BBS5_CAEEL
ID BBS5_CAEEL Reviewed; 361 AA.
AC Q21626;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Bardet-Biedl syndrome 5 protein homolog {ECO:0000312|WormBase:R01H10.6};
GN Name=bbs-5 {ECO:0000312|WormBase:R01H10.6};
GN ORFNames=R01H10.6 {ECO:0000312|WormBase:R01H10.6};
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 FUNCTION.
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 [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BBS-4, 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).
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 BBSome
CC complex ciliary localization but not for the proper complex assembly
CC (By similarity). Required, redundantly with bbs-4, for cilia biogenesis
CC and both the assembly and movement of intraflagellar transport proteins
CC along the ciliary axoneme (PubMed:22922713, PubMed:26150102). Plays a
CC role in the removal of degraded mechanosensory receptors within the
CC cilia (PubMed:26150102). {ECO:0000250|UniProtKB:Q8N3I7,
CC ECO:0000269|PubMed:22922713, ECO:0000269|PubMed:26150102}.
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-4 (via C-terminus); the interaction is direct
CC (PubMed:26150102). {ECO:0000250|UniProtKB:Q8N3I7,
CC ECO:0000269|PubMed:26150102}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:Q8N3I7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8N3I7}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q9CZQ9}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q8N3I7}. Note=Localizes to basal bodies.
CC {ECO:0000250|UniProtKB:Q9CZQ9}.
CC -!- DISRUPTION PHENOTYPE: Single mutants do not display any obvious defects
CC in ciliogenesis. Double bbs-5 and bbs-4 mutants display a defect in
CC cilia structure and function. This is characterized by increased
CC accumulation and mislocalization of intraflagellar transport proteins
CC and impaired movement of intraflagellar transport proteins along the
CC ciliary axoneme. Double mutants also have defective polycystin-mediated
CC cilia signaling and mislocalized and increased accumulation of
CC mechanosensory receptors pkd-2, osm-9 and odr-10 within cilia.
CC {ECO:0000269|PubMed:26150102}.
CC -!- SIMILARITY: Belongs to the BBS5 family. {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; BX284603; CAA83463.1; -; Genomic_DNA.
DR PIR; E88577; E88577.
DR PIR; S43569; S43569.
DR RefSeq; NP_499272.1; NM_066871.1.
DR AlphaFoldDB; Q21626; -.
DR SMR; Q21626; -.
DR ComplexPortal; CPX-428; BBSome complex.
DR DIP; DIP-25246N; -.
DR IntAct; Q21626; 3.
DR STRING; 6239.R01H10.6; -.
DR EPD; Q21626; -.
DR PaxDb; Q21626; -.
DR EnsemblMetazoa; R01H10.6.1; R01H10.6.1; WBGene00010974.
DR GeneID; 187516; -.
DR KEGG; cel:CELE_R01H10.6; -.
DR UCSC; R01H10.6; c. elegans.
DR CTD; 187516; -.
DR WormBase; R01H10.6; CE01042; WBGene00010974; bbs-5.
DR eggNOG; ENOG502QR2Z; Eukaryota.
DR GeneTree; ENSGT00390000002753; -.
DR HOGENOM; CLU_052113_0_0_1; -.
DR InParanoid; Q21626; -.
DR OMA; PNFGIQY; -.
DR OrthoDB; 1257336at2759; -.
DR PhylomeDB; Q21626; -.
DR Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:Q21626; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010974; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0034464; C:BBSome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR006606; BBL5.
DR InterPro; IPR030804; BBS5/fem-3.
DR InterPro; IPR014003; DM16_repeat.
DR PANTHER; PTHR21351; PTHR21351; 1.
DR Pfam; PF07289; BBL5; 1.
DR PIRSF; PIRSF010072; DUF1448; 1.
DR SMART; SM00683; DM16; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..361
FT /note="Bardet-Biedl syndrome 5 protein homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435350"
SQ SEQUENCE 361 AA; 41054 MW; E6FD8532A73E3698 CRC64;
MERVNGEDIW QDREIRFDVD HKLLRLINGE IQVAKIEHVE DTKGNNGDRG TMRVTNLRLI
WHAASMPRIN ITIGWNAITG VQSKQTTSLV TRNRGISNEA IYVLAKVSAT TTKFEFIFTT
TNPASHSKLF NTISSISRAY ETTKMYRELK MRGVFIREDG TLKILPQETI IEKVNGVWNL
STETGSLGVF VITNIRVVWY AEMNIGYNVS VPYITLYSVR VRESKFGMAL VLETTTSSGE
YVLGFRVDPA ERLQNLLKTV QSLHKAHLLK PIFGVSYVKE IAEKVEPRKD DDEIDIIDNN
EDDVEIDDKI RPDAFASYFD GEHTATDEKQ LPVLNPELGL AIEPIRNGFT LHDLWNIHVD
V
