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   27-MAR-2024, entry version 176.
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=7; IntAct=EBI-1806001, EBI-6128352;
CC       Q8IWZ6; Q9BXC9: BBS2; NbExp=13; 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; 87.
DR   ComplexPortal; CPX-1908; BBSome complex.
DR   CORUM; Q8IWZ6; -.
DR   DIP; DIP-46566N; -.
DR   IntAct; Q8IWZ6; 70.
DR   STRING; 9606.ENSP00000264499; -.
DR   TCDB; 3.A.33.1.1; the bbsome complex (bbsome) family.
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; 9606-ENSP00000264499; -.
DR   PeptideAtlas; Q8IWZ6; -.
DR   ProteomicsDB; 70943; -. [Q8IWZ6-1]
DR   ProteomicsDB; 70944; -. [Q8IWZ6-2]
DR   Pumba; Q8IWZ6; -.
DR   Antibodypedia; 26763; 250 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   AGR; HGNC:18758; -.
DR   CTD; 55212; -.
DR   DisGeNET; 55212; -.
DR   GeneCards; BBS7; -.
DR   GeneReviews; BBS7; -.
DR   HGNC; HGNC:18758; BBS7.
DR   HPA; ENSG00000138686; Tissue enhanced (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; CKDADSY; -.
DR   OrthoDB; 312457at2759; -.
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; 10 hits in 1151 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 180 other cell types or tissues.
DR   ExpressionAtlas; Q8IWZ6; baseline and differential.
DR   GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR   GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR   GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell.
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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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   PANTHER; PTHR16074; BARDET-BIEDL SYNDROME 7 PROTEIN; 1.
DR   PANTHER; PTHR16074:SF4; BARDET-BIEDL SYNDROME 7 PROTEIN; 1.
DR   PIRSF; PIRSF011091; BBS7; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   Genevisible; Q8IWZ6; HS.
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
//