BBS2_RAT
ID BBS2_RAT Reviewed; 721 AA.
AC Q99MH9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bardet-Biedl syndrome 2 protein homolog;
GN Name=Bbs2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=11285252; DOI=10.1093/hmg/10.8.865;
RA Nishimura D.Y., Searby C.C., Carmi R., Elbedour K., Van Maldergem L.,
RA Fulton A.B., Lam B.L., Powell B.R., Swiderski R.E., Bugge K.E.,
RA Haider N.B., Kwitek-Black A.E., Ying L., Duhl D.M., Gorman S.M., Heon E.,
RA Iannaccone A., Bonneau D., Biesecker L.G., Jacobson S.G., Stone E.M.,
RA Sheffield V.C.;
RT "Positional cloning of a novel gene on chromosome 16q causing Bardet-Biedl
RT syndrome (BBS2).";
RL Hum. Mol. Genet. 10:865-874(2001).
CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC required for sorting of specific membrane proteins to the primary
CC cilia. The BBSome complex is required for ciliogenesis but is
CC dispensable for centriolar satellite function. This ciliogenic function
CC is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC the primary cilium and promotes extension of the ciliary membrane.
CC Firstly the BBSome associates with the ciliary membrane and binds to
CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC carrier vesicles to the base of the ciliary membrane. The BBSome
CC complex, together with the LTZL1, controls SMO ciliary trafficking and
CC contributes to the sonic hedgehog (SHH) pathway regulation. Required
CC for proper BBSome complex assembly and its ciliary localization (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus) with BBS7.
CC Interacts (via coiled coil domain) with MKKS. Interacts with CCDC28B
CC (By similarity). Interacts with DLEC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXC9}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite {ECO:0000250}.
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DR EMBL; AF342738; AAK28554.1; -; mRNA.
DR RefSeq; NP_446070.1; NM_053618.1.
DR AlphaFoldDB; Q99MH9; -.
DR SMR; Q99MH9; -.
DR STRING; 10116.ENSRNOP00000026076; -.
DR iPTMnet; Q99MH9; -.
DR PhosphoSitePlus; Q99MH9; -.
DR PaxDb; Q99MH9; -.
DR PRIDE; Q99MH9; -.
DR Ensembl; ENSRNOT00000026076; ENSRNOP00000026076; ENSRNOG00000019020.
DR GeneID; 113948; -.
DR KEGG; rno:113948; -.
DR UCSC; RGD:71091; rat.
DR CTD; 583; -.
DR RGD; 71091; Bbs2.
DR eggNOG; ENOG502QPWU; Eukaryota.
DR GeneTree; ENSGT00390000017113; -.
DR HOGENOM; CLU_023359_0_0_1; -.
DR InParanoid; Q99MH9; -.
DR OMA; IKVDEYH; -.
DR OrthoDB; 327831at2759; -.
DR PhylomeDB; Q99MH9; -.
DR TreeFam; TF313236; -.
DR Reactome; R-RNO-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:Q99MH9; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019020; Expressed in testis and 20 other tissues.
DR Genevisible; Q99MH9; RN.
DR GO; GO:0034464; C:BBSome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0031514; C:motile cilium; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0032420; C:stereocilium; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0014824; P:artery smooth muscle contraction; ISO:RGD.
DR GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0033365; P:protein localization to organelle; ISO:RGD.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISO:RGD.
DR GO; GO:0044321; P:response to leptin; ISO:RGD.
DR GO; GO:0007288; P:sperm axoneme assembly; ISO:RGD.
DR GO; GO:0021756; P:striatum development; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; ISO:RGD.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
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; 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 membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..721
FT /note="Bardet-Biedl syndrome 2 protein homolog"
FT /id="PRO_0000064845"
FT COILED 325..369
FT /evidence="ECO:0000255"
SQ SEQUENCE 721 AA; 79918 MW; 55935DE19C0509DC CRC64;
MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQAGKV FIHNPHMRSQ HFSTSRVFQS
PLESDVSLLN INQTVSCLGA GVLNPELGYD TLLVGTQTSL LAYDIYNNSD LFYREVADGA
NALVLGTLGD IAPPLAIIGG NCALQGFDHE GNDLFWTVTG DNVHSLALCD FDGDGKSELL
VGSEDFDIRV FKEDEIVAEM TETEIVTSLC PMYGSRFGYA LSNGTVGVYD KTARYWRIKS
KNHAMSIHAF DINSDGVCEL ITGWSNGKVD ARSDRTGEVI FKDNFSSAVA GVVEGDYRMD
GHVQLICCSV DGEIRGYLPG TAEMKGNLLD TSVEQGLIRE LSQKKQNLLL ELRNYEENTK
AELSSPLNEA DGQKGIIPAN TKLHTALSVN LGNDAQDAHA ELRISTSNDT IIRAVLIFAE
GIFAGESHVV HPSTHNLSSS IRVPITPPKD VPVDLHLKTF VGYRSSTQFH VFELIRQLPR
FTMYALTSPD AASEPVSFVN FIVVERAQRM VTWLNQNFLL PEDSNIQNAP FHVCFTSLRN
GGQLYIKMKP SGEITVNTDD IDLAGDIIQS MASFFAIEDL QVEADFPVYF EELRKVLLKV
DEYHSVHQKL SANMADNSNL IRSLLVRAED ARLMRDMKTM KTRYMELYDL NKDLLNGYKI
RCNNHTELLG NLKAVNQAIQ RAGRLRVGKP KNQVISACRD AIRSNNINTL FRIMRVGTAP
S
