BBS7_MOUSE
ID BBS7_MOUSE Reviewed; 715 AA.
AC Q8K2G4; Q8C7G3; Q8CH00; Q9CXC2;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Bardet-Biedl syndrome 7 protein homolog;
DE AltName: Full=BBS2-like protein 1;
GN Name=Bbs7; Synonyms=Bbs2l1;
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 [MRNA] (ISOFORM 2).
RX PubMed=12567324; DOI=10.1086/368204;
RA Badano J.L., Ansley S.J., Leitch C.C., Lewis R.A., Lupski J.R.,
RA Katsanis N.;
RT "Identification of a novel Bardet-Biedl syndrome protein, BBS7, that shares
RT structural features with BBS1 and BBS2.";
RL Am. J. Hum. Genet. 72:650-658(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-584 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic lung, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 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 [5]
RP INTERACTION WITH SMO, AND IDENTIFICATION IN THE BBSOME COMPLEX.
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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA Santama N.;
RT "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT ciliogenesis.";
RL Cell. Mol. Life Sci. 71:517-538(2014).
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: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with BBS2 (via C-terminus).
CC Interacts with CCDC28B. Interacts with SMO; the interaction is
CC indicative for the association of SMO with the BBsome complex to
CC facilitate ciliary localization of SMO. {ECO:0000269|PubMed:22072986}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:Q8IWZ6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8IWZ6}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q8IWZ6}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:23807208}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K2G4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2G4-2; Sequence=VSP_008851;
CC Name=3;
CC IsoId=Q8K2G4-3; Sequence=VSP_008852, VSP_008853;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
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DR EMBL; AF521645; AAO16027.1; -; mRNA.
DR EMBL; AK018389; BAB31190.1; -; mRNA.
DR EMBL; AK050291; BAC34169.1; -; mRNA.
DR EMBL; BC031505; AAH31505.1; -; mRNA.
DR CCDS; CCDS17314.2; -. [Q8K2G4-1]
DR RefSeq; NP_082086.2; NM_027810.3. [Q8K2G4-1]
DR AlphaFoldDB; Q8K2G4; -.
DR SMR; Q8K2G4; -.
DR ComplexPortal; CPX-1909; BBSome complex.
DR DIP; DIP-60353N; -.
DR IntAct; Q8K2G4; 6.
DR MINT; Q8K2G4; -.
DR STRING; 10090.ENSMUSP00000103791; -.
DR iPTMnet; Q8K2G4; -.
DR PhosphoSitePlus; Q8K2G4; -.
DR MaxQB; Q8K2G4; -.
DR PaxDb; Q8K2G4; -.
DR PRIDE; Q8K2G4; -.
DR ProteomicsDB; 273465; -. [Q8K2G4-1]
DR ProteomicsDB; 273466; -. [Q8K2G4-2]
DR ProteomicsDB; 273467; -. [Q8K2G4-3]
DR Antibodypedia; 26763; 226 antibodies from 31 providers.
DR Ensembl; ENSMUST00000040148; ENSMUSP00000047273; ENSMUSG00000037325. [Q8K2G4-2]
DR Ensembl; ENSMUST00000108156; ENSMUSP00000103791; ENSMUSG00000037325. [Q8K2G4-1]
DR GeneID; 71492; -.
DR KEGG; mmu:71492; -.
DR UCSC; uc008ozp.2; mouse. [Q8K2G4-2]
DR UCSC; uc008ozq.2; mouse. [Q8K2G4-1]
DR UCSC; uc008ozr.1; mouse. [Q8K2G4-3]
DR CTD; 55212; -.
DR MGI; MGI:1918742; Bbs7.
DR VEuPathDB; HostDB:ENSMUSG00000037325; -.
DR eggNOG; ENOG502QPS5; Eukaryota.
DR GeneTree; ENSGT00390000012346; -.
DR HOGENOM; CLU_018704_1_0_1; -.
DR InParanoid; Q8K2G4; -.
DR OMA; YSGWLTG; -.
DR OrthoDB; 341332at2759; -.
DR PhylomeDB; Q8K2G4; -.
DR TreeFam; TF315013; -.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR BioGRID-ORCS; 71492; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Bbs7; mouse.
DR PRO; PR:Q8K2G4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8K2G4; protein.
DR Bgee; ENSMUSG00000037325; Expressed in retinal neural layer and 202 other tissues.
DR ExpressionAtlas; Q8K2G4; baseline and differential.
DR Genevisible; Q8K2G4; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IGI:MGI.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0001654; P:eye development; IGI:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0060173; P:limb development; IGI:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:InterPro.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:1903929; P:primary palate development; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR InterPro; IPR016575; Bardet-Biedl_syndrome_7_prot.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PIRSF; PIRSF011091; BBS7; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..715
FT /note="Bardet-Biedl syndrome 7 protein homolog"
FT /id="PRO_0000064847"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWZ6"
FT VAR_SEQ 56..57
FT /note="PV -> VM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12567324"
FT /id="VSP_008851"
FT VAR_SEQ 116..161
FT /note="ISGSDLFLSASYIYNHYCDCKDQNYYLSGDKINDVICLPVEKLSRV -> VL
FT FSFMFTYVSIIHLIKLVYTSRFFWKRNLATGISLFRTWNQYTVD (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008852"
FT VAR_SEQ 162..715
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008853"
SQ SEQUENCE 715 AA; 80320 MW; F7D8C284B04DA15B CRC64;
MDLTLSRADY LQVGVTSQKT MKLLPTSRQR ATQKVVVGDQ DGVVICFGVK KGEAVPVFKT
LPGQKISRLE LGGAVNTPQE KIFIAAGSEI RGFTKRGKQF LSFETNLTES IKAMYISGSD
LFLSASYIYN HYCDCKDQNY YLSGDKINDV ICLPVEKLSR VTPVLACQDR VLRVLQGSDV
MYEIEVPGPP TVLALHNGDG GDSGEGLLFG TSDGRLGLIQ ITTSKPIHKW EIRNDKKRGG
ILCVDSFDIM GDGVKDLLVG RDDGMVEVYS FENANEPVLR FDQMLSESVT SIQGGCVGKD
GYDEIVLATY SGWVTGLTTE PTHKESGPGE ELKLNQEMQN KISSLRSEIE HLQFKVLQER
ENYQQSSQSS QAKSTVPSFS INDKFTLNKE DASYSLVLEV RTAIDNVLIQ SDVPIDLLDV
DKNSAVVSFS SCDTESNDNF LLATYRCQAN TTRLELKIRS IEGQYGTLQA YVTPRIQPKT
CQVRQYHIKP LSLHQRTHFI DHDRPMNTLT LTGQFSFAEV HSWVVFCLPE VPEKPPAGEC
ATFYFQNTFL DTQLECVYRK GEGVFKSDNI STISILKDVL SKEATKRKIN LNISYEINEV
SVKHTLKLIH PKLEYQLLLA KKVQLIDALK ELQVHEGNTD FLTPEYRCIL EEADHLQEEY
KKQPAHLERL YGMITDLFID KFKFKGTNVK TKVPMLLEIL DSYDQNTLIS FFDAA
