ID   PTHB1_HUMAN             Reviewed;         887 AA.
AC   Q3SYG4; E9PDC9; P78514; Q7KYS6; Q7KYS7; Q8N570; Q99844; Q99854; Q9Y699;
AC   Q9Y6A0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   07-APR-2021, entry version 135.
DE   RecName: Full=Protein PTHB1;
DE   AltName: Full=Bardet-Biedl syndrome 9 protein;
DE   AltName: Full=Parathyroid hormone-responsive B1 gene protein;
GN   Name=BBS9; Synonyms=PTHB1;
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 GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   TISSUE=Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 20-887 (ISOFORM 2), INDUCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Osteosarcoma;
RX   PubMed=10221542; DOI=10.1016/s8756-3282(98)00188-4;
RA   Adams A.E., Rosenblatt M., Suva L.J.;
RT   "Identification of a novel parathyroid hormone-responsive gene in human
RT   osteoblastic cells.";
RL   Bone 24:305-313(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 424-887 (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 611-887 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 435-887
RP   (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 842-887.
RC   TISSUE=Brain, and Spleen;
RA   Keen T.J.;
RT   "Positional candidates for the RP9 retinitis pigmentosa gene.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORMS 1; 2; 4 AND 6), AND CHROMOSOMAL
RP   TRANSLOCATION WITH OBSCN.
RX   PubMed=12618763; DOI=10.1038/sj.onc.1206332;
RA   Vernon E.G., Malik K., Reynolds P., Powlesland R., Dallosso A.R.,
RA   Jackson S., Henthorn K., Green E.D., Brown K.W.;
RT   "The parathyroid hormone-responsive B1 gene is interrupted by a
RT   t(1;7)(q42;p15) breakpoint associated with Wilms' tumour.";
RL   Oncogene 22:1371-1380(2003).
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   FUNCTION, FUNCTION OF THE BBSOME COMPLEX, INTERACTION WITH LZTL1,
RP   IDENTIFICATION IN THE BBSOME COMPLEX, 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   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-407, CHARACTERIZATION OF
RP   VARIANT BBS9 ARG-141, AND MUTAGENESIS OF SER-142 AND TYR-186.
RX   PubMed=26085087; DOI=10.1074/jbc.m115.649202;
RA   Knockenhauer K.E., Schwartz T.U.;
RT   "Structural characterization of Bardet-Biedl syndrome 9 protein (BBS9).";
RL   J. Biol. Chem. 290:19569-19583(2015).
RN   [9]
RP   VARIANT BBS9 ARG-141, AND TISSUE SPECIFICITY.
RX   PubMed=16380913; DOI=10.1086/498323;
RA   Nishimura D.Y., Swiderski R.E., Searby C.C., Berg E.M., Ferguson A.L.,
RA   Hennekam R.C.M., Merin S., Weleber R.G., Biesecker L.G., Stone E.M.,
RA   Sheffield V.C.;
RT   "Comparative genomics and gene expression analysis identifies BBS9, a new
RT   Bardet-Biedl syndrome gene.";
RL   Am. J. Hum. Genet. 77:1021-1033(2005).
RN   [10]
RP   VARIANTS ILE-549; PHE-665 AND GLN-779.
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).
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. Required for
CC       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 LZTL1; the interaction
CC       mediates the association of LZTL1 with the BBsome complex and regulates
CC       BBSome ciliary trafficking. {ECO:0000269|PubMed:17574030,
CC       ECO:0000269|PubMed:22072986}.
CC   -!- INTERACTION:
CC       Q3SYG4; Q8NFJ9: BBS1; NbExp=12; IntAct=EBI-2826852, EBI-1805484;
CC       Q3SYG4; Q8TAM1: BBS10; NbExp=2; IntAct=EBI-2826852, EBI-6128013;
CC       Q3SYG4; Q6ZW61: BBS12; NbExp=2; IntAct=EBI-2826852, EBI-6128352;
CC       Q3SYG4; Q9BXC9: BBS2; NbExp=15; IntAct=EBI-2826852, EBI-748297;
CC       Q3SYG4; Q96RK4: BBS4; NbExp=6; IntAct=EBI-2826852, EBI-1805814;
CC       Q3SYG4; Q8N3I7: BBS5; NbExp=6; IntAct=EBI-2826852, EBI-2892592;
CC       Q3SYG4; Q15051: IQCB1; NbExp=5; IntAct=EBI-2826852, EBI-2805823;
CC       Q3SYG4; Q9NQ48: LZTFL1; NbExp=8; IntAct=EBI-2826852, EBI-2824799;
CC       Q3SYG4; A0A0C4DGX9: TTC8; NbExp=3; IntAct=EBI-2826852, EBI-20959097;
CC       Q3SYG4; Q8TAM2: TTC8; NbExp=2; IntAct=EBI-2826852, EBI-2892638;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome. Cell projection, cilium membrane. Cytoplasm.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC       centriolar satellite.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q3SYG4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3SYG4-2; Sequence=VSP_018426;
CC       Name=3;
CC         IsoId=Q3SYG4-3; Sequence=VSP_018428;
CC       Name=4;
CC         IsoId=Q3SYG4-4; Sequence=VSP_018427;
CC       Name=5;
CC         IsoId=Q3SYG4-5; Sequence=VSP_018421, VSP_018422, VSP_018423;
CC       Name=6;
CC         IsoId=Q3SYG4-6; Sequence=VSP_018424, VSP_018425;
CC       Name=7;
CC         IsoId=Q3SYG4-7; Sequence=VSP_054063;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in adult heart,
CC       skeletal muscle, lung, liver, kidney, placenta and brain, and in fetal
CC       kidney, lung, liver and brain. {ECO:0000269|PubMed:10221542,
CC       ECO:0000269|PubMed:16380913}.
CC   -!- INDUCTION: Down-regulated by parathyroid hormone.
CC       {ECO:0000269|PubMed:10221542}.
CC   -!- DISEASE: Note=A chromosomal aberration involving PTHB1 has been found
CC       in Wilms tumor. Translocation t(1;7)(q42;p15) with OBSCN.
CC       {ECO:0000269|PubMed:12618763}.
CC   -!- DISEASE: Bardet-Biedl syndrome 9 (BBS9) [MIM:615986]: A syndrome
CC       characterized by usually severe pigmentary retinopathy, early-onset
CC       obesity, polydactyly, hypogenitalism, renal malformation and mental
CC       retardation. Secondary features include diabetes mellitus, hypertension
CC       and congenital heart disease. Bardet-Biedl syndrome inheritance is
CC       autosomal recessive, but three mutated alleles (two at one locus, and a
CC       third at a second locus) may be required for clinical manifestation of
CC       some forms of the disease. {ECO:0000269|PubMed:16380913,
CC       ECO:0000269|PubMed:26085087}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD25980.1; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305};
CC       Sequence=AAD25981.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC006195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC007312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC074338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC078833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC032715; AAH32715.1; -; mRNA.
DR   EMBL; BC103831; AAI03832.1; -; mRNA.
DR   EMBL; AF095770; AAD25980.1; ALT_SEQ; mRNA.
DR   EMBL; AF095771; AAD25981.1; ALT_INIT; mRNA.
DR   EMBL; U85994; AAB61918.1; -; mRNA.
DR   EMBL; U85995; AAB61919.1; -; mRNA.
DR   EMBL; U85997; AAB46606.1; -; Genomic_DNA.
DR   EMBL; U87408; AAB47568.1; -; mRNA.
DR   CCDS; CCDS34618.1; -. [Q3SYG4-7]
DR   CCDS; CCDS43566.1; -. [Q3SYG4-1]
DR   CCDS; CCDS47572.1; -. [Q3SYG4-4]
DR   CCDS; CCDS5441.1; -. [Q3SYG4-2]
DR   RefSeq; NP_001028776.1; NM_001033604.1. [Q3SYG4-4]
DR   RefSeq; NP_001028777.1; NM_001033605.1. [Q3SYG4-7]
DR   RefSeq; NP_001334965.1; NM_001348036.1. [Q3SYG4-1]
DR   RefSeq; NP_055266.2; NM_014451.3. [Q3SYG4-2]
DR   RefSeq; NP_940820.1; NM_198428.2. [Q3SYG4-1]
DR   PDB; 4YD8; X-ray; 1.80 A; A/B=1-407.
DR   PDB; 6XT9; EM; 3.80 A; I=1-887.
DR   PDBsum; 4YD8; -.
DR   PDBsum; 6XT9; -.
DR   SMR; Q3SYG4; -.
DR   BioGRID; 118089; 18.
DR   ComplexPortal; CPX-1908; BBSome complex.
DR   CORUM; Q3SYG4; -.
DR   DIP; DIP-60358N; -.
DR   IntAct; Q3SYG4; 25.
DR   MINT; Q3SYG4; -.
DR   STRING; 9606.ENSP00000242067; -.
DR   iPTMnet; Q3SYG4; -.
DR   PhosphoSitePlus; Q3SYG4; -.
DR   BioMuta; BBS9; -.
DR   DMDM; 97180305; -.
DR   jPOST; Q3SYG4; -.
DR   MassIVE; Q3SYG4; -.
DR   MaxQB; Q3SYG4; -.
DR   PaxDb; Q3SYG4; -.
DR   PeptideAtlas; Q3SYG4; -.
DR   PRIDE; Q3SYG4; -.
DR   ProteomicsDB; 19635; -.
DR   ProteomicsDB; 61861; -. [Q3SYG4-1]
DR   ProteomicsDB; 61862; -. [Q3SYG4-2]
DR   ProteomicsDB; 61863; -. [Q3SYG4-3]
DR   ProteomicsDB; 61864; -. [Q3SYG4-4]
DR   ProteomicsDB; 61865; -. [Q3SYG4-5]
DR   ProteomicsDB; 61866; -. [Q3SYG4-6]
DR   Antibodypedia; 12805; 163 antibodies.
DR   Ensembl; ENST00000242067; ENSP00000242067; ENSG00000122507. [Q3SYG4-1]
DR   Ensembl; ENST00000350941; ENSP00000313122; ENSG00000122507. [Q3SYG4-2]
DR   Ensembl; ENST00000355070; ENSP00000347182; ENSG00000122507. [Q3SYG4-7]
DR   Ensembl; ENST00000396127; ENSP00000379433; ENSG00000122507. [Q3SYG4-4]
DR   Ensembl; ENST00000425508; ENSP00000405151; ENSG00000122507. [Q3SYG4-5]
DR   Ensembl; ENST00000672717; ENSP00000499835; ENSG00000122507. [Q3SYG4-4]
DR   Ensembl; ENST00000673462; ENSP00000499848; ENSG00000122507. [Q3SYG4-6]
DR   GeneID; 27241; -.
DR   KEGG; hsa:27241; -.
DR   UCSC; uc003tdn.2; human. [Q3SYG4-1]
DR   CTD; 27241; -.
DR   DisGeNET; 27241; -.
DR   GeneCards; BBS9; -.
DR   GeneReviews; BBS9; -.
DR   HGNC; HGNC:30000; BBS9.
DR   HPA; ENSG00000122507; Low tissue specificity.
DR   MalaCards; BBS9; -.
DR   MIM; 607968; gene.
DR   MIM; 615986; phenotype.
DR   neXtProt; NX_Q3SYG4; -.
DR   OpenTargets; ENSG00000122507; -.
DR   Orphanet; 110; Bardet-Biedl syndrome.
DR   PharmGKB; PA162377359; -.
DR   VEuPathDB; HostDB:ENSG00000122507.20; -.
DR   eggNOG; KOG3679; Eukaryota.
DR   GeneTree; ENSGT00390000000803; -.
DR   HOGENOM; CLU_015674_1_0_1; -.
DR   InParanoid; Q3SYG4; -.
DR   OMA; DTHWAIR; -.
DR   OrthoDB; 332152at2759; -.
DR   PhylomeDB; Q3SYG4; -.
DR   TreeFam; TF314513; -.
DR   PathwayCommons; Q3SYG4; -.
DR   Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR   SIGNOR; Q3SYG4; -.
DR   BioGRID-ORCS; 27241; 11 hits in 992 CRISPR screens.
DR   ChiTaRS; BBS9; human.
DR   GeneWiki; BBS9; -.
DR   GenomeRNAi; 27241; -.
DR   Pharos; Q3SYG4; Tbio.
DR   PRO; PR:Q3SYG4; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q3SYG4; protein.
DR   Bgee; ENSG00000122507; Expressed in oocyte and 226 other tissues.
DR   ExpressionAtlas; Q3SYG4; baseline and differential.
DR   Genevisible; Q3SYG4; HS.
DR   GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR   GO; GO:0034451; C:centriolar satellite; IDA:GO_Central.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035869; C:ciliary transition zone; IDA:GO_Central.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0061512; P:protein localization to cilium; IMP:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR028074; PHTB1_C_dom.
DR   InterPro; IPR028073; PHTB1_N_dom.
DR   InterPro; IPR026511; PTHB1.
DR   PANTHER; PTHR20991; PTHR20991; 1.
DR   Pfam; PF14728; PHTB1_C; 1.
DR   Pfam; PF14727; PHTB1_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Bardet-Biedl syndrome; Cell membrane;
KW   Cell projection; Chromosomal rearrangement; Ciliopathy; Cilium;
KW   Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant;
KW   Membrane; Mental retardation; Obesity; Protein transport;
KW   Reference proteome; Sensory transduction; Transport; Vision.
FT   CHAIN           1..887
FT                   /note="Protein PTHB1"
FT                   /id="PRO_0000235269"
FT   REGION          1..407
FT                   /note="Seven-bladed beta-propeller"
FT                   /evidence="ECO:0000269|PubMed:26085087"
FT   REGION          685..765
FT                   /note="Interaction with LZTL1"
FT                   /evidence="ECO:0000269|PubMed:22072986"
FT   SITE            141
FT                   /note="Critical for protein stability"
FT                   /evidence="ECO:0000269|PubMed:26085087"
FT   VAR_SEQ         1..45
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018421"
FT   VAR_SEQ         339..355
FT                   /note="HDLKGVIVTLSDDGHLQ -> QFSLWKHLLPRSSTLEK (in isoform
FT                   5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018422"
FT   VAR_SEQ         356..887
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018423"
FT   VAR_SEQ         478..518
FT                   /note="TPDLTRTVSFSVYLKRSYTPSELEGNAVVSYSRPTDRNPDG -> S (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10221542"
FT                   /id="VSP_018426"
FT   VAR_SEQ         478..513
FT                   /note="TPDLTRTVSFSVYLKRSYTPSELEGNAVVSYSRPTD -> N (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_018427"
FT   VAR_SEQ         478..481
FT                   /note="TPDL -> IFSS (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018424"
FT   VAR_SEQ         482..887
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018425"
FT   VAR_SEQ         513..517
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054063"
FT   VAR_SEQ         878..887
FT                   /note="EVSPLQGVSE -> GKRLDGLHKR (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_018428"
FT   VARIANT         12
FT                   /note="T -> A (in dbSNP:rs4498440)"
FT                   /id="VAR_051289"
FT   VARIANT         141
FT                   /note="G -> R (in BBS9; severe loss of protein stability,
FT                   probably due to aberrant folding; dbSNP:rs137852857)"
FT                   /evidence="ECO:0000269|PubMed:16380913,
FT                   ECO:0000269|PubMed:26085087"
FT                   /id="VAR_026389"
FT   VARIANT         455
FT                   /note="A -> T (in dbSNP:rs11773504)"
FT                   /id="VAR_051290"
FT   VARIANT         455
FT                   /note="A -> V (in dbSNP:rs764873070)"
FT                   /id="VAR_026390"
FT   VARIANT         521
FT                   /note="R -> Q (in dbSNP:rs34218557)"
FT                   /id="VAR_051291"
FT   VARIANT         549
FT                   /note="T -> I (in dbSNP:rs59252892)"
FT                   /evidence="ECO:0000269|PubMed:21344540"
FT                   /id="VAR_066292"
FT   VARIANT         665
FT                   /note="L -> F (in dbSNP:rs116262072)"
FT                   /evidence="ECO:0000269|PubMed:21344540"
FT                   /id="VAR_066293"
FT   VARIANT         779
FT                   /note="L -> Q (in dbSNP:rs142434516)"
FT                   /evidence="ECO:0000269|PubMed:21344540"
FT                   /id="VAR_066294"
FT   MUTAGEN         142
FT                   /note="S->G: Fails to restore protein stability; when
FT                   associated with pathogenic variant BBS9 R-141."
FT                   /evidence="ECO:0000269|PubMed:26085087"
FT   MUTAGEN         186
FT                   /note="Y->A: Fails to restore protein stability; when
FT                   associated with pathogenic variant BBS9 R-141."
FT                   /evidence="ECO:0000269|PubMed:26085087"
FT   CONFLICT        282
FT                   /note="K -> R (in Ref. 3; AAD25981)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        759
FT                   /note="L -> V (in Ref. 4; AAB47568)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..13
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   TURN            15..17
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          24..28
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          39..43
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          47..52
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          57..62
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          67..73
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          80..84
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          94..98
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          100..108
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          123..130
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          135..141
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   HELIX           143..145
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          151..156
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          159..165
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          168..174
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          184..187
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   TURN            188..191
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          192..196
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          200..206
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   HELIX           207..212
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          236..240
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          245..251
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          259..271
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          277..282
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          287..294
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          302..307
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          310..316
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          319..325
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          330..338
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          341..349
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   STRAND          353..358
FT                   /evidence="ECO:0007744|PDB:4YD8"
FT   TURN            363..365
FT                   /evidence="ECO:0007744|PDB:4YD8"
SQ   SEQUENCE   887 AA;  99280 MW;  8E333B7680243B7A CRC64;
     MSLFKARDWW STILGDKEEF DQGCLCLANV DNSGNGQDKI IVGSFMGYLR IFSPHPAKTG
     DGAQAEDLLL EVDLRDPVLQ VEVGKFVSGT EMLHLAVLHS RKLCVYSVSG TLGNVEHGNQ
     CQMKLMYEHN LQRTACNMTY GSFGGVKGRD LICIQSMDGM LMVFEQESYA FGRFLPGFLL
     PGPLAYSSRT DSFLTVSSCQ QVESYKYQVL AFATDADKRQ ETEQQKLGSG KRLVVDWTLN
     IGEQALDICI VSFNQSASSV FVLGERNFFC LKDNGQIRFM KKLDWSPSCF LPYCSVSEGT
     INTLIGNHNN MLHIYQDVTL KWATQLPHIP VAVRVGCLHD LKGVIVTLSD DGHLQCSYLG
     TDPSLFQAPN VQSRELNYDE LDVEMKELQK IIKDVNKSQG VWPMTEREDD LNVSVVVSPN
     FDSVSQATDV EVGTDLVPSV TVKVTLQNRV ILQKAKLSVY VQPPLELTCD QFTFEFMTPD
     LTRTVSFSVY LKRSYTPSEL EGNAVVSYSR PTDRNPDGIP RVIQCKFRLP LKLICLPGQP
     SKTASHKITI DTNKSPVSLL SLFPGFASQS DDDQVNVMGF HFLGGARITV LASKTSQRYR
     IQSEQFEDLW LITNELILRL QEYFEKQGVK DFACSFSGSI PLQEYFELID HHFELRINGE
     KLEELLSERA VQFRAIQRRL LARFKDKTPA PLQHLDTLLD GTYKQVIALA DAVEENQGNL
     FQSFTRLKSA THLVILLIAL WQKLSADQVA ILEAAFLPLQ EDTQELGWEE TVDAAISHLL
     KTCLSKSSKE QALNLNSQLN IPKDTSQLKK HITLLCDRLS KGGRLCLSTD AAAPQTMVMP
     GGCTTIPESD LEERSVEQDS TELFTNHRHL TAETPRPEVS PLQGVSE
//