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Bardet-Biedl syndrome 4 protein homolog

 BBS4_MOUSE              Reviewed;         520 AA.
Q8C1Z7; Q3UYF0; Q562E1; Q5EBJ7; Q8CA57;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-APR-2018, entry version 134.
RecName: Full=Bardet-Biedl syndrome 4 protein homolog;
Name=Bbs4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12016587; DOI=10.1086/341031;
Katsanis N., Eichers E.R., Ansley S.J., Lewis R.A., Kayserili H.,
Hoskins B.E., Scambler P.J., Beales P.L., Lupski J.R.;
"BBS4 is a minor contributor to Bardet-Biedl syndrome and may also
participate in triallelic inheritance.";
Am. J. Hum. Genet. 71:22-29(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15107855; DOI=10.1038/ng1352;
Kim J.C., Badano J.L., Sibold S., Esmail M.A., Hill J., Hoskins B.E.,
Leitch C.C., Venner K., Ansley S.J., Ross A.J., Leroux M.R.,
Katsanis N., Beales P.L.;
"The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar
region and is required for microtubule anchoring and cell cycle
progression.";
Nat. Genet. 36:462-470(2004).
[5]
DISRUPTION PHENOTYPE.
PubMed=18317593; DOI=10.1172/JCI32357;
Rahmouni K., Fath M.A., Seo S., Thedens D.R., Berry C.J., Weiss R.,
Nishimura D.Y., Sheffield V.C.;
"Leptin resistance contributes to obesity and hypertension in mouse
models of Bardet-Biedl syndrome.";
J. Clin. Invest. 118:1458-1467(2008).
[6]
IDENTIFICATION IN THE BBSOME COMPLEX, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
Sheffield V.C.;
"A novel protein LZTFL1 regulates ciliary trafficking of the BBSome
and Smoothened.";
PLoS Genet. 7:E1002358-E1002358(2011).
[7]
SUBCELLULAR LOCATION.
PubMed=23943788; DOI=10.1093/hmg/ddt394;
Zhang Y., Seo S., Bhattarai S., Bugge K., Searby C.C., Zhang Q.,
Drack A.V., Stone E.M., Sheffield V.C.;
"BBS mutations modify phenotypic expression of CEP290-related
ciliopathies.";
Hum. Mol. Genet. 23:40-51(2014).
[8]
INTERACTION WITH C2CD3.
PubMed=24469809; DOI=10.1073/pnas.1318737111;
Ye X., Zeng H., Ning G., Reiter J.F., Liu A.;
"C2cd3 is critical for centriolar distal appendage assembly and
ciliary vesicle docking in mammals.";
Proc. Natl. Acad. Sci. U.S.A. 111:2164-2169(2014).
-!- FUNCTION: The BBSome complex is thought to function as a coat
complex required for sorting of specific membrane proteins to the
primary cilia. The BBSome complex is required for ciliogenesis but
is dispensable for centriolar satellite function. This ciliogenic
function is mediated in part by the Rab8 GDP/GTP exchange factor,
which localizes to the basal body and contacts the BBSome.
Rab8(GTP) enters the primary cilium and promotes extension of the
ciliary membrane. Firstly the BBSome associates with the ciliary
membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor
(GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and
promotes docking and fusion of carrier vesicles to the base of the
ciliary membrane. The BBSome complex, together with the LTZL1,
controls SMO ciliary trafficking and contributes to the sonic
hedgehog (SHH) pathway regulation. Required for proper BBSome
complex assembly and its ciliary localization. Required for
microtubule anchoring at the centrosome but not for microtubule
nucleation. May be required for the dynein-mediated transport of
pericentriolar proteins to the centrosome (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4,
BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with PCM1 and
DCTN1. Interacts with DC28B. Interacts with ALDOB and C2CD3.
Interacts with PKD1 (By similarity). Interacts with CEP290 (By
similarity). {ECO:0000250|UniProtKB:Q96RK4,
ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:24469809}.
-!- INTERACTION:
Q3V3N7:Bbs1; NbExp=5; IntAct=EBI-2892887, EBI-2892836;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Cell projection,
cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome,
centriolar satellite {ECO:0000250}. Cell projection, cilium,
flagellum {ECO:0000269|PubMed:15107855,
ECO:0000269|PubMed:22072986}. Cell projection, cilium
{ECO:0000269|PubMed:23943788}. Note=Localizes to the
pericentriolar material. Centrosomal localization requires dynein
(By similarity). Localizes to the connecting cilium of
photoreceptor cells (PubMed:23943788).
-!- TISSUE SPECIFICITY: Expressed in the hippocampus and dentate
gyrus, the columnar epithelial cells of bronchioles, the olfactory
epithelium and the inner segment and outer nuclear layer of the
retina. Expressed in testis. {ECO:0000269|PubMed:15107855,
ECO:0000269|PubMed:22072986}.
-!- DEVELOPMENTAL STAGE: Expressed in the pericardium of the
developing embryo and in the epidermal layer surrounding the
digits. {ECO:0000269|PubMed:15107855}.
-!- DISRUPTION PHENOTYPE: Males are sterile due to a loss of sperm
flagella. In mice obesity is associated with hyperleptinemia and
resistance to the anorectic and weight-reducing effects of leptin.
Although mice are resistant to the metabolic actions of leptin,
animals remain responsive to the effects of leptin on renal
sympathetic nerve activity and arterial pressure and developed
hypertension. BBS mice have decreased hypothalamic expression of
proopiomelanocortin (POMC). BBS genes play an important role in
maintaining leptin sensitivity in POMC neurons.
{ECO:0000269|PubMed:18317593, ECO:0000269|PubMed:22072986}.
-!- SIMILARITY: Belongs to the BBS4 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK039560; BAC30384.1; -; mRNA.
EMBL; AK089970; BAC41021.1; -; mRNA.
EMBL; AK134734; BAE22262.1; -; mRNA.
EMBL; BC055797; AAH55797.1; -; mRNA.
EMBL; BC089507; AAH89507.1; ALT_TERM; mRNA.
EMBL; BC092531; AAH92531.1; ALT_TERM; mRNA.
CCDS; CCDS40658.1; -.
RefSeq; NP_780534.1; NM_175325.3.
UniGene; Mm.200714; -.
ProteinModelPortal; Q8C1Z7; -.
SMR; Q8C1Z7; -.
BioGrid; 221946; 3.
DIP; DIP-60352N; -.
IntAct; Q8C1Z7; 5.
STRING; 10090.ENSMUSP00000026265; -.
iPTMnet; Q8C1Z7; -.
PhosphoSitePlus; Q8C1Z7; -.
MaxQB; Q8C1Z7; -.
PaxDb; Q8C1Z7; -.
PRIDE; Q8C1Z7; -.
Ensembl; ENSMUST00000026265; ENSMUSP00000026265; ENSMUSG00000025235.
GeneID; 102774; -.
KEGG; mmu:102774; -.
UCSC; uc009pxr.2; mouse.
CTD; 585; -.
MGI; MGI:2143311; Bbs4.
eggNOG; KOG1124; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00530000063455; -.
HOGENOM; HOG000261391; -.
HOVERGEN; HBG024456; -.
InParanoid; Q8C1Z7; -.
KO; K16531; -.
OMA; INFQPKM; -.
OrthoDB; EOG091G09T3; -.
PhylomeDB; Q8C1Z7; -.
TreeFam; TF324966; -.
Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
PRO; PR:Q8C1Z7; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000025235; -.
CleanEx; MM_BBS4; -.
ExpressionAtlas; Q8C1Z7; baseline and differential.
Genevisible; Q8C1Z7; MM.
GO; GO:0034464; C:BBSome; IDA:MGI.
GO; GO:0034451; C:centriolar satellite; IDA:MGI.
GO; GO:0005814; C:centriole; ISO:MGI.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0036064; C:ciliary basal body; ISO:MGI.
GO; GO:0060170; C:ciliary membrane; ISO:MGI.
GO; GO:0035869; C:ciliary transition zone; ISO:MGI.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0031514; C:motile cilium; IMP:BHF-UCL.
GO; GO:0097730; C:non-motile cilium; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:GOC.
GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
GO; GO:0034452; F:dynactin binding; ISO:MGI.
GO; GO:0003777; F:microtubule motor activity; ISS:UniProtKB.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:MGI.
GO; GO:0030534; P:adult behavior; IMP:MGI.
GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL.
GO; GO:0016358; P:dendrite development; IMP:MGI.
GO; GO:0060324; P:face development; IMP:MGI.
GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
GO; GO:0060613; P:fat pad development; IMP:MGI.
GO; GO:0021766; P:hippocampus development; IMP:MGI.
GO; GO:0033210; P:leptin-mediated signaling pathway; IMP:MGI.
GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
GO; GO:0034454; P:microtubule anchoring at centrosome; ISO:MGI.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:MGI.
GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0034260; P:negative regulation of GTPase activity; IMP:MGI.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:MGI.
GO; GO:0045724; P:positive regulation of cilium assembly; IMP:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
GO; GO:0061512; P:protein localization to cilium; ISO:MGI.
GO; GO:0033365; P:protein localization to organelle; IDA:BHF-UCL.
GO; GO:1903546; P:protein localization to photoreceptor outer segment; IMP:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IMP:BHF-UCL.
GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
GO; GO:1902855; P:regulation of non-motile cilium assembly; IMP:MGI.
GO; GO:0051492; P:regulation of stress fiber assembly; IMP:MGI.
GO; GO:0044321; P:response to leptin; IMP:MGI.
GO; GO:0001895; P:retina homeostasis; IMP:MGI.
GO; GO:0046548; P:retinal rod cell development; IMP:MGI.
GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
GO; GO:0035176; P:social behavior; IMP:MGI.
GO; GO:0007286; P:spermatid development; IMP:MGI.
GO; GO:0021756; P:striatum development; IMP:MGI.
GO; GO:0021591; P:ventricular system development; IMP:MGI.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
Pfam; PF13181; TPR_8; 2.
SMART; SM00028; TPR; 8.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50005; TPR; 8.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
Complete proteome; Cytoplasm; Cytoskeleton; Flagellum; Membrane;
Protein transport; Reference proteome; Repeat; TPR repeat; Transport.
CHAIN 1 520 Bardet-Biedl syndrome 4 protein homolog.
/FTId=PRO_0000106264.
REPEAT 67 100 TPR 1.
REPEAT 102 134 TPR 2.
REPEAT 135 167 TPR 3.
REPEAT 168 201 TPR 4.
REPEAT 203 235 TPR 5.
REPEAT 237 269 TPR 6.
REPEAT 270 303 TPR 7.
REPEAT 304 337 TPR 8.
REPEAT 339 371 TPR 9.
REPEAT 373 408 TPR 10.
REGION 1 66 Required for localization to centrosomes.
{ECO:0000250}.
REGION 101 337 Interaction with PCM1. {ECO:0000250}.
REGION 338 520 Required for localization to centrosomes.
{ECO:0000250}.
CONFLICT 515 515 E -> V (in Ref. 3; AAH92531).
{ECO:0000305}.
SEQUENCE 520 AA; 58255 MW; 70640E41509F2479 CRC64;
MAEVKLGMKT QVPASVESQK PRSKKAPDFP IVEKQNWLIH LHYIRKDYEA CKAVIKEQLQ
ETQGLCEYAI YVQALIFRLE GNIQESLELF QTCAVLSPQC ADNLKQVARS LFLLGKHKAA
TEVYNEAAKL NQKDWEICHN LGVCYTYLKQ FNKAQDQLHS ALQLNKHDLT YIMLGKIHLL
QGDLDKAIEI YKKAVEFSPE NTELLTTLGL LYLQLGVYQK AFEHLGNALT YDPANYKAIL
AAGSMMQTHG DFDVALTKYR VVACAIPESP PLWNNIGMCF FGKKKYVAAI SCLKRANYLA
PFDWKILYNL GLVHLTMQQY ASAFHFLSAA INFQPKMGEL YMLLAVALTN LEDIENARRA
YVEAVRLDKC NPLVNLNYAV LLYNQGEKKS ALAQYQEMEK KVNFLKDNSP LEFDSEMVEM
AQKLGAALQV GEALVWTKPV KDPKTKHRTN SGSKSATLQQ PLGSIQALGQ AMSSAAAYRK
ILSGAVGAQL PKPPSLPLEP EPEPTVEASP TEASEQKKEK


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