B9D2_MOUSE
ID B9D2_MOUSE Reviewed; 175 AA.
AC Q3UK10; Q8R045;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=B9 domain-containing protein 2;
DE AltName: Full=Stumpy;
GN Name=B9d2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH TUBG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18287022; DOI=10.1073/pnas.0712385105;
RA Town T., Breunig J.J., Sarkisian M.R., Spilianakis C., Ayoub A.E., Liu X.,
RA Ferrandino A.F., Gallagher A.R., Li M.O., Rakic P., Flavell R.A.;
RT "The stumpy gene is required for mammalian ciliogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2853-2858(2008).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH MKS1 AND B9D1.
RX PubMed=21763481; DOI=10.1016/j.ajhg.2011.06.003;
RA Dowdle W.E., Robinson J.F., Kneist A., Sirerol-Piquer M.S., Frints S.G.,
RA Corbit K.C., Zaghloul N.A., van Lijnschoten G., Mulders L., Verver D.E.,
RA Zerres K., Reed R.R., Attie-Bitach T., Johnson C.A., Garcia-Verdugo J.M.,
RA Katsanis N., Bergmann C., Reiter J.F.;
RT "Disruption of a ciliary B9 protein complex causes Meckel syndrome.";
RL Am. J. Hum. Genet. 89:94-110(2011).
RN [5]
RP IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX, AND FUNCTION.
RX PubMed=22179047; DOI=10.1038/ncb2410;
RA Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E.,
RA Sandoval W., Peterson A.S.;
RT "A ciliopathy complex at the transition zone protects the cilia as a
RT privileged membrane domain.";
RL Nat. Cell Biol. 14:61-72(2012).
CC -!- FUNCTION: Component of the tectonic-like complex, a complex localized
CC at the transition zone of primary cilia and acting as a barrier that
CC prevents diffusion of transmembrane proteins between the cilia and
CC plasma membranes. {ECO:0000269|PubMed:18287022,
CC ECO:0000269|PubMed:22179047}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex).
CC Interacts with TUBG1. {ECO:0000269|PubMed:18287022,
CC ECO:0000269|PubMed:21763481, ECO:0000269|PubMed:22179047}.
CC -!- INTERACTION:
CC Q3UK10; Q9R1S0: B9d1; NbExp=5; IntAct=EBI-5652008, EBI-5652050;
CC Q3UK10; Q5SW45: Mks1; NbExp=3; IntAct=EBI-5652008, EBI-4281059;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:18287022}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:18287022}. Nucleus {ECO:0000269|PubMed:18287022}.
CC -!- TISSUE SPECIFICITY: Highest expression in thymus and skeletal muscle.
CC Also expressed in spleen, kidney, lung, heart, microglia and liver.
CC Detected in brain (at protein level). {ECO:0000269|PubMed:18287022}.
CC -!- DISRUPTION PHENOTYPE: Mice expressing reduced levels of the protein in
CC the central nervous system and kidney develop perinatal triventricular
CC hydrocephaly, polycystic kidney disease, lack functional intact cilia
CC and die at the time of weaning. {ECO:0000269|PubMed:18287022}.
CC -!- SIMILARITY: Belongs to the B9D family. {ECO:0000305}.
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DR EMBL; AK141500; BAE24704.1; -; mRNA.
DR EMBL; AK146227; BAE26994.1; -; mRNA.
DR EMBL; BC028440; AAH28440.1; -; mRNA.
DR CCDS; CCDS20992.1; -.
DR RefSeq; NP_742160.1; NM_172148.1.
DR RefSeq; XP_006539917.1; XM_006539854.3.
DR AlphaFoldDB; Q3UK10; -.
DR CORUM; Q3UK10; -.
DR DIP; DIP-29732N; -.
DR IntAct; Q3UK10; 9.
DR STRING; 10090.ENSMUSP00000104040; -.
DR EPD; Q3UK10; -.
DR MaxQB; Q3UK10; -.
DR PaxDb; Q3UK10; -.
DR PeptideAtlas; Q3UK10; -.
DR PRIDE; Q3UK10; -.
DR ProteomicsDB; 277156; -.
DR Antibodypedia; 48740; 36 antibodies from 14 providers.
DR Ensembl; ENSMUST00000108403; ENSMUSP00000104040; ENSMUSG00000063439.
DR Ensembl; ENSMUST00000205658; ENSMUSP00000146289; ENSMUSG00000063439.
DR GeneID; 232987; -.
DR KEGG; mmu:232987; -.
DR UCSC; uc009fto.1; mouse.
DR CTD; 80776; -.
DR MGI; MGI:2387643; B9d2.
DR VEuPathDB; HostDB:ENSMUSG00000063439; -.
DR eggNOG; KOG4028; Eukaryota.
DR GeneTree; ENSGT00940000161428; -.
DR HOGENOM; CLU_084934_2_1_1; -.
DR InParanoid; Q3UK10; -.
DR OMA; IMRHFDK; -.
DR OrthoDB; 367491at2759; -.
DR PhylomeDB; Q3UK10; -.
DR TreeFam; TF314883; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 232987; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q3UK10; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UK10; protein.
DR Bgee; ENSMUSG00000063439; Expressed in bone marrow and 63 other tissues.
DR ExpressionAtlas; Q3UK10; baseline and differential.
DR Genevisible; Q3UK10; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR InterPro; IPR010796; C2_B9-type_dom.
DR PANTHER; PTHR12968; PTHR12968; 1.
DR Pfam; PF07162; B9-C2; 1.
DR PROSITE; PS51381; C2_B9; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Nucleus; Reference proteome.
FT CHAIN 1..175
FT /note="B9 domain-containing protein 2"
FT /id="PRO_0000307675"
FT DOMAIN 2..118
FT /note="C2 B9-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00713"
FT CONFLICT 167
FT /note="H -> N (in Ref. 1; BAE26994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 19250 MW; F36F5AA5636163D1 CRC64;
MAEVHVIGQI IGATGFSESS LFCKWGIHTG AAWKLLSGVR EGQTQVDTPQ IGDMAYWSHP
IDLHFATKGL QGWPRLHLQV WSQDSFGRCQ LAGYGFCHVP SSPGTHQLDC PTWRPLGSWR
EQLARAFVGG GPQLLHADTI YSGADRYRLH TAAGGTVHLG IGLLLRHFDR YGVEC
