BBS7_HUMAN
ID BBS7_HUMAN Reviewed; 715 AA.
AC Q8IWZ6; Q4W5P8; Q8N581; Q9NVI4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Bardet-Biedl syndrome 7 protein;
DE AltName: Full=BBS2-like protein 1;
GN Name=BBS7; Synonyms=BBS2L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS BBS7 ILE-211
RP AND ARG-323.
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 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP INTERACTION WITH CCDC28B.
RX PubMed=16327777; DOI=10.1038/nature04370;
RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S.,
RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.;
RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome.";
RL Nature 439:326-330(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17574030; DOI=10.1016/j.cell.2007.03.053;
RA Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J., Merdes A.,
RA Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C., Jackson P.K.;
RT "A core complex of BBS proteins cooperates with the GTPase Rab8 to promote
RT ciliary membrane biogenesis.";
RL Cell 129:1201-1213(2007).
RN [7]
RP INTERACTION WITH ALDOB.
RX PubMed=18000879; DOI=10.1002/cm.20250;
RA Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.;
RT "Novel interaction partners of Bardet-Biedl syndrome proteins.";
RL Cell Motil. Cytoskeleton 65:143-155(2008).
RN [8]
RP INTERACTION WITH BBS2.
RX PubMed=20080638; DOI=10.1073/pnas.0910268107;
RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
RA Sheffield V.C.;
RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and
RT mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [9]
RP FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME
RP COMPLEX, INTERACTION WITH SMO, AND SUBCELLULAR LOCATION.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP VARIANT BBS7 ILE-211.
RX PubMed=12677556; DOI=10.1086/375178;
RA Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E., Kirsten B.,
RA Mein C.A., Froguel P., Scambler P.J., Lewis R.A., Lupski J.R., Katsanis N.;
RT "Genetic interaction of BBS1 mutations with alleles at other BBS loci can
RT result in non-Mendelian Bardet-Biedl syndrome.";
RL Am. J. Hum. Genet. 72:1187-1199(2003).
RN [12]
RP VARIANT BBS7 PHE-66.
RX PubMed=15770229; DOI=10.1038/sj.ejhg.5201372;
RA Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P.,
RA Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M., Kaplan J.,
RA Bitoun P., Lacombe D., Verloes A., Bonneau D., Perrin-Schmitt F.,
RA Brandt C., Besancon A.-F., Mandel J.-L., Cossee M., Dollfus H.;
RT "Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl
RT syndrome family cohort.";
RL Eur. J. Hum. Genet. 13:607-616(2005).
RN [13]
RP VARIANT BBS7 ARG-63.
RX PubMed=21344540; DOI=10.1002/humu.21480;
RA Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A.,
RA Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A.,
RA Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D.,
RA Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K., Heon E.;
RT "BBS genotype-phenotype assessment of a multiethnic patient cohort calls
RT for a revision of the disease definition.";
RL Hum. Mutat. 32:610-619(2011).
RN [14]
RP VARIANT PRO-293.
RX PubMed=21552264; DOI=10.1038/ng.826;
RA Putoux A., Thomas S., Coene K.L., Davis E.E., Alanay Y., Ogur G., Uz E.,
RA Buzas D., Gomes C., Patrier S., Bennett C.L., Elkhartoufi N., Frison M.H.,
RA Rigonnot L., Joye N., Pruvost S., Utine G.E., Boduroglu K., Nitschke P.,
RA Fertitta L., Thauvin-Robinet C., Munnich A., Cormier-Daire V., Hennekam R.,
RA Colin E., Akarsu N.A., Bole-Feysot C., Cagnard N., Schmitt A., Goudin N.,
RA Lyonnet S., Encha-Razavi F., Siffroi J.P., Winey M., Katsanis N.,
RA Gonzales M., Vekemans M., Beales P.L., Attie-Bitach T.;
RT "KIF7 mutations cause fetal hydrolethalus and acrocallosal syndromes.";
RL Nat. Genet. 43:601-606(2011).
RN [15]
RP VARIANT CYS-671, AND INVOLVEMENT IN CILIOPATHIES.
RX PubMed=21258341; DOI=10.1038/ng.756;
RA Davis E.E., Zhang Q., Liu Q., Diplas B.H., Davey L.M., Hartley J.,
RA Stoetzel C., Szymanska K., Ramaswami G., Logan C.V., Muzny D.M.,
RA Young A.C., Wheeler D.A., Cruz P., Morgan M., Lewis L.R., Cherukuri P.,
RA Maskeri B., Hansen N.F., Mullikin J.C., Blakesley R.W., Bouffard G.G.,
RA Gyapay G., Rieger S., Tonshoff B., Kern I., Soliman N.A., Neuhaus T.J.,
RA Swoboda K.J., Kayserili H., Gallagher T.E., Lewis R.A., Bergmann C.,
RA Otto E.A., Saunier S., Scambler P.J., Beales P.L., Gleeson J.G.,
RA Maher E.R., Attie-Bitach T., Dollfus H., Johnson C.A., Green E.D.,
RA Gibbs R.A., Hildebrandt F., Pierce E.A., Katsanis N.;
RT "TTC21B contributes both causal and modifying alleles across the ciliopathy
RT spectrum.";
RL Nat. Genet. 43:189-196(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 proper BBSome complex assembly and its ciliary localization.
CC {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.
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 and ALDOB. Interacts with SMO; the interaction
CC is indicative for the association of SMO with the BBsome complex to
CC facilitate ciliary localization of SMO. {ECO:0000269|PubMed:16327777,
CC ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:18000879,
CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:22072986}.
CC -!- INTERACTION:
CC Q8IWZ6; P05062: ALDOB; NbExp=4; IntAct=EBI-1806001, EBI-1045507;
CC Q8IWZ6; Q8NFJ9: BBS1; NbExp=7; IntAct=EBI-1806001, EBI-1805484;
CC Q8IWZ6; Q8TAM1: BBS10; NbExp=4; IntAct=EBI-1806001, EBI-6128013;
CC Q8IWZ6; Q6ZW61: BBS12; NbExp=8; IntAct=EBI-1806001, EBI-6128352;
CC Q8IWZ6; Q9BXC9: BBS2; NbExp=14; IntAct=EBI-1806001, EBI-748297;
CC Q8IWZ6; P78371: CCT2; NbExp=3; IntAct=EBI-1806001, EBI-357407;
CC Q8IWZ6; Q15051: IQCB1; NbExp=5; IntAct=EBI-1806001, EBI-2805823;
CC Q8IWZ6; P05412: JUN; NbExp=3; IntAct=EBI-1806001, EBI-852823;
CC Q8IWZ6-2; Q9BXC9: BBS2; NbExp=6; IntAct=EBI-20947190, EBI-748297;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}. Cytoplasm
CC {ECO:0000269|PubMed:22072986}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:22072986}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q8K2G4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long, lBBS2L1;
CC IsoId=Q8IWZ6-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, sBBS2L1;
CC IsoId=Q8IWZ6-2; Sequence=VSP_008850;
CC -!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed. Isoform 1 is
CC expressed in retina, lung, liver, testis, ovary, prostate, small
CC intestine, liver, brain, heart and pancreas.
CC -!- DISEASE: Note=Ciliary dysfunction leads to a broad spectrum of
CC disorders, collectively termed ciliopathies. Overlapping clinical
CC features include retinal degeneration, renal cystic disease, skeletal
CC abnormalities, fibrosis of various organ, and a complex range of
CC anatomical and functional defects of the central and peripheral nervous
CC system. The ciliopathy range of diseases includes Meckel-Gruber
CC syndrome, Bardet-Biedl syndrome, Joubert syndrome, nephronophtisis,
CC Senior-Loken syndrome, and Jeune asphyxiating thoracic dystrophy among
CC others. Single-locus allelism is insufficient to explain the variable
CC penetrance and expressivity of such disorders, leading to the
CC suggestion that variations across multiple sites of the ciliary
CC proteome, including BBS7, influence the clinical outcome.
CC -!- DISEASE: Bardet-Biedl syndrome 7 (BBS7) [MIM:615984]: A syndrome
CC characterized by usually severe pigmentary retinopathy, early-onset
CC obesity, polydactyly, hypogenitalism, renal malformation and
CC intellectual disability. Secondary features include diabetes mellitus,
CC hypertension and congenital heart disease. Bardet-Biedl syndrome
CC inheritance is autosomal recessive, but three mutated alleles (two at
CC one locus, and a third at a second locus) may be required for clinical
CC manifestation of some forms of the disease.
CC {ECO:0000269|PubMed:12567324, ECO:0000269|PubMed:12677556,
CC ECO:0000269|PubMed:15770229, ECO:0000269|PubMed:21344540}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Mutations of the BBS7 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/bbs7mut.htm";
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DR EMBL; AF521643; AAO16025.1; -; mRNA.
DR EMBL; AF521644; AAO16026.1; -; mRNA.
DR EMBL; AK001577; BAA91767.1; -; mRNA.
DR EMBL; AC079341; AAY40970.1; -; Genomic_DNA.
DR EMBL; BC032691; AAH32691.1; -; mRNA.
DR CCDS; CCDS3724.1; -. [Q8IWZ6-1]
DR CCDS; CCDS54799.1; -. [Q8IWZ6-2]
DR RefSeq; NP_060660.2; NM_018190.3. [Q8IWZ6-2]
DR RefSeq; NP_789794.1; NM_176824.2. [Q8IWZ6-1]
DR AlphaFoldDB; Q8IWZ6; -.
DR SMR; Q8IWZ6; -.
DR BioGRID; 120508; 83.
DR ComplexPortal; CPX-1908; BBSome complex.
DR CORUM; Q8IWZ6; -.
DR DIP; DIP-46566N; -.
DR IntAct; Q8IWZ6; 70.
DR STRING; 9606.ENSP00000264499; -.
DR iPTMnet; Q8IWZ6; -.
DR PhosphoSitePlus; Q8IWZ6; -.
DR BioMuta; BBS7; -.
DR DMDM; 90110978; -.
DR EPD; Q8IWZ6; -.
DR jPOST; Q8IWZ6; -.
DR MassIVE; Q8IWZ6; -.
DR MaxQB; Q8IWZ6; -.
DR PaxDb; Q8IWZ6; -.
DR PeptideAtlas; Q8IWZ6; -.
DR PRIDE; Q8IWZ6; -.
DR ProteomicsDB; 70943; -. [Q8IWZ6-1]
DR ProteomicsDB; 70944; -. [Q8IWZ6-2]
DR Antibodypedia; 26763; 226 antibodies from 31 providers.
DR DNASU; 55212; -.
DR Ensembl; ENST00000264499.9; ENSP00000264499.4; ENSG00000138686.10. [Q8IWZ6-1]
DR Ensembl; ENST00000506636.1; ENSP00000423626.1; ENSG00000138686.10. [Q8IWZ6-2]
DR GeneID; 55212; -.
DR KEGG; hsa:55212; -.
DR MANE-Select; ENST00000264499.9; ENSP00000264499.4; NM_176824.3; NP_789794.1.
DR UCSC; uc003ied.4; human. [Q8IWZ6-1]
DR CTD; 55212; -.
DR DisGeNET; 55212; -.
DR GeneCards; BBS7; -.
DR GeneReviews; BBS7; -.
DR HGNC; HGNC:18758; BBS7.
DR HPA; ENSG00000138686; Tissue enriched (retina).
DR MalaCards; BBS7; -.
DR MIM; 607590; gene.
DR MIM; 615984; phenotype.
DR neXtProt; NX_Q8IWZ6; -.
DR OpenTargets; ENSG00000138686; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR PharmGKB; PA134923753; -.
DR VEuPathDB; HostDB:ENSG00000138686; -.
DR eggNOG; ENOG502QPS5; Eukaryota.
DR GeneTree; ENSGT00390000012346; -.
DR HOGENOM; CLU_018704_1_0_1; -.
DR InParanoid; Q8IWZ6; -.
DR OMA; YSGWLTG; -.
DR OrthoDB; 341332at2759; -.
DR PhylomeDB; Q8IWZ6; -.
DR TreeFam; TF315013; -.
DR PathwayCommons; Q8IWZ6; -.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; Q8IWZ6; -.
DR SIGNOR; Q8IWZ6; -.
DR BioGRID-ORCS; 55212; 9 hits in 1073 CRISPR screens.
DR GeneWiki; BBS7; -.
DR GenomeRNAi; 55212; -.
DR Pharos; Q8IWZ6; Tbio.
DR PRO; PR:Q8IWZ6; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8IWZ6; protein.
DR Bgee; ENSG00000138686; Expressed in endothelial cell and 178 other tissues.
DR ExpressionAtlas; Q8IWZ6; baseline and differential.
DR Genevisible; Q8IWZ6; HS.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0060170; C:ciliary membrane; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; ISS:BHF-UCL.
DR GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL.
DR GO; GO:0048546; P:digestive tract morphogenesis; ISS:BHF-UCL.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:InterPro.
DR GO; GO:0051877; P:pigment granule aggregation in cell center; ISS:BHF-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IPI:MGI.
DR GO; GO:1903929; P:primary palate development; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IPI:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR016575; Bardet-Biedl_syndrome_7_prot.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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; Bardet-Biedl syndrome; Cell membrane;
KW Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Disease variant; Intellectual disability;
KW Membrane; Obesity; Protein transport; Reference proteome;
KW Sensory transduction; Transport; Vision.
FT CHAIN 1..715
FT /note="Bardet-Biedl syndrome 7 protein"
FT /id="PRO_0000064846"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 673..715
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12567324,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_008850"
FT VARIANT 63
FT /note="G -> R (in BBS7; dbSNP:rs754579374)"
FT /evidence="ECO:0000269|PubMed:21344540"
FT /id="VAR_066286"
FT VARIANT 66
FT /note="I -> F (in BBS7; dbSNP:rs1553934343)"
FT /evidence="ECO:0000269|PubMed:15770229"
FT /id="VAR_038893"
FT VARIANT 211
FT /note="T -> I (in BBS7; dbSNP:rs119466002)"
FT /evidence="ECO:0000269|PubMed:12567324,
FT ECO:0000269|PubMed:12677556"
FT /id="VAR_017212"
FT VARIANT 293
FT /note="Q -> P (found in a patient with Bardet-Biedl
FT syndrome also carrying a frameshift mutation in BBS10 and
FT variant R-834 in KIF7; dbSNP:rs889417696)"
FT /evidence="ECO:0000269|PubMed:21552264"
FT /id="VAR_066459"
FT VARIANT 323
FT /note="H -> R (in BBS7; dbSNP:rs119466001)"
FT /evidence="ECO:0000269|PubMed:12567324"
FT /id="VAR_017213"
FT VARIANT 671
FT /note="Y -> C (in a patient with Meckel-Gruber like
FT syndrome also carrying Y-60 in TTC21B; dbSNP:rs1013002037)"
FT /evidence="ECO:0000269|PubMed:21258341"
FT /id="VAR_065555"
FT CONFLICT 469
FT /note="Q -> L (in Ref. 1; AAO16025/AAO16026 and 2;
FT BAA91767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 80353 MW; A7856647969713FF CRC64;
MDLILNRMDY LQVGVTSQKT MKLIPASRHR ATQKVVIGDH DGVVMCFGMK KGEAAAVFKT
LPGPKIARLE LGGVINTPQE KIFIAAASEI RGFTKRGKQF LSFETNLTES IKAMHISGSD
LFLSASYIYN HYCDCKDQHY YLSGDKINDV ICLPVERLSR ITPVLACQDR VLRVLQGSDV
MYAVEVPGPP TVLALHNGNG GDSGEDLLFG TSDGKLALIQ ITTSKPVRKW EIQNEKKRGG
ILCIDSFDIV GDGVKDLLVG RDDGMVEVYS FDNANEPVLR FDQMLSESVT SIQGGCVGKD
SYDEIVVSTY SGWVTGLTTE PIHKESGPGE ELKINQEMQN KISSLRNELE HLQYKVLQER
ENYQQSSQSS KAKSAVPSFG INDKFTLNKD DASYSLILEV QTAIDNVLIQ SDVPIDLLDV
DKNSAVVSFS SCDSESNDNF LLATYRCQAD TTRLELKIRS IEGQYGTLQA YVTPRIQPKT
CQVRQYHIKP LSLHQRTHFI DHDRPMNTLT LTGQFSFAEV HSWVVFCLPE VPEKPPAGEC
VTFYFQNTFL DTQLESTYRK GEGVFKSDNI STISILKDVL SKEATKRKIN LNISYEINEV
SVKHTLKLIH PKLEYQLLLA KKVQLIDALK ELQIHEGNTN FLIPEYHCIL EEADHLQEEY
KKQPAHLERL YGMITDLFID KFKFKGTNVK TKVPLLLEIL DSYDQNALIS FFDAA
