B9D1_MOUSE
ID B9D1_MOUSE Reviewed; 204 AA.
AC Q9R1S0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=B9 domain-containing protein 1;
DE AltName: Full=Endothelial precursor cells protein B9;
GN Name=B9d1; Synonyms=Eppb9;
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 [MRNA].
RC TISSUE=Endothelial cell;
RA Miyashita H., Sato Y.;
RT "A protein isolated from endothelial precursor cells.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=15625703; DOI=10.1002/mrd.20210;
RA Cui X.S., Shin M.R., Lee K.A., Kim N.H.;
RT "Identification of differentially expressed genes in murine embryos at the
RT blastocyst stage using annealing control primer system.";
RL Mol. Reprod. Dev. 70:278-287(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION IN A COMPLEX WITH MKS1
RP AND B9D2.
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 [8]
RP ERRATUM OF PUBMED:21763481.
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.;
RL Am. J. Hum. Genet. 89:589-589(2011).
RN [9]
RP INTERACTION WITH MKS1.
RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019;
RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A.,
RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K.,
RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D.,
RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A.,
RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B.,
RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.;
RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes
RT and pathways.";
RL Cell 145:513-528(2011).
RN [10]
RP IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX, FUNCTION, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
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).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE TECTONIC-LIKE
RP COMPLEX.
RX PubMed=21725307; DOI=10.1038/ng.891;
RA Garcia-Gonzalo F.R., Corbit K.C., Sirerol-Piquer M.S., Ramaswami G.,
RA Otto E.A., Noriega T.R., Seol A.D., Robinson J.F., Bennett C.L.,
RA Josifova D.J., Garcia-Verdugo J.M., Katsanis N., Hildebrandt F.,
RA Reiter J.F.;
RT "A transition zone complex regulates mammalian ciliogenesis and ciliary
RT membrane composition.";
RL Nat. Genet. 43:776-784(2011).
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. Required for ciliogenesis and sonic hedgehog/SHH
CC signaling. {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:21763481,
CC ECO:0000269|PubMed:22179047}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex).
CC {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:21763481,
CC ECO:0000269|PubMed:22179047}.
CC -!- INTERACTION:
CC Q9R1S0; Q3UK10: B9d2; NbExp=5; IntAct=EBI-5652050, EBI-5652008;
CC Q9R1S0; Q5SW45: Mks1; NbExp=4; IntAct=EBI-5652050, EBI-4281059;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}.
CC Note=Localizes at the transition zone, a region between the basal body
CC and the ciliary axoneme.
CC -!- DEVELOPMENTAL STAGE: Specifically or prominently expressed in mouse
CC blastocysts compared to 4-cell stage embryos.
CC {ECO:0000269|PubMed:15625703}.
CC -!- DISRUPTION PHENOTYPE: Mice display impaired cilia formation associated
CC with renal cystic dysplasia, as well as ductal plate malformation of
CC the liver and polydactyly. Additional phenotypes, occurring at varying
CC frequencies, include randomized heart looping, holoprosencephaly,
CC microphthalmia, cleft palate, ventricular septal defect and thinning of
CC the myocardial wall. Depending on their genetic background, mutant mice
CC die between 14.5 dpc and P1. {ECO:0000269|PubMed:21763481,
CC ECO:0000269|PubMed:22179047}.
CC -!- SIMILARITY: Belongs to the B9D family. {ECO:0000305}.
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DR EMBL; AB030483; BAA82643.1; -; mRNA.
DR EMBL; AK003038; BAB22525.1; -; mRNA.
DR EMBL; AK010355; BAB26875.1; -; mRNA.
DR EMBL; AK131701; BAE20767.1; -; mRNA.
DR EMBL; AL604029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008113; AAH08113.1; -; mRNA.
DR CCDS; CCDS24815.1; -.
DR RefSeq; NP_001317709.1; NM_001330780.1.
DR RefSeq; NP_001317710.1; NM_001330781.1.
DR RefSeq; NP_038745.1; NM_013717.3.
DR AlphaFoldDB; Q9R1S0; -.
DR BioGRID; 205118; 2.
DR CORUM; Q9R1S0; -.
DR IntAct; Q9R1S0; 79.
DR STRING; 10090.ENSMUSP00000099717; -.
DR iPTMnet; Q9R1S0; -.
DR PhosphoSitePlus; Q9R1S0; -.
DR EPD; Q9R1S0; -.
DR MaxQB; Q9R1S0; -.
DR PaxDb; Q9R1S0; -.
DR PRIDE; Q9R1S0; -.
DR ProteomicsDB; 277155; -.
DR Antibodypedia; 13647; 80 antibodies from 22 providers.
DR DNASU; 27078; -.
DR Ensembl; ENSMUST00000102657; ENSMUSP00000099717; ENSMUSG00000001039.
DR GeneID; 27078; -.
DR KEGG; mmu:27078; -.
DR UCSC; uc007jhu.1; mouse.
DR CTD; 27077; -.
DR MGI; MGI:1351471; B9d1.
DR VEuPathDB; HostDB:ENSMUSG00000001039; -.
DR eggNOG; KOG4027; Eukaryota.
DR GeneTree; ENSGT00940000160079; -.
DR HOGENOM; CLU_084934_0_0_1; -.
DR InParanoid; Q9R1S0; -.
DR OMA; GWPQILV; -.
DR OrthoDB; 1387644at2759; -.
DR PhylomeDB; Q9R1S0; -.
DR TreeFam; TF314883; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 27078; 5 hits in 73 CRISPR screens.
DR ChiTaRS; B9d1; mouse.
DR PRO; PR:Q9R1S0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9R1S0; protein.
DR Bgee; ENSMUSG00000001039; Expressed in animal zygote and 206 other tissues.
DR ExpressionAtlas; Q9R1S0; baseline and differential.
DR Genevisible; Q9R1S0; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
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:0008158; F:hedgehog receptor activity; IMP:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
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; Reference proteome.
FT CHAIN 1..204
FT /note="B9 domain-containing protein 1"
FT /id="PRO_0000307668"
FT DOMAIN 9..127
FT /note="C2 B9-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00713"
SQ SEQUENCE 204 AA; 22592 MW; C2C65AE39A65DB95 CRC64;
MAAASPSVFL LMITGQVESA QFPEYDDLYC KYCFVYGQDW APTAGLEEGI SQIASKSQDV
RQALVWNFPI DVTFKSTNPY GWPQIVLSVY GPDVFGNDVV RGYGAVHVPL SPGRHKRTIP
MFVPESTSTL QKFTSWFMGR RPEYTDPKVV AQGEGREVTR VRSQGFVTLL FNVVTKDMKK
LGYDTGPVDT QGVLGPSLPQ GNPQ
