BBS1_CAEEL
ID BBS1_CAEEL Reviewed; 576 AA.
AC Q9NEZ7;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Bardet-Biedl syndrome 1 protein homolog {ECO:0000312|WormBase:Y105E8A.5};
GN Name=bbs-1 {ECO:0000312|WormBase:Y105E8A.5};
GN ORFNames=Y105E8A.5 {ECO:0000312|WormBase:Y105E8A.5};
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, AND TISSUE SPECIFICITY.
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] {ECO:0000305}
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 [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BBS-7 AND BBS-9, AND MUTAGENESIS OF GLY-207.
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).
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 (PubMed:22922713).
CC Required for cilia biogenesis and both the assembly and movement of
CC intraflagellar transport proteins along the ciliary axoneme
CC (PubMed:15231740, PubMed:22022287, PubMed:22922713).
CC {ECO:0000250|UniProtKB:Q8NFJ9, ECO:0000269|PubMed:15231740,
CC ECO:0000269|PubMed:22022287, ECO:0000269|PubMed:22922713}.
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-7 and bbs-9 (PubMed:22922713). {ECO:0000250|UniProtKB:Q8NFJ9,
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}.
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. Defective cilia structure and function.
CC {ECO:0000269|PubMed:22022287}.
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DR EMBL; BX284601; CAC48119.1; -; Genomic_DNA.
DR RefSeq; NP_740933.1; NM_170937.1.
DR AlphaFoldDB; Q9NEZ7; -.
DR SMR; Q9NEZ7; -.
DR ComplexPortal; CPX-428; BBSome complex.
DR DIP; DIP-61854N; -.
DR IntAct; Q9NEZ7; 3.
DR STRING; 6239.Y105E8A.5; -.
DR PaxDb; Q9NEZ7; -.
DR EnsemblMetazoa; Y105E8A.5.1; Y105E8A.5.1; WBGene00000241.
DR GeneID; 260219; -.
DR KEGG; cel:CELE_Y105E8A.5; -.
DR UCSC; Y105E8A.5; c. elegans.
DR CTD; 260219; -.
DR WormBase; Y105E8A.5; CE25181; WBGene00000241; bbs-1.
DR eggNOG; ENOG502QS2X; Eukaryota.
DR GeneTree; ENSGT00390000005232; -.
DR HOGENOM; CLU_032988_1_0_1; -.
DR InParanoid; Q9NEZ7; -.
DR OMA; AMLYGRM; -.
DR OrthoDB; 783386at2759; -.
DR PhylomeDB; Q9NEZ7; -.
DR Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:Q9NEZ7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000241; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005930; C:axoneme; IDA:WormBase.
DR GO; GO:0034464; C:BBSome; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0005113; F:patched binding; IBA:GO_Central.
DR GO; GO:0005119; F:smoothened binding; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IC:ComplexPortal.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IEP:BHF-UCL.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR028784; BBS1.
DR InterPro; IPR032728; BBS1_N.
DR PANTHER; PTHR20870; PTHR20870; 1.
DR Pfam; PF14779; BBS1; 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..576
FT /note="Bardet-Biedl syndrome 1 protein homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434994"
FT MUTAGEN 207
FT /note="G->D: In ju598; impaired movement of intraflagellar
FT transport proteins along the ciliary axoneme and
FT accumulation of intraflagellar protein-B at the ciliary
FT tip. Accumulation of all BBSome proteins around the ciliary
FT base."
FT /evidence="ECO:0000269|PubMed:22922713"
SQ SEQUENCE 576 AA; 64552 MW; 3C1896F2AA12A176 CRC64;
MAKPVNVNQS KWTVPVLLKE CEIYCPSTCV AFGPILSDND SKLIIAHGGH RGVNMKLKVF
QQLEQLSESS LADMPTALVH FINDLSSIPS IAVAAGPSLL IYKNLKPFYK FTVPSSAINP
TESEAWKAVV NKKINGDTLL TVLKRLEDDV AFSKLTPISQ TYLRADKETQ VVLVEHYGTK
IANSATITCI AKLTKSTAEP LDILVIGTEH CEIFLIDSQA FTILETIKIG SVPVNICAYG
TYDVDYRLFV QTRASLIFCM KRGEADYQPI VISQSMITSM VLVNKMIVYT TVENLIHFAS
FRGKKMNTVK CPSKIKMLEP FIYPLKQLAA VIAVFDKEIR MYNEHYLLDT VQYEKPLAWV
KYGCYGREDS TLVVAFKDGS IAIQIFRRKA NFDTKLDYNQ VPQAHALKLQ IPKKTKVFID
LTQREVQLGN RIHKVYQKNL FDVKYRLAAS YLELTSSASA TVSTTTVLPV EISVDIHGFG
PTFRMTIHLL SSSKQNLYDM HLSIISDPEL YDFDTPLIPV HLLASGQSYS FTTLLYCKDP
EKAANCDVRA LLVHAKRATP IVTAVIKMPF SEFPLD
