B9D2_DROME
ID B9D2_DROME Reviewed; 177 AA.
AC M9MRD5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=B9 domain-containing protein 2 {ECO:0000312|FlyBase:FBgn0261683};
DE AltName: Full=MKS1-related protein 2 {ECO:0000305};
GN Name=B9d2 {ECO:0000312|FlyBase:FBgn0261683};
GN ORFNames=CG42730 {ECO:0000312|FlyBase:FBgn0261683};
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:0000305}
RP FUNCTION, 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 [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE MKS COMPLEX, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE MKS COMPLEX, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
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).
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:27646273, PubMed:25447994, PubMed:27577095). Has a role
CC in ciliary structure and function (PubMed:27646273).
CC {ECO:0000269|PubMed:25447994, 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:25447994, ECO:0000269|PubMed:27577095,
CC ECO:0000269|PubMed:27646273}. Note=Localizes at the transition zone
CC (TZ), a region between the basal body and the ciliary axoneme
CC (PubMed:27646273). 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 -!- TISSUE SPECIFICITY: Expressed in chordotonal neurons in the antennae
CC (at protein level) (PubMed:27646273). Expressed in spermatids (at
CC protein level) (PubMed:25447994, PubMed:27577095).
CC {ECO:0000269|PubMed:25447994, ECO:0000269|PubMed:27577095,
CC ECO:0000269|PubMed:27646273}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous knockout of B9d2 and tctn is viable
CC and does not show sensory behavioral defects (PubMed:27646273). Males
CC produce motile sperm and show only slightly reduced fertility
CC (PubMed:27646273). Sperm flagella show weakly ultrastructural defects
CC including broken and disorganised structure (PubMed:27646273). Length
CC of the transition zone is decreased and recruitment of the tectonic-
CC like complex compromised (PubMed:27646273).
CC {ECO:0000269|PubMed:27646273}.
CC -!- SIMILARITY: Belongs to the B9D family. {ECO:0000305}.
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DR EMBL; AE014134; ADV36954.1; -; Genomic_DNA.
DR RefSeq; NP_001188704.1; NM_001201775.2.
DR AlphaFoldDB; M9MRD5; -.
DR STRING; 7227.FBpp0292197; -.
DR PaxDb; M9MRD5; -.
DR PRIDE; M9MRD5; -.
DR EnsemblMetazoa; FBtr0303078; FBpp0292197; FBgn0261683.
DR GeneID; 10178891; -.
DR KEGG; dme:Dmel_CG42730; -.
DR CTD; 80776; -.
DR FlyBase; FBgn0261683; B9d2.
DR VEuPathDB; VectorBase:FBgn0261683; -.
DR eggNOG; KOG4028; Eukaryota.
DR GeneTree; ENSGT00940000161428; -.
DR HOGENOM; CLU_084934_2_1_1; -.
DR OMA; IMRHFDK; -.
DR PhylomeDB; M9MRD5; -.
DR BioGRID-ORCS; 10178891; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 10178891; -.
DR PRO; PR:M9MRD5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261683; Expressed in testis and 2 other tissues.
DR GO; GO:0035869; C:ciliary transition zone; IDA:FlyBase.
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:1905349; P:ciliary transition zone assembly; IMP:FlyBase.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP: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..177
FT /note="B9 domain-containing protein 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445801"
FT DOMAIN 2..118
FT /note="C2 B9-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00713"
SQ SEQUENCE 177 AA; 19746 MW; 356B5A45B4F18341 CRC64;
MAEVHIIGQI LKAVDFAEPH LYCKWSLQSG NAWRLVQGEV QGQSHVASHR LQSSSDFAQP
LDIHLSTASV QGWPRLLVEV YAVNVLQQSW PVGYGFVHVP STPGTHRLEI GTWKVAPNGL
WQSLRERFGG GGAALSKTDL LYSGVERYKL QTLSSGKVIV ELNLIFRKFD EYGVEFK
