BBS2_CAEEL
ID BBS2_CAEEL Reviewed; 714 AA.
AC Q19640;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Bardet-Biedl syndrome 2 protein homolog {ECO:0000312|WormBase:F20D12.3};
GN Name=bbs-2 {ECO:0000312|WormBase:F20D12.3};
GN ORFNames=F20D12.3 {ECO:0000312|WormBase:F20D12.3};
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, 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).
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. The BBSome complex
CC is required for ciliogenesis but is dispensable for centriolar
CC satellite function (By similarity). Required for proper BBSome complex
CC assembly and its ciliary localization (PubMed:22922713). Required for
CC cilia biogenesis and both the assembly and movement of intraflagellar
CC transport proteins along the ciliary axoneme (PubMed:15231740,
CC PubMed:22022287, PubMed:22922713). {ECO:0000250|UniProtKB:Q9BXC9,
CC ECO:0000269|PubMed:15231740, ECO:0000269|PubMed:22022287,
CC 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.
CC {ECO:0000250|UniProtKB:Q9BXC9}.
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 (PubMed:22022287). Defective cilia structure and
CC function (PubMed:22022287). Disrupted assembly of the BBSome complex at
CC the base of the cilia (PubMed:22922713). {ECO:0000269|PubMed:22022287,
CC ECO:0000269|PubMed:22922713}.
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DR EMBL; BX284604; CCD67718.2; -; Genomic_DNA.
DR PIR; T16109; T16109.
DR RefSeq; NP_501325.2; NM_068924.2.
DR AlphaFoldDB; Q19640; -.
DR SMR; Q19640; -.
DR ComplexPortal; CPX-428; BBSome complex.
DR STRING; 6239.F20D12.3; -.
DR PaxDb; Q19640; -.
DR EnsemblMetazoa; F20D12.3.1; F20D12.3.1; WBGene00000242.
DR GeneID; 259580; -.
DR KEGG; cel:CELE_F20D12.3; -.
DR UCSC; F20D12.3; c. elegans.
DR CTD; 259580; -.
DR WormBase; F20D12.3; CE49510; WBGene00000242; bbs-2.
DR eggNOG; ENOG502QPWU; Eukaryota.
DR GeneTree; ENSGT00390000017113; -.
DR HOGENOM; CLU_023359_0_0_1; -.
DR InParanoid; Q19640; -.
DR OMA; IKVDEYH; -.
DR OrthoDB; 327831at2759; -.
DR Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:Q19640; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000242; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0034464; C:BBSome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; IEP:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR016616; Bardet-Biedl_syndrome_2_prot.
DR InterPro; IPR029333; BBS2_C.
DR InterPro; IPR029429; BBS2_Mid.
DR InterPro; IPR029430; BBS2_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR32465; PTHR32465; 1.
DR Pfam; PF14782; BBS2_C; 1.
DR Pfam; PF14783; BBS2_Mid; 1.
DR Pfam; PF14781; BBS2_N; 1.
DR PIRSF; PIRSF013684; BBS2; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Protein transport; Reference proteome; Transport.
FT CHAIN 1..714
FT /note="Bardet-Biedl syndrome 2 protein homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434995"
FT COILED 332..361
FT /evidence="ECO:0000255"
FT COILED 597..627
FT /evidence="ECO:0000255"
SQ SEQUENCE 714 AA; 80950 MW; BDF0F4B94EEC2ED6 CRC64;
MDGDRTPEEQ IEIAESDQGP QLDDNVELAN VFSYSLDQRI MEGCVISAIL EPRGLETIVA
VSVTNKIIIK DKETSLNITE TIRCIAAAPF GDGYDCIIIG TDSSVICYDV HNNLTVFRND
VPDGVSCFVY GKLGELDEAI YCGGNCCIWG FDKTGANTYW TVTGDQVTTM CLSDYDNDGE
TELVIGSPDF EIRVFKNDLM RTELMETDEI TCLAHVANGC FAYSLNNGTI GTYVLKERQW
RIKSKSNVSK IFNFEEEGLM VVVWKQGKVD LRFAHNGEVL SRDSVSSHVA SASVSKKGDE
SFITVVCLDG KVKGFKIQRA QNGSIDKTQQ LIREFGQKKH NLMMELSNYE QEEQLADVEK
DRDFRIPVDT EVAVVFVVNT ELQLLSLRVE ASHNIPIRGV LIFAEGLFEG ESYIWIPPNE
YQSRSVIDIP LVIDKDSTND LHTKVFLGQV DSNKLMVMEN TRILPKFCRF TLLREEYSKF
FYMPTAYIQF DINSRAAKLS EWVQESFTID ASLVEMFDEP EGEFKFMGLR PKHEKSLMFK
ISHSEKTCKI YHDKIETMGA IVQSYASFYQ IQNMESVAHF PDVFKEADEI LEEIDPMTEV
RDRLTAELQE RQAAVKEIII RAEDSIAIDN IPDARKFYIR LKANDAAARQ AAQLRWNNQE
RCVKSLRRLN KIIENCSRLR VGEPGRQIVV SCRSAIADDN KQIITKILQY GASV
