ID   BBS5_MOUSE              Reviewed;         341 AA.
AC   Q9CZQ9; A2AUC7;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Bardet-Biedl syndrome 5 protein homolog;
GN   Name=Bbs5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15137946; DOI=10.1016/s0092-8674(04)00450-7;
RA   Li J.B., Gerdes J.M., Haycraft C.J., Fan Y., Teslovich T.M., May-Simera H.,
RA   Li H., Blacque O.E., Li L., Leitch C.C., Lewis R.A., Green J.S.,
RA   Parfrey P.S., Leroux M.R., Davidson W.S., Beales P.L., Guay-Woodford L.M.,
RA   Yoder B.K., Stormo G.D., Katsanis N., Dutcher S.K.;
RT   "Comparative genomics identifies a flagellar and basal body proteome that
RT   includes the BBS5 human disease gene.";
RL   Cell 117:541-552(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   IDENTIFICATION IN THE BBSOME COMPLEX, AND INTERACTION WITH SMO.
RX   PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
RA   Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
RA   Sheffield V.C.;
RT   "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and
RT   Smoothened.";
RL   PLoS Genet. 7:E1002358-E1002358(2011).
CC   -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC       required for sorting of specific membrane proteins to the primary
CC       cilia. The BBSome complex is required for ciliogenesis but is
CC       dispensable for centriolar satellite function. This ciliogenic function
CC       is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC       localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC       the primary cilium and promotes extension of the ciliary membrane.
CC       Firstly the BBSome associates with the ciliary membrane and binds to
CC       RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC       Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC       carrier vesicles to the base of the ciliary membrane. The BBSome
CC       complex, together with the LTZL1, controls SMO ciliary trafficking and
CC       contributes to the sonic hedgehog (SHH) pathway regulation. Required
CC       for BBSome complex ciliary localization but not for the proper complex
CC       assembly (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: PPart of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC       BBS7, BBS8/TTC8, BBS9 and BBIP10. Binds to phosphoinositides. Interacts
CC       with CCDC28B. Interacts with SMO; the interaction is indicative for the
CC       association of SMO with the BBsome complex to facilitate ciliary
CC       localization of SMO. Interacts with PKD1 (By similarity). Interacts
CC       with DLEC1 (By similarity). {ECO:0000250|UniProtKB:Q8N3I7,
CC       ECO:0000269|PubMed:22072986}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}.
CC       Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000269|PubMed:15137946}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriolar satellite {ECO:0000250}.
CC       Note=Localizes to basal bodies.
CC   -!- SIMILARITY: Belongs to the BBS5 family. {ECO:0000305}.
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DR   EMBL; AK012283; BAB28141.1; -; mRNA.
DR   EMBL; AL929083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC061031; AAH61031.1; -; mRNA.
DR   CCDS; CCDS16094.1; -.
DR   RefSeq; NP_082560.1; NM_028284.2.
DR   AlphaFoldDB; Q9CZQ9; -.
DR   SMR; Q9CZQ9; -.
DR   BioGRID; 215445; 35.
DR   ComplexPortal; CPX-1909; BBSome complex.
DR   IntAct; Q9CZQ9; 7.
DR   MINT; Q9CZQ9; -.
DR   STRING; 10090.ENSMUSP00000074494; -.
DR   PhosphoSitePlus; Q9CZQ9; -.
DR   MaxQB; Q9CZQ9; -.
DR   PaxDb; 10090-ENSMUSP00000074494; -.
DR   ProteomicsDB; 277182; -.
DR   ABCD; Q9CZQ9; 1 sequenced antibody.
DR   Antibodypedia; 35007; 162 antibodies from 27 providers.
DR   DNASU; 72569; -.
DR   Ensembl; ENSMUST00000074963.9; ENSMUSP00000074494.3; ENSMUSG00000063145.11.
DR   GeneID; 72569; -.
DR   KEGG; mmu:72569; -.
DR   UCSC; uc008jyf.1; mouse.
DR   AGR; MGI:1919819; -.
DR   CTD; 129880; -.
DR   MGI; MGI:1919819; Bbs5.
DR   VEuPathDB; HostDB:ENSMUSG00000063145; -.
DR   eggNOG; ENOG502QR2Z; Eukaryota.
DR   GeneTree; ENSGT00390000002753; -.
DR   HOGENOM; CLU_052113_0_0_1; -.
DR   InParanoid; Q9CZQ9; -.
DR   OMA; PNFGIQY; -.
DR   OrthoDB; 5476447at2759; -.
DR   PhylomeDB; Q9CZQ9; -.
DR   TreeFam; TF106129; -.
DR   Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR   BioGRID-ORCS; 72569; 3 hits in 76 CRISPR screens.
DR   PRO; PR:Q9CZQ9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9CZQ9; Protein.
DR   Bgee; ENSMUSG00000063145; Expressed in spermatid and 214 other cell types or tissues.
DR   ExpressionAtlas; Q9CZQ9; baseline and differential.
DR   GO; GO:0005930; C:axoneme; IDA:MGI.
DR   GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR   GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR   GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL.
DR   GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR   GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd00900; PH-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR006606; BBL5.
DR   InterPro; IPR030804; BBS5/fem-3.
DR   InterPro; IPR014003; DM16_repeat.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR21351:SF0; BARDET-BIEDL SYNDROME 5 PROTEIN; 1.
DR   PANTHER; PTHR21351; BARDET-BIEDL SYNDROME PROTEIN 5; 1.
DR   Pfam; PF07289; BBL5; 1.
DR   PIRSF; PIRSF010072; DUF1448; 1.
DR   SMART; SM00683; DM16; 2.
DR   Genevisible; Q9CZQ9; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..341
FT                   /note="Bardet-Biedl syndrome 5 protein homolog"
FT                   /id="PRO_0000223256"
SQ   SEQUENCE   341 AA;  38862 MW;  8FD2BF5943F72325 CRC64;
     MSVLDVLWED RDVRFDVSSQ QMKTRPGEVL IDCLDSIEDT KGNNGDRGRL LVTNLRIIWH
     SLALPRVNLS IGYNCILNIT TRTANSKLRG QTEALYILTK CNTTRFEFIF TNLVPGSPRL
     FTSVIAVHRA YETSKMYRDF KLRSAVIQNK QLRLLPQEHV YDKINGVWNL SSDQGNLGTF
     FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV
     EKLQESVKEI NSLHKVYSAS PIFGVNYEME EKPQPLEALT VEQIQDDVEI DSDDHTDAFV
     AYFADGNKQQ DREPVFSEEL GLAIEKLKDG FTLQGLWEVM S
//