PTHB1_HUMAN
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 03-AUG-2022, entry version 140.
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
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:16380913, ECO:0000269|PubMed:26085087}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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};
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; 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 AlphaFoldDB; Q3SYG4; -.
DR SMR; Q3SYG4; -.
DR BioGRID; 118089; 20.
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 EPD; Q3SYG4; -.
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; 167 antibodies from 22 providers.
DR DNASU; 27241; -.
DR Ensembl; ENST00000242067.11; ENSP00000242067.6; ENSG00000122507.21. [Q3SYG4-1]
DR Ensembl; ENST00000350941.7; ENSP00000313122.6; ENSG00000122507.21. [Q3SYG4-2]
DR Ensembl; ENST00000355070.6; ENSP00000347182.2; ENSG00000122507.21. [Q3SYG4-7]
DR Ensembl; ENST00000396127.6; ENSP00000379433.2; ENSG00000122507.21. [Q3SYG4-4]
DR Ensembl; ENST00000425508.6; ENSP00000405151.2; ENSG00000122507.21. [Q3SYG4-5]
DR Ensembl; ENST00000672717.1; ENSP00000499835.1; ENSG00000122507.21. [Q3SYG4-4]
DR Ensembl; ENST00000673462.1; ENSP00000499848.1; ENSG00000122507.21. [Q3SYG4-6]
DR GeneID; 27241; -.
DR KEGG; hsa:27241; -.
DR MANE-Select; ENST00000242067.11; ENSP00000242067.6; NM_198428.3; NP_940820.1.
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; -.
DR eggNOG; KOG3679; Eukaryota.
DR GeneTree; ENSGT00390000000803; -.
DR HOGENOM; CLU_015674_1_0_1; -.
DR InParanoid; Q3SYG4; -.
DR OMA; VPVEDWT; -.
DR OrthoDB; 332152at2759; -.
DR PhylomeDB; Q3SYG4; -.
DR TreeFam; TF314513; -.
DR PathwayCommons; Q3SYG4; -.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; Q3SYG4; -.
DR SIGNOR; Q3SYG4; -.
DR BioGRID-ORCS; 27241; 16 hits in 1074 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 195 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; IDA:ComplexPortal.
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 Intellectual disability; Membrane; 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 REGION 850..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:4YD8"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:4YD8"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4YD8"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:4YD8"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 259..271
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 341..349
FT /evidence="ECO:0007829|PDB:4YD8"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:4YD8"
FT TURN 363..365
FT /evidence="ECO:0007829|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
