B9D1_DROME
ID B9D1_DROME Reviewed; 241 AA.
AC Q9VF59;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=B9 domain-containing protein 1 {ECO:0000312|FlyBase:FBgn0038342};
DE AltName: Full=MKS1-related protein 1 {ECO:0000303|PubMed:22508513};
GN Name=B9d1 {ECO:0000312|FlyBase:FBgn0038342};
GN ORFNames=CG14870 {ECO:0000312|FlyBase:FBgn0038342};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:ACD81742.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22508513; DOI=10.1083/jcb.201109148;
RA Enjolras C., Thomas J., Chhin B., Cortier E., Duteyrat J.L., Soulavie F.,
RA Kernan M.J., Laurencon A., Durand B.;
RT "Drosophila chibby is required for basal body formation and ciliogenesis
RT but not for Wg signaling.";
RL J. Cell Biol. 197:313-325(2012).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25447994; DOI=10.1016/j.cub.2014.09.047;
RA Basiri M.L., Ha A., Chadha A., Clark N.M., Polyanovsky A., Cook B.,
RA Avidor-Reiss T.;
RT "A migrating ciliary gate compartmentalizes the site of axoneme assembly in
RT Drosophila spermatids.";
RL Curr. Biol. 24:2622-2631(2014).
RN [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE MKS COMPLEX, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=27646273; DOI=10.1083/jcb.201603086;
RA Vieillard J., Paschaki M., Duteyrat J.L., Augiere C., Cortier E.,
RA Lapart J.A., Thomas J., Durand B.;
RT "Transition zone assembly and its contribution to axoneme formation in
RT Drosophila male germ cells.";
RL J. Cell Biol. 214:875-889(2016).
RN [7] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE MKS COMPLEX, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27577095; DOI=10.1242/jcs.194621;
RA Pratt M.B., Titlow J.S., Davis I., Barker A.R., Dawe H.R., Raff J.W.,
RA Roque H.;
RT "Drosophila sensory cilia lacking MKS proteins exhibit striking defects in
RT development but only subtle defects in adults.";
RL J. Cell Sci. 129:3732-3743(2016).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30013109; DOI=10.1038/s41556-018-0132-1;
RA Jana S.C., Mendonca S., Machado P., Werner S., Rocha J., Pereira A.,
RA Maiato H., Bettencourt-Dias M.;
RT "Differential regulation of transition zone and centriole proteins
RT contributes to ciliary base diversity.";
RL Nat. Cell Biol. 20:928-941(2018).
CC -!- FUNCTION: Probable component of the tectonic-like complex (also named
CC MKS complex), a complex localized at the transition zone of primary
CC cilia (PubMed:27577095, PubMed:27646273). Required for ciliary
CC structure and function (PubMed:27577095). {ECO:0000269|PubMed:27577095,
CC ECO:0000269|PubMed:27646273}.
CC -!- SUBUNIT: Probable component of the tectonic-like complex (also named
CC MKS complex), composed of B9d1, B9d2, Cc2d2a, Mks1 and tctn.
CC {ECO:0000305|PubMed:27577095, ECO:0000305|PubMed:27646273}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:22508513, ECO:0000269|PubMed:25447994,
CC ECO:0000269|PubMed:27577095, ECO:0000269|PubMed:27646273,
CC ECO:0000269|PubMed:30013109}. Note=Localizes at the transition zone
CC (TZ), a region between the basal body and the ciliary axoneme in the
CC olfactory, auditory and speromatocyte system (PubMed:27646273,
CC PubMed:30013109). In spermatocytes, localizes in the transition zone
CC and the migrating base of the spermatid ciliary cap (PubMed:25447994,
CC PubMed:27577095). Co-localizes with the tectonic-like complex
CC (PubMed:27646273). {ECO:0000269|PubMed:25447994,
CC ECO:0000269|PubMed:27577095, ECO:0000269|PubMed:27646273,
CC ECO:0000269|PubMed:30013109}.
CC -!- TISSUE SPECIFICITY: Expressed in type I sensory neurons (at protein
CC level) (PubMed:22508513, PubMed:30013109). Expressed in spermatids and
CC spermatocytes (at protein level) (PubMed:25447994, PubMed:27646273,
CC PubMed:27577095, PubMed:30013109). {ECO:0000269|PubMed:22508513,
CC ECO:0000269|PubMed:25447994, ECO:0000269|PubMed:27577095,
CC ECO:0000269|PubMed:27646273, ECO:0000269|PubMed:30013109}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:27577095). Results in
CC lack of localization of the tectonic-like module proteins, namely MKS1
CC and B9d2, to the transition zone resulting in minor defects in sensory
CC cilia (PubMed:27577095). {ECO:0000269|PubMed:27577095}.
CC -!- SIMILARITY: Belongs to the B9D family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014297; AAF55201.1; -; Genomic_DNA.
DR EMBL; BT032728; ACD81742.1; -; mRNA.
DR RefSeq; NP_650470.1; NM_142213.2.
DR AlphaFoldDB; Q9VF59; -.
DR IntAct; Q9VF59; 3.
DR STRING; 7227.FBpp0082599; -.
DR PaxDb; Q9VF59; -.
DR DNASU; 41888; -.
DR EnsemblMetazoa; FBtr0083145; FBpp0082599; FBgn0038342.
DR GeneID; 41888; -.
DR KEGG; dme:Dmel_CG14870; -.
DR UCSC; CG14870-RA; d. melanogaster.
DR CTD; 27077; -.
DR FlyBase; FBgn0038342; B9d1.
DR VEuPathDB; VectorBase:FBgn0038342; -.
DR eggNOG; KOG4027; Eukaryota.
DR GeneTree; ENSGT00940000160079; -.
DR HOGENOM; CLU_084934_0_0_1; -.
DR InParanoid; Q9VF59; -.
DR OMA; GWPQILV; -.
DR OrthoDB; 1387644at2759; -.
DR PhylomeDB; Q9VF59; -.
DR BioGRID-ORCS; 41888; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41888; -.
DR PRO; PR:Q9VF59; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038342; Expressed in testis and 7 other tissues.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0036038; C:MKS complex; ISS:FlyBase.
DR GO; GO:0060271; P:cilium assembly; IEP:FlyBase.
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 biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..241
FT /note="B9 domain-containing protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445800"
FT DOMAIN 53..197
FT /note="C2 B9-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00713"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 26866 MW; E75A04B184EE13AE CRC64;
MSASEGISLP GNEETTPPHE KHKQKAKKAK KKSRSAKESV PNAMDAKATA SYFSLSIVGQ
IVSATFPLGP DKEFVFLRYE MVAGPDWQLS SGPQHGLTQL ATNRRGHFNE PIVFNMPIEV
TYKSTSPYGW PQILVTVFGR SGLGRETLLG YAHIHLPVFG SRRPADQTEQ LQAPILMPKC
PNMMADITSW LLRREPELKD PKVLLDNLKC KGLSMESYGS LQFQLSSVMR GARKLGYHWH
S
