BBS10_HUMAN
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 03-AUG-2022, entry version 165.
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=4; 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};
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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.ENSP00000376946; -.
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; Q8TAM1; -.
DR PeptideAtlas; Q8TAM1; -.
DR PRIDE; Q8TAM1; -.
DR ProteomicsDB; 73892; -.
DR Antibodypedia; 29650; 171 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 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; AKTFIIF; -.
DR OrthoDB; 1411586at2759; -.
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; 9 hits in 1078 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 177 other tissues.
DR Genevisible; Q8TAM1; HS.
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; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 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; PTHR14667; 1.
DR Pfam; PF00118; Cpn60_TCP1; 2.
DR SUPFAM; SSF48592; SSF48592; 1.
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 homozygous for a mutation in BBS2; unknown
FT pathological significance; 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 compound heterozygote for mutations in BBS1; rare
FT variant; unknown pathological significance;
FT 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; unknown pathological
FT 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; unknown pathological
FT 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
