BBS1_MOUSE
ID BBS1_MOUSE Reviewed; 593 AA.
AC Q3V3N7;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bardet-Biedl syndrome 1 protein homolog;
GN Name=Bbs1;
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=Thymus;
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; TISSUE=Thymus;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15322545; DOI=10.1038/ng1418;
RA Kulaga H.M., Leitch C.C., Eichers E.R., Badano J.L., Lesemann A.,
RA Hoskins B.E., Lupski J.R., Beales P.L., Reed R.R., Katsanis N.;
RT "Loss of BBS proteins causes anosmia in humans and defects in olfactory
RT cilia structure and function in the mouse.";
RL Nat. Genet. 36:994-998(2004).
RN [4]
RP MUTAGENESIS OF MET-390.
RX PubMed=18032602; DOI=10.1073/pnas.0708571104;
RA Davis R.E., Swiderski R.E., Rahmouni K., Nishimura D.Y., Mullins R.F.,
RA Agassandian K., Philp A.R., Searby C.C., Andrews M.P., Thompson S.,
RA Berry C.J., Thedens D.R., Yang B., Weiss R.M., Cassell M.D., Stone E.M.,
RA Sheffield V.C.;
RT "A knockin mouse model of the Bardet-Biedl syndrome 1 M390R mutation has
RT cilia defects, ventriculomegaly, retinopathy, and obesity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19422-19427(2007).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28237838; DOI=10.1016/j.ymthe.2017.02.006;
RA Williams C.L., Uytingco C.R., Green W.W., McIntyre J.C., Ukhanov K.,
RA Zimmerman A.D., Shively D.T., Zhang L., Nishimura D.Y., Sheffield V.C.,
RA Martens J.R.;
RT "Gene therapeutic reversal of peripheral olfactory impairment in Bardet-
RT Biedl syndrome.";
RL Mol. Ther. 25:904-916(2017).
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 proper BBSome complex assembly (By similarity). Plays a role in
CC olfactory cilium biogenesis/maintenance and trafficking and is
CC essential for the localization of the BBSome complex in the olfactory
CC sensory neurons cilia (PubMed:15322545, PubMed:28237838).
CC {ECO:0000250|UniProtKB:Q8NFJ9, ECO:0000269|PubMed:15322545,
CC ECO:0000269|PubMed:28237838}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with the C-terminus of
CC RAB3IP. Interacts with CCDC28B and ALDOB. Interacts with PKD1.
CC {ECO:0000250|UniProtKB:Q8NFJ9}.
CC -!- INTERACTION:
CC Q3V3N7; Q8C1Z7: Bbs4; NbExp=5; IntAct=EBI-2892836, EBI-2892887;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:Q8NFJ9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8NFJ9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q8NFJ9}.
CC -!- DISRUPTION PHENOTYPE: Mice are anosmic (inability to perceive odors)
CC and have defective olfactory cilia. Significant reduction in olfactory
CC sensory neurons ciliation in the olfactory epithelium with decreased
CC cilium length and number. Impaired cilium localization of the BBSome
CC complex. {ECO:0000269|PubMed:15322545, ECO:0000269|PubMed:28237838}.
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DR EMBL; AK037753; BAE20519.1; -; mRNA.
DR EMBL; AC141437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS29442.1; -.
DR RefSeq; NP_001028300.1; NM_001033128.3.
DR AlphaFoldDB; Q3V3N7; -.
DR SMR; Q3V3N7; -.
DR ComplexPortal; CPX-1909; BBSome complex.
DR IntAct; Q3V3N7; 10.
DR STRING; 10090.ENSMUSP00000055321; -.
DR iPTMnet; Q3V3N7; -.
DR PhosphoSitePlus; Q3V3N7; -.
DR MaxQB; Q3V3N7; -.
DR PaxDb; Q3V3N7; -.
DR PRIDE; Q3V3N7; -.
DR ProteomicsDB; 273440; -.
DR Ensembl; ENSMUST00000053506; ENSMUSP00000055321; ENSMUSG00000006464.
DR GeneID; 52028; -.
DR KEGG; mmu:52028; -.
DR UCSC; uc008gbk.2; mouse.
DR CTD; 582; -.
DR MGI; MGI:1277215; Bbs1.
DR VEuPathDB; HostDB:ENSMUSG00000006464; -.
DR eggNOG; ENOG502QS2X; Eukaryota.
DR GeneTree; ENSGT00390000005232; -.
DR HOGENOM; CLU_032988_1_0_1; -.
DR InParanoid; Q3V3N7; -.
DR OMA; AMLYGRM; -.
DR OrthoDB; 783386at2759; -.
DR PhylomeDB; Q3V3N7; -.
DR TreeFam; TF312892; -.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR BioGRID-ORCS; 52028; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q3V3N7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3V3N7; protein.
DR Bgee; ENSMUSG00000006464; Expressed in embryonic brain and 170 other tissues.
DR ExpressionAtlas; Q3V3N7; baseline and differential.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0034464; C:BBSome; IDA:MGI.
DR GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IMP:BHF-UCL.
DR GO; GO:0005113; F:patched binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0005119; F:smoothened binding; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0035721; P:intraciliary retrograde transport; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0042048; P:olfactory behavior; IMP:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:MGI.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0061512; P:protein localization to cilium; ISO:MGI.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IMP:BHF-UCL.
DR GO; GO:0001895; P:retina homeostasis; IMP:MGI.
DR GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR GO; GO:0021756; P:striatum development; IMP:MGI.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR028784; BBS1.
DR InterPro; IPR032728; BBS1_N.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PANTHER; PTHR20870; PTHR20870; 1.
DR Pfam; PF14779; BBS1; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Membrane;
KW Olfaction; Protein transport; Reference proteome; Sensory transduction;
KW Transport; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8NFJ9"
FT CHAIN 2..593
FT /note="Bardet-Biedl syndrome 1 protein homolog"
FT /id="PRO_0000441016"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFJ9"
FT MUTAGEN 390
FT /note="M->R: Knockin mice exhibit olfaction deficits, male
FT infertility, ventriculomegaly, retinopathy and obesity."
FT /evidence="ECO:0000269|PubMed:18032602"
SQ SEQUENCE 593 AA; 65094 MW; 322E9DD4DD554813 CRC64;
MAAASSSDSD SGRAESNEAN SKWLDAHYDP MANIHTFSSC LSLADLHGDG EYKLVVGDLG
PGGQQPRLKV LKGPTVLTES PLPALPASAA TFLMDQHEPR TPALALASGP CVYVYKNLRP
YFKFSLPQLP PNPLEQDVWN QAKEDQIDPL TLKEMLEDIR EKADVPLSVQ SLRFLQLELS
EMEAFVNQHK SKVIKRQTVI TTMTTLKKNL ADEDAASCLV LGTESKELLV LDPEAFTILA
KMSLPSVPVF LEVSGQFDVE FRLTAACRNG SIYILRRDSK HPKYCIELSA QPVGLVRVHK
VLVVGSTQES LHGFTHKGKK LWTVQMPAAI LTMNLLEQRS RGLQAVMAAL ANGEVRIYRD
KALLNVIHAP DAVTSLCFGR YGREDNTLIM TTRGGGLIIK ILKRTAVFVE GTGEVGPPLA
QTTKLSVPRK TRLYVDQTLR EREAGTAMHR TFQTDLYLLR LRAARAYVQA LESSLSPMST
TAREPLKLHA VVQGLGPTFK LTLHLQNTST ARPVLGLHVC FLYNKALYAL PQAFFKVPLL
VPGLSYPLET FVESLSSKGI SDMIKVLVLR EGQSAPLLSA HINMPVSEGL AAA
