggNOGNOG82102.
GeneTreeENSGT00390000002753.
HOGENOMHOG000231964.
HOVERGENHBG053449.
InParanoidA2AUC7.
KOK16748.
OMAELGFAME.
PhylomeDBQ9CZQ9.
TreeFamTF106129.

Gene expression databases

BgeeQ9CZQ9.
CleanExMM_BBS5.
GenevestigatorQ9CZQ9.

Family and domain databases

InterProIPR006606. BBL5.
[Graphical view]
PANTHERPTHR21351. PTHR21351. 1 hit.
PfamPF07289. DUF1448. 1 hit.
[Graphical view]
PIRSFPIRSF010072. DUF1448. 1 hit.
ProtoNetSearch...

Other

NextBio336521.
PROQ9CZQ9.
SOURCESearch...

Entry information

Entry nameBBS5_MOUSE
AccessionPrimary (citable) accession number: Q9CZQ9
Secondary accession number(s): A2AUC7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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