ID BBS10_HUMAN Reviewed; 723 AA. AC Q8TAM1; Q96CW2; Q9H5D2; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 24-JAN-2024, entry version 173. DE RecName: Full=Bardet-Biedl syndrome 10 protein; GN Name=BBS10; Synonyms=C12orf58; 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 [LARGE SCALE MRNA]. RC TISSUE=Hippocampus, and Skin; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 512-723. RC TISSUE=Lung; 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 INVOLVEMENT IN BBS10, AND VARIANTS BBS10 GLY-11 AND ALA-311. RX PubMed=16823392; DOI=10.1038/sj.ejhg.5201688; RA Laurier V., Stoetzel C., Muller J., Thibault C., Corbani S., Jalkh N., RA Salem N., Chouery E., Poch O., Licaire S., Danse J.M., Amati-Bonneau P., RA Bonneau D., Megarbane A., Mandel J.L., Dollfus H.; RT "Pitfalls of homozygosity mapping: an extended consanguineous Bardet-Biedl RT syndrome family with two mutant genes (BBS2, BBS10), three mutations, but RT no triallelism."; RL Eur. J. Hum. Genet. 14:1195-1203(2006). RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19190184; DOI=10.1073/pnas.0812518106; RA Marion V., Stoetzel C., Schlicht D., Messaddeq N., Koch M., Flori E., RA Danse J.M., Mandel J.-L., Dollfus H.; RT "Transient ciliogenesis involving Bardet-Biedl syndrome proteins is a RT fundamental characteristic of adipogenic differentiation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:1820-1825(2009). RN [5] RP FUNCTION, IDENTIFICATION IN A MULTIPROTEIN COMPLEX, CHARACTERIZATION OF RP VARIANTS BBS10 PRO-34; TRP-49; TRP-91; GLY-240; PHE-308; ALA-311; LEU-329; RP LEU-363; HIS-613; VAL-677 AND PRO-689, AND MUTAGENESIS OF ASP-81. 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 [6] RP VARIANTS BBS10 PRO-34; TRP-49; TRP-91; SER-170; TRP-195; CYS-197; GLY-240; RP PHE-308; ALA-311; LEU-329; LEU-363; SER-414; ARG-579; HIS-613; CYS-613; RP VAL-677 AND PRO-689. RX PubMed=16582908; DOI=10.1038/ng1771; RA Stoetzel C., Laurier V., Davis E.E., Muller J., Rix S., Badano J.L., RA Leitch C.C., Salem N., Chouery E., Corbani S., Jalk N., Vicaire S., RA Sarda P., Hamel C., Lacombe D., Holder M., Odent S., Holder S., RA Brooks A.S., Elcioglu N.H., Da Silva E., Rossillion B., Sigaudy S., RA de Ravel T.J., Alan Lewis R., Leheup B., Verloes A., Amati-Bonneau P., RA Megarbane A., Poch O., Bonneau D., Beales P.L., Mandel J.-L., Katsanis N., RA Dollfus H.; RT "BBS10 encodes a vertebrate-specific chaperonin-like protein and is a major RT BBS locus."; RL Nat. Genet. 38:521-524(2006). RN [7] RP VARIANTS BBS10 TRP-49 AND PRO-687, AND VARIANTS ASN-142; ILE-255 AND RP LEU-539. RX PubMed=20120035; DOI=10.1002/humu.21204; RA Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R., RA Sheffield V.C., Rosenberg T., Brondum-Nielsen K.; RT "Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence variations RT in six genes."; RL Hum. Mutat. 31:429-436(2010). RN [8] RP VARIANTS BBS10 TRP-49; PRO-55; TRP-91; THR-188; GLN-410; SER-414; SER-600 RP AND VAL-636, AND VARIANTS THR-296 AND ARG-715. 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 [9] RP INVOLVEMENT IN BBS10. RX PubMed=23219996; DOI=10.1016/j.gene.2012.11.023; RA Khan S., Ullah I., Irfanullah X., Touseef M., Basit S., Khan M.N., RA Ahmad W.; RT "Novel homozygous mutations in the genes ARL6 and BBS10 underlying Bardet- RT Biedl syndrome."; RL Gene 515:84-88(2013). RN [10] RP VARIANTS BBS10 559-TYR--LEU-723 DEL AND 658-TYR--LEU-723 DEL. RX PubMed=28808579; DOI=10.1038/hgv.2017.33; RA Ohto T., Enokizono T., Tanaka R., Tanaka M., Suzuki H., Sakai A., RA Imagawa K., Fukushima H., Fukushima T., Sumazaki R., Uehara T., RA Takenouchi T., Kosaki K.; RT "A novel BBS10 mutation identified in a patient with Bardet-Biedl syndrome RT with a violent emotional outbreak."; RL Hum. Genome Var. 4:17033-17033(2017). CC -!- FUNCTION: Probable molecular chaperone that assists the folding of CC proteins upon ATP hydrolysis (PubMed:20080638). Plays a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). Involved in CC adipogenic differentiation (PubMed:19190184). CC {ECO:0000269|PubMed:19190184, ECO:0000269|PubMed:20080638}. CC -!- SUBUNIT: Component of a complex composed at least of MKKS, BBS10, CC BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 and CCT8. CC {ECO:0000269|PubMed:20080638}. CC -!- INTERACTION: CC Q8TAM1; Q6ZW61: BBS12; NbExp=5; IntAct=EBI-6128013, EBI-6128352; CC Q8TAM1; Q8IWZ6: BBS7; NbExp=4; IntAct=EBI-6128013, EBI-1806001; CC Q8TAM1; Q3SYG4: BBS9; NbExp=2; IntAct=EBI-6128013, EBI-2826852; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium CC {ECO:0000269|PubMed:19190184}. Note=Located within the basal body of CC the primary cilium of differentiating preadipocytes. CC {ECO:0000269|PubMed:19190184}. CC -!- DISEASE: Bardet-Biedl syndrome 10 (BBS10) [MIM:615987]: 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:16582908, ECO:0000269|PubMed:16823392, CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:20120035, CC ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:23219996, CC ECO:0000269|PubMed:28808579}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Adipocytes derived from BBS-patients' dermal fibroblasts CC in culture exhibit higher propensity for fat accumulation when compared CC to controls. This strongly suggests that a peripheral primary CC dysfunction of adipogenesis participates in the pathogenesis of obesity CC in BBS. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH13795.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15695.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC013795; AAH13795.1; ALT_INIT; mRNA. DR EMBL; BC026355; AAH26355.2; -; mRNA. DR EMBL; AK027213; BAB15695.1; ALT_INIT; mRNA. DR CCDS; CCDS9014.2; -. DR RefSeq; NP_078961.3; NM_024685.3. DR AlphaFoldDB; Q8TAM1; -. DR BioGRID; 122851; 23. DR CORUM; Q8TAM1; -. DR DIP; DIP-60347N; -. DR IntAct; Q8TAM1; 24. DR MINT; Q8TAM1; -. DR STRING; 9606.ENSP00000497413; -. DR iPTMnet; Q8TAM1; -. DR PhosphoSitePlus; Q8TAM1; -. DR BioMuta; BBS10; -. DR DMDM; 97043964; -. DR EPD; Q8TAM1; -. DR jPOST; Q8TAM1; -. DR MassIVE; Q8TAM1; -. DR MaxQB; Q8TAM1; -. DR PaxDb; 9606-ENSP00000376946; -. DR PeptideAtlas; Q8TAM1; -. DR ProteomicsDB; 73892; -. DR Antibodypedia; 29650; 182 antibodies from 27 providers. DR DNASU; 79738; -. DR Ensembl; ENST00000650064.2; ENSP00000497413.1; ENSG00000179941.9. DR GeneID; 79738; -. DR KEGG; hsa:79738; -. DR MANE-Select; ENST00000650064.2; ENSP00000497413.1; NM_024685.4; NP_078961.3. DR UCSC; uc001syd.2; human. DR AGR; HGNC:26291; -. DR CTD; 79738; -. DR DisGeNET; 79738; -. DR GeneCards; BBS10; -. DR GeneReviews; BBS10; -. DR HGNC; HGNC:26291; BBS10. DR HPA; ENSG00000179941; Low tissue specificity. DR MalaCards; BBS10; -. DR MIM; 610148; gene. DR MIM; 615987; phenotype. DR neXtProt; NX_Q8TAM1; -. DR OpenTargets; ENSG00000179941; -. DR Orphanet; 110; Bardet-Biedl syndrome. DR PharmGKB; PA143485387; -. DR VEuPathDB; HostDB:ENSG00000179941; -. DR eggNOG; KOG0357; Eukaryota. DR eggNOG; KOG0360; Eukaryota. DR GeneTree; ENSGT00390000002417; -. DR HOGENOM; CLU_028678_0_0_1; -. DR InParanoid; Q8TAM1; -. DR OMA; YFFKCMT; -. DR OrthoDB; 5362208at2759; -. DR PhylomeDB; Q8TAM1; -. DR TreeFam; TF335867; -. DR PathwayCommons; Q8TAM1; -. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR SignaLink; Q8TAM1; -. DR BioGRID-ORCS; 79738; 10 hits in 1156 CRISPR screens. DR ChiTaRS; BBS10; human. DR GeneWiki; BBS10; -. DR GenomeRNAi; 79738; -. DR Pharos; Q8TAM1; Tbio. DR PRO; PR:Q8TAM1; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q8TAM1; Protein. DR Bgee; ENSG00000179941; Expressed in calcaneal tendon and 179 other cell types or tissues. DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:MGI. DR GO; GO:1905515; P:non-motile cilium assembly; IMP:BHF-UCL. DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:BHF-UCL. DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IMP:MGI. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 2. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1. DR InterPro; IPR042619; BBS10. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR14667; BARDET-BIEDL SYNDROME 10 PROTEIN; 1. DR PANTHER; PTHR14667:SF2; BARDET-BIEDL SYNDROME 10 PROTEIN; 1. DR Pfam; PF00118; Cpn60_TCP1; 2. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR Genevisible; Q8TAM1; HS. PE 1: Evidence at protein level; KW ATP-binding; Bardet-Biedl syndrome; Cell projection; Chaperone; Ciliopathy; KW Disease variant; Intellectual disability; Nucleotide-binding; Obesity; KW Reference proteome; Sensory transduction; Vision. FT CHAIN 1..723 FT /note="Bardet-Biedl syndrome 10 protein" FT /id="PRO_0000235272" FT VARIANT 11 FT /note="V -> G (in BBS10; dbSNP:rs137852838)" FT /evidence="ECO:0000269|PubMed:16823392" FT /id="VAR_075722" FT VARIANT 34 FT /note="R -> P (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; dbSNP:rs137852836)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026391" FT VARIANT 49 FT /note="R -> W (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; dbSNP:rs768933093)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:20120035, FT ECO:0000269|PubMed:21344540" FT /id="VAR_026392" FT VARIANT 55 FT /note="L -> P (in BBS10; dbSNP:rs1460517643)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066252" FT VARIANT 91 FT /note="C -> W (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; dbSNP:rs148374859)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:21344540" FT /id="VAR_026393" FT VARIANT 142 FT /note="D -> N (in dbSNP:rs142863601)" FT /evidence="ECO:0000269|PubMed:20120035" FT /id="VAR_066253" FT VARIANT 170 FT /note="L -> S (in BBS10; dbSNP:rs780916348)" FT /evidence="ECO:0000269|PubMed:16582908" FT /id="VAR_026394" FT VARIANT 188 FT /note="K -> T (in BBS10; associated with V-636)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066254" FT VARIANT 195 FT /note="C -> W (in BBS10)" FT /evidence="ECO:0000269|PubMed:16582908" FT /id="VAR_026395" FT VARIANT 197 FT /note="Y -> C (in BBS10; dbSNP:rs756632517)" FT /evidence="ECO:0000269|PubMed:16582908" FT /id="VAR_026396" FT VARIANT 240 FT /note="V -> G (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; severely reduces the FT interaction with BBS12; 8% of wild-type)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026397" FT VARIANT 255 FT /note="M -> I (found in a patient with Bardet-Biedl FT syndrome; uncertain significance; the patient is homozygous FT for a mutation in BBS2; dbSNP:rs139658279)" FT /evidence="ECO:0000269|PubMed:20120035" FT /id="VAR_066255" FT VARIANT 296 FT /note="A -> T (found in a patient with Bardet-Biedl FT syndrome; uncertain significance; the patient is compound FT heterozygote for mutations in BBS1; dbSNP:rs150587582)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066256" FT VARIANT 308 FT /note="L -> F (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026398" FT VARIANT 311 FT /note="S -> A (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; severely reduces the FT interaction with BBS12; 19% of wild-type; FT dbSNP:rs137852837)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:16823392, ECO:0000269|PubMed:20080638" FT /id="VAR_026399" FT VARIANT 329 FT /note="S -> L (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; severely reduces the FT interaction with BBS12; 15% of wild-type; FT dbSNP:rs1000990130)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026400" FT VARIANT 363 FT /note="P -> L (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; dbSNP:rs938066133)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026401" FT VARIANT 376 FT /note="L -> F (in dbSNP:rs11109474)" FT /id="VAR_026402" FT VARIANT 410 FT /note="H -> Q (in BBS10; dbSNP:rs1447555059)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066257" FT VARIANT 414 FT /note="L -> S (in BBS10; dbSNP:rs786204575)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:21344540" FT /id="VAR_026403" FT VARIANT 539 FT /note="P -> L (in dbSNP:rs35676114)" FT /evidence="ECO:0000269|PubMed:20120035" FT /id="VAR_052272" FT VARIANT 559..723 FT /note="Missing (in BBS10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28808579" FT /id="VAR_079367" FT VARIANT 579 FT /note="K -> R (in BBS10; dbSNP:rs141521925)" FT /evidence="ECO:0000269|PubMed:16582908" FT /id="VAR_026404" FT VARIANT 600 FT /note="L -> S (in BBS10)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066258" FT VARIANT 613 FT /note="Y -> C (in BBS10; dbSNP:rs575957641)" FT /evidence="ECO:0000269|PubMed:16582908" FT /id="VAR_026405" FT VARIANT 613 FT /note="Y -> H (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; dbSNP:rs141647931)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026406" FT VARIANT 636 FT /note="A -> V (in BBS10; associated with T-188; FT dbSNP:rs113224628)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066259" FT VARIANT 658..723 FT /note="Missing (in BBS10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28808579" FT /id="VAR_079368" FT VARIANT 677 FT /note="G -> V (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; dbSNP:rs1555202553)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026407" FT VARIANT 687 FT /note="L -> P (in BBS10)" FT /evidence="ECO:0000269|PubMed:20120035" FT /id="VAR_066260" FT VARIANT 689 FT /note="T -> P (in BBS10; has moderately reduced ability to FT interact with BBS7 and BBS9; dbSNP:rs759387000)" FT /evidence="ECO:0000269|PubMed:16582908, FT ECO:0000269|PubMed:20080638" FT /id="VAR_026408" FT VARIANT 715 FT /note="H -> R (in dbSNP:rs769179905)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066261" FT MUTAGEN 81 FT /note="D->N: Greatly decreases all interactions with BBS7, FT BBS9 and BBS12 indicating that this residue may be required FT for overall protein conformation rather than required for FT ATP binding and substrate folding." FT /evidence="ECO:0000269|PubMed:20080638" FT CONFLICT 514 FT /note="T -> S (in Ref. 2; BAB15695)" FT /evidence="ECO:0000305" FT CONFLICT 586 FT /note="S -> Y (in Ref. 2; BAB15695)" FT /evidence="ECO:0000305" FT CONFLICT 607 FT /note="E -> D (in Ref. 1; AAH26355)" FT /evidence="ECO:0000305" SQ SEQUENCE 723 AA; 80838 MW; 558143FFA5F191DD CRC64; MLSSMAAAGS VKAALQVAEV LEAIVSCCVG PEGRQVLCTK PTGEVLLSRN GGRLLEALHL EHPIARMIVD CVSSHLKKTG DGAKTFIIFL CHLLRGLHAI TDREKDPLMC ENIQTHGRHW KNCSRWKFIS QALLTFQTQI LDGIMDQYLS RHFLSIFSSA KERTLCRSSL ELLLEAYFCG RVGRNNHKFI SQLMCDYFFK CMTCKSGIGV FELVDDHFVE LNVGVTGLPV SDSRIIAGLV LQKDFSVYRP ADGDMRMVIV TETIQPLFST SGSEFILNSE AQFQTSQFWI MEKTKAIMKH LHSQNVKLLI SSVKQPDLVS YYAGVNGISV VECLSSEEVS LIRRIIGLSP FVPPQAFSQC EIPNTALVKF CKPLILRSKR YVHLGLISTC AFIPHSIVLC GPVHGLIEQH EDALHGALKM LRQLFKDLDL NYMTQTNDQN GTSSLFIYKN SGESYQAPDP GNGSIQRPYQ DTVAENKDAL EKTQTYLKVH SNLVIPDVEL ETYIPYSTPT LTPTDTFQTV ETLTCLSLER NRLTDYYEPL LKNNSTAYST RGNRIEISYE NLQVTNITRK GSMLPVSCKL PNMGTSQSYL SSSMPAGCVL PVGGNFEILL HYYLLNYAKK CHQSEETMVS MIIANALLGI PKVLYKSKTG KYSFPHTYIR AVHALQTNQP LVSSQTGLES VMGKYQLLTS VLQCLTKILT IDMVITVKRH PQKVHNQDSE DEL //