BBS4_CAEEL
ID BBS4_CAEEL Reviewed; 462 AA.
AC Q5CZ52; G3MTX0; G3MTX1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Bardet-Biedl syndrome 4 protein homolog;
GN Name=bbs-4 {ECO:0000312|WormBase:F58A4.14a};
GN ORFNames=F58A4.14 {ECO:0000312|WormBase:F58A4.14a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
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]
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]
RP FUNCTION, INTERACTION WITH BBS-5, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLU-107 AND ALA-388.
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 proper
CC BBSome complex assembly and its ciliary localization (By similarity).
CC May be required for microtubule anchoring at the centrosome but not for
CC microtubule nucleation (By similarity). May be required for the dynein-
CC mediated transport of pericentriolar proteins to the centrosome (By
CC similarity). Required, redundantly with bbs-5, for cilia biogenesis and
CC 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:Q96RK4,
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 (via C-terminus) with bbs-5; the interaction is direct
CC (PubMed:26150102). {ECO:0000250|UniProtKB:Q96RK4,
CC ECO:0000269|PubMed:26150102}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q5CZ52-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q5CZ52-2; Sequence=VSP_044208;
CC -!- DISRUPTION PHENOTYPE: Single mutants do not display any obvious defects
CC in ciliogenesis. Double bbs-4 and bbs-5 mutants display a defect in
CC cilia structure and function. This is characterized by an 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 BBS4 family. {ECO:0000305}.
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DR EMBL; Z22179; CCD31085.1; -; Genomic_DNA.
DR EMBL; Z22179; CCD31086.1; -; Genomic_DNA.
DR RefSeq; NP_001255013.1; NM_001268084.1. [Q5CZ52-1]
DR RefSeq; NP_001255014.1; NM_001268085.1. [Q5CZ52-2]
DR AlphaFoldDB; Q5CZ52; -.
DR SMR; Q5CZ52; -.
DR BioGRID; 532999; 1.
DR ComplexPortal; CPX-428; BBSome complex.
DR STRING; 6239.F58A4.14a; -.
DR PaxDb; Q5CZ52; -.
DR EnsemblMetazoa; F58A4.14a.1; F58A4.14a.1; WBGene00043992. [Q5CZ52-1]
DR EnsemblMetazoa; F58A4.14b.1; F58A4.14b.1; WBGene00043992. [Q5CZ52-2]
DR GeneID; 3565681; -.
DR KEGG; cel:CELE_F58A4.14; -.
DR UCSC; F58A4.14; c. elegans. [Q5CZ52-1]
DR CTD; 3565681; -.
DR WormBase; F58A4.14a; CE46408; WBGene00043992; bbs-4. [Q5CZ52-1]
DR WormBase; F58A4.14b; CE46292; WBGene00043992; bbs-4. [Q5CZ52-2]
DR eggNOG; KOG1124; Eukaryota.
DR HOGENOM; CLU_033477_0_0_1; -.
DR InParanoid; Q5CZ52; -.
DR OMA; WNNIGAC; -.
DR OrthoDB; 609083at2759; -.
DR PhylomeDB; Q5CZ52; -.
DR Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:Q5CZ52; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00043992; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0034464; C:BBSome; IC:ComplexPortal.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR028786; BBS4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44186; PTHR44186; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Membrane;
KW Protein transport; Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..462
FT /note="Bardet-Biedl syndrome 4 protein homolog"
FT /id="PRO_0000284044"
FT REPEAT 89..122
FT /note="TPR 1"
FT REPEAT 124..156
FT /note="TPR 2"
FT REPEAT 199..232
FT /note="TPR 3"
FT REPEAT 234..266
FT /note="TPR 4"
FT REPEAT 268..300
FT /note="TPR 5"
FT REPEAT 335..368
FT /note="TPR 6"
FT REPEAT 369..402
FT /note="TPR 7"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044208"
FT MUTAGEN 107
FT /note="E->Q: No obvious phenotype."
FT /evidence="ECO:0000269|PubMed:26150102"
FT MUTAGEN 388
FT /note="A->E: Abolishes interaction with bbs-5. Unable to
FT target to cilia."
FT /evidence="ECO:0000269|PubMed:26150102"
SQ SEQUENCE 462 AA; 51511 MW; AA118C49CA2CC9F4 CRC64;
MEASNQDEII GTDVIPNEQD NPEEVVPEPT SLDVPPPPPE RAPSAPKRVE ILDCNSLNGL
MYHYFAQGDY IECKSIIGEI QSKYLERNEA AFHVRGLIAR NEGELEEAME CFHKAYELSG
KNKRYFYETG RCNFLLGRHQ IAVEQLTKAS EVMKDNPKVW YWLARAIYHF PAEKVQGKTF
NPVESARTIL MKPDIAKDAT LICFLGRLCE ELGDTSGAIA AYKSSLKLQP DNTEVMNLLG
LIYLRTGQVQ EGFVQLGNCL AYDPANSQAI LTIGSIMQNH SDHDVALNKY RVAADVSDYN
GCLWNNIGIG LLARNKPAAS HSALKKAAFI NPLNYKISYN LGVLHDIMNL HCSALHYIKL
CTELYPQNAK AVGAMAVILS HMNDDKNARL AYKKSIELKK NPSTILNYAI FEYRMKDVTA
ASNALKLYKD LQASGVKCSA NNKETANLLE SVLKQPDQSA EQ
