BBS7_CAEEL
ID BBS7_CAEEL Reviewed; 721 AA.
AC Q9XW70;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Bardet-Biedl syndrome 7 protein homolog {ECO:0000250|UniProtKB:Q8IWZ6};
DE AltName: Full=Osmotic avoidance abnormal protein 12 {ECO:0000312|WormBase:Y75B8A.12};
GN Name=osm-12 {ECO:0000312|WormBase:Y75B8A.12};
GN Synonyms=bbs-7 {ECO:0000312|WormBase:Y75B8A.12};
GN ORFNames=Y75B8A.12 {ECO:0000312|WormBase:Y75B8A.12};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=14520415; DOI=10.1038/nature02030;
RA Ansley S.J., Badano J.L., Blacque O.E., Hill J., Hoskins B.E., Leitch C.C.,
RA Kim J.C., Ross A.J., Eichers E.R., Teslovich T.M., Mah A.K., Johnsen R.C.,
RA Cavender J.C., Lewis R.A., Leroux M.R., Beales P.L., Katsanis N.;
RT "Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl
RT syndrome.";
RL Nature 425:628-633(2003).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15231740; DOI=10.1101/gad.1194004;
RA Blacque O.E., Reardon M.J., Li C., McCarthy J., Mahjoub M.R., Ansley S.J.,
RA Badano J.L., Mah A.K., Beales P.L., Davidson W.S., Johnsen R.C., Audeh M.,
RA Plasterk R.H., Baillie D.L., Katsanis N., Quarmby L.M., Wicks S.R.,
RA Leroux M.R.;
RT "Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia
RT defects and compromised intraflagellar transport.";
RL Genes Dev. 18:1630-1642(2004).
RN [4]
RP FUNCTION.
RX PubMed=17000880; DOI=10.1083/jcb.200606003;
RA Pan X., Ou G., Civelekoglu-Scholey G., Blacque O.E., Endres N.F., Tao L.,
RA Mogilner A., Leroux M.R., Vale R.D., Scholey J.M.;
RT "Mechanism of transport of IFT particles in C. elegans cilia by the
RT concerted action of kinesin-II and OSM-3 motors.";
RL J. Cell Biol. 174:1035-1045(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22022287; DOI=10.1371/journal.pgen.1002335;
RA Mok C.A., Healey M.P., Shekhar T., Leroux M.R., Heon E., Zhen M.;
RT "Mutations in a guanylate cyclase GCY-35/GCY-36 modify Bardet-Biedl
RT syndrome-associated phenotypes in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002335-E1002335(2011).
RN [6]
RP FUNCTION, INTERACTION WITH BBS-1, AND DISRUPTION PHENOTYPE.
RX PubMed=22922713; DOI=10.1038/ncb2560;
RA Wei Q., Zhang Y., Li Y., Zhang Q., Ling K., Hu J.;
RT "The BBSome controls IFT assembly and turnaround in cilia.";
RL Nat. Cell Biol. 14:950-957(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25335890; DOI=10.1242/jcs.157610;
RA Nguyen P.A., Liou W., Hall D.H., Leroux M.R.;
RT "Ciliopathy proteins establish a bipartite signaling compartment in a C.
RT elegans thermosensory neuron.";
RL J. Cell Sci. 127:5317-5330(2014).
RN [8]
RP MUTAGENESIS OF GLY-314.
RX PubMed=25486278; DOI=10.1371/journal.pone.0113737;
RA Braunreiter K., Hamlin S., Lyman-Gingerich J.;
RT "Identification and characterization of a novel allele of Caenorhabditis
RT elegans bbs-7.";
RL PLoS ONE 9:E113737-E113737(2014).
RN [9]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=26150102; DOI=10.1038/srep11855;
RA Xu Q., Zhang Y., Wei Q., Huang Y., Li Y., Ling K., Hu J.;
RT "BBS4 and BBS5 show functional redundancy in the BBSome to regulate the
RT degradative sorting of ciliary sensory receptors.";
RL Sci. Rep. 5:11855-11855(2015).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF 233-TRP--ASP-721.
RX PubMed=30014846; DOI=10.7554/elife.36833;
RA Hao Y., Yang W., Ren J., Hall Q., Zhang Y., Kaplan J.M.;
RT "Thioredoxin shapes the C. elegans sensory response to Pseudomonas produced
RT nitric oxide.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Component of the BBSome complex (By similarity). The BBSome
CC complex is thought to function as a coat complex required for sorting
CC of specific membrane proteins to the primary cilia (By similarity). The
CC BBSome complex is required for ciliogenesis but is dispensable for
CC centriolar satellite function (By similarity). Required for proper
CC BBSome complex assembly and its ciliary localization (By similarity).
CC Required for cilia biogenesis and both the assembly and movement of
CC intraflagellar transport proteins along the ciliary axoneme
CC (PubMed:15231740, PubMed:17000880, PubMed:22022287, PubMed:22922713,
CC PubMed:26150102). Plays a role in the removal of degraded
CC mechanosensory receptors within the cilia (PubMed:26150102). Plays a
CC role in guanylyl cyclase localization in the ring-like structures at
CC the base of the finger compartment in AFD sensory neurons
CC (PubMed:25335890). In ciliated sensory neurons, required for the
CC sensation of nitric oxide and avoidance of NO-producing organisms like
CC P.aeruginosa (PubMed:30014846). {ECO:0000250|UniProtKB:Q8IWZ6,
CC ECO:0000269|PubMed:15231740, ECO:0000269|PubMed:17000880,
CC ECO:0000269|PubMed:22022287, ECO:0000269|PubMed:22922713,
CC ECO:0000269|PubMed:25335890, ECO:0000269|PubMed:26150102,
CC ECO:0000269|PubMed:30014846}.
CC -!- SUBUNIT: Part of BBSome complex, that contains at least bbs-1, bbs-2,
CC bbs-4, bbs-5, osm-12, bbs-8/ttc-8 and bbs-9 (By similarity). Interacts
CC with bbs-1 (PubMed:22922713). {ECO:0000250|UniProtKB:Q8IWZ6,
CC ECO:0000269|PubMed:22922713}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:15231740}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:15231740}. Cytoplasm, cytoskeleton, cilium
CC axoneme {ECO:0000269|PubMed:15231740}. Note=Moves in anterograde and
CC retrograde directions along the ciliary axonemes.
CC {ECO:0000269|PubMed:15231740}.
CC -!- TISSUE SPECIFICITY: Expressed in ciliated cells including amphid and
CC both inner and outer labial neurons of the head and in both phasmid
CC neurons PHA and PHB in the tail at larval stages L1 and L2.
CC {ECO:0000269|PubMed:14520415, ECO:0000269|PubMed:15231740}.
CC -!- DISRUPTION PHENOTYPE: Mutants have normal body morphology, but with
CC reduced body length and width, delayed larval development and decreased
CC roaming movements (PubMed:22022287). May exhibit defective chemotaxis
CC tendencies (PubMed:15231740). Defective cilia structure and function
CC (PubMed:15231740, PubMed:22022287, PubMed:26150102). This is
CC characterized by increased accumulation and mislocalization of
CC intraflagellar transport proteins and impaired movement of
CC intraflagellar transport proteins along the ciliary axoneme
CC (PubMed:15231740, PubMed:22922713, PubMed:26150102). Defective
CC polycystin-mediated cilia signaling and mislocalized and increased
CC accumulation of mechanosensory receptors pkd-2, osm-9 and odr-10 within
CC cilia (PubMed:26150102). Impaired localization of the guanylyl cyclase
CC proteins, gcy-8, gcy-18 and gcy-23, within AFD sensory neurons, with
CC accumulation along the dendrite as well as in the finger compartment of
CC AFD neurons (PubMed:25335890). {ECO:0000269|PubMed:15231740,
CC ECO:0000269|PubMed:22922713, ECO:0000269|PubMed:25335890,
CC ECO:0000269|PubMed:26150102}.
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; BX284603; CAA22100.1; -; Genomic_DNA.
DR PIR; T27399; T27399.
DR RefSeq; NP_499585.1; NM_067184.1.
DR AlphaFoldDB; Q9XW70; -.
DR SMR; Q9XW70; -.
DR ComplexPortal; CPX-428; BBSome complex.
DR DIP; DIP-25936N; -.
DR IntAct; Q9XW70; 3.
DR STRING; 6239.Y75B8A.12; -.
DR PaxDb; Q9XW70; -.
DR PRIDE; Q9XW70; -.
DR EnsemblMetazoa; Y75B8A.12.1; Y75B8A.12.1; WBGene00003892.
DR GeneID; 190704; -.
DR KEGG; cel:CELE_Y75B8A.12; -.
DR UCSC; Y75B8A.12; c. elegans.
DR CTD; 190704; -.
DR WormBase; Y75B8A.12; CE23024; WBGene00003892; osm-12.
DR eggNOG; ENOG502QPS5; Eukaryota.
DR GeneTree; ENSGT00390000012346; -.
DR HOGENOM; CLU_018704_1_0_1; -.
DR InParanoid; Q9XW70; -.
DR OMA; YSGWLTG; -.
DR OrthoDB; 341332at2759; -.
DR PhylomeDB; Q9XW70; -.
DR Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:Q9XW70; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003892; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0034464; C:BBSome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0060271; P:cilium assembly; IMP:WormBase.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0042073; P:intraciliary transport; IMP:WormBase.
DR GO; GO:1905515; P:non-motile cilium assembly; IEP:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1904107; P:protein localization to microvillus membrane; IMP:WormBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR016575; Bardet-Biedl_syndrome_7_prot.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PIRSF; PIRSF011091; BBS7; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Protein transport; Reference proteome; Transport.
FT CHAIN 1..721
FT /note="Bardet-Biedl syndrome 7 protein homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434996"
FT MUTAGEN 233..721
FT /note="Missing: In n1606; results in defective avoidance of
FT nitric oxide and P.aeruginosa."
FT /evidence="ECO:0000269|PubMed:30014846"
FT MUTAGEN 314
FT /note="G->E: In my13; results in cilia with structural
FT defects and increased accumulation of the mechanosensory
FT receptor, pkd-2. Mutants may have slightly altered
FT chemotactic tendencies and have vacuoles in amphid sheath
FT cells."
FT /evidence="ECO:0000269|PubMed:25486278"
SQ SEQUENCE 721 AA; 79889 MW; FFDB5EB3398582A2 CRC64;
MQNYSRTDFA QVGTTNRGCM RVIPSDKEKE HDLIVVGGQN GSLICLSRKS NDTTIIFKTQ
PGYPVQSLAL GGPASSKKKD KIFVASQNTV RGVNRKGKTF FSMETNMAEV ANRMFVRGLD
VVLTGRKSYS RYHDTVDSNS YLCTEDIHDV VSLVFEEAWG SREYTSILAC GNSTLQIIEG
NNFAYDVRLD SVPFTVSLFM GDGGHTKLLV LYGTKTGRLG LVSVPQGGGK ILWEIDTTSG
ACVTTIVCFN VTGGQFPDII VGKEDGLIEI YVIDETDHAH LFGTFSCDES ITGISCGHVS
SKSEIDIIIC TFTGWLFSLA KTSRPMIENL PVAANFSVKM QQLRSEVEEL QTKVNEERLR
YEEITKRQGS GTGSTFFHSF QVHENFEYSA AHGAYNLTIE LVIPIDFVVV QSQLPIRLME
VEKNASVVSE VRQDALNPWP LLASYRCQAN VCRLELRVQA NEGDSGVINL YVCPKVMPKC
AQITTHYIKA LSSHMRSHDF DLYRPMNTLQ FTGNFSIAEA HAWLHNLLPN VPSKCPPADT
ITNNYQCSVN GGTQLQVVYS KGSAVFRSDC MTTICIIRDK VSEQTMKMQI RVEVACELNQ
DSVNHCLKLI DPKITSMLNI EKNKLYAAAL KELESNNDDV FSFLSAANAK ILKDHDAIYE
KSEGVSIEDS GVLAILENLM VARGKLTGRS SKGRGDAIRD LISTDYSLEN MQTLFKNAMN
D
