FAM92_DROME
ID FAM92_DROME Reviewed; 395 AA.
AC Q9VK91; Q95SS2;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=CBY1-interacting BAR domain-containing protein homolog {ECO:0000305};
DE AltName: Full=Protein Fam92 {ECO:0000303|PubMed:31821146};
GN Name=Fam92 {ECO:0000303|PubMed:31821146, ECO:0000312|FlyBase:FBgn0032428};
GN ORFNames=CG6405 {ECO:0000312|FlyBase:FBgn0032428};
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:AAL28167.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28167.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAL28167.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH FAM92 AND CBY, INTERACTION WITH
RP CBY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31821146; DOI=10.7554/elife.49307;
RA Lapart J.A., Gottardo M., Cortier E., Duteyrat J.L., Augiere C., Mange A.,
RA Jerber J., Solassol J., Gopalakrishnan J., Thomas J., Durand B.;
RT "Dzip1 and Fam92 form a ciliary transition zone complex with cell type
RT specific roles in Drosophila.";
RL Elife 8:0-0(2019).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=33370260; DOI=10.1371/journal.pbio.3001034;
RA Wu Z., Pang N., Zhang Y., Chen H., Peng Y., Fu J., Wei Q.;
RT "CEP290 is essential for the initiation of ciliary transition zone
RT assembly.";
RL PLoS Biol. 18:e3001034-e3001034(2020).
CC -!- FUNCTION: Component of the DZIP1-Fam92-Cby complex which promotes
CC ciliogenesis in sensory neurons and spermatocytes by acting downstream
CC of Cep290 to initiate early ciliary membrane formation and thus
CC transition zone (TZ) assembly (PubMed:31821146). During
CC spermatogenesis, also regulates distal elongation of the basal-body and
CC their docking (anchoring) to the plasma membrane and as a consequence,
CC regulates the initiation and proper elongation of axonemal microtubules
CC (PubMed:31821146). Within the complex, required to recruit or stabilize
CC Cby at the distal basal body of cilia to promote DZIP1-mediated early
CC ciliary membrane formation and initiate TZ assembly (PubMed:31821146,
CC PubMed:33370260). May also act with Dzip1 to restrict cep290
CC localization to the proximal part of the TZ (PubMed:31821146). May also
CC be involved in recruitment or stabilization of Mks1 at the TZ
CC (PubMed:31821146). {ECO:0000269|PubMed:31821146,
CC ECO:0000269|PubMed:33370260}.
CC -!- SUBUNIT: Component of a ciliary transition zone (TZ)-localized complex
CC composed of DZIP1, Fam92 and Cby (PubMed:31821146). Interacts directly
CC with Cby (PubMed:31821146). {ECO:0000269|PubMed:31821146}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:31821146}. Note=Localizes at the transition zone
CC (TZ) in type I sensory neurons and spermatocytes (PubMed:31821146).
CC Localizes at the centriolar distal ends of early spermatocytes and in
CC elongating spermatids, when the TZ migrates away from the basal body,
CC localizes at the ring centriole (PubMed:31821146).
CC {ECO:0000269|PubMed:31821146}.
CC -!- TISSUE SPECIFICITY: In neurons of the second and third antennal
CC segments, expressed at the tip of the dendrites.
CC {ECO:0000269|PubMed:31821146}.
CC -!- DISRUPTION PHENOTYPE: Viable but displays adherent transition zone (TZ)
CC assembly in sensory neurons and spermatocytes (PubMed:31821146).
CC Consequently, adults display phenotypes associated with ciliary
CC dysfunction and disorganization, such as reduced geotaxis response and
CC decreased male fertility (PubMed:31821146). Some mutants also display,
CC reduced scolopidia cilia number, deformed axonemes, excess accumulation
CC of material beneath the ciliary membrane and deformation of the ciliary
CC membrane (PubMed:31821146). In spermatocytes, some centrioles are
CC undocked and display irregular distal ends or microtubules extending
CC from the distal ends (PubMed:31821146). Dzip expression is slightly
CC reduced and in spermatocytes, Mks1 is lost or reduced at the cilliary
CC transition zone and Cby is completely lost at the tip of the centrioles
CC (PubMed:31821146). {ECO:0000269|PubMed:31821146}.
CC -!- SIMILARITY: Belongs to the CIBAR family. {ECO:0000305}.
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DR EMBL; AE014134; AAF53187.2; -; Genomic_DNA.
DR EMBL; AY060619; AAL28167.1; -; mRNA.
DR RefSeq; NP_609564.1; NM_135720.2.
DR AlphaFoldDB; Q9VK91; -.
DR SMR; Q9VK91; -.
DR STRING; 7227.FBpp0079948; -.
DR PaxDb; Q9VK91; -.
DR EnsemblMetazoa; FBtr0080366; FBpp0079948; FBgn0032428.
DR GeneID; 34654; -.
DR KEGG; dme:Dmel_CG6405; -.
DR UCSC; CG6405-RA; d. melanogaster.
DR FlyBase; FBgn0032428; Fam92.
DR VEuPathDB; VectorBase:FBgn0032428; -.
DR eggNOG; ENOG502QQ0N; Eukaryota.
DR GeneTree; ENSGT00390000010285; -.
DR HOGENOM; CLU_792926_0_0_1; -.
DR InParanoid; Q9VK91; -.
DR OMA; ICSIDER; -.
DR OrthoDB; 862508at2759; -.
DR PhylomeDB; Q9VK91; -.
DR BioGRID-ORCS; 34654; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34654; -.
DR PRO; PR:Q9VK91; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032428; Expressed in testis and 10 other tissues.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISS:FlyBase.
DR CDD; cd07598; BAR_FAM92; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035590; BAR_CBAR1/2.
DR InterPro; IPR009602; CBAR/FAM92.
DR PANTHER; PTHR21223; PTHR21223; 1.
DR Pfam; PF06730; FAM92; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..395
FT /note="CBY1-interacting BAR domain-containing protein
FT homolog"
FT /id="PRO_0000452642"
FT REGION 240..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 45179 MW; 98CB7D2069E73037 CRC64;
MFRRGKLSFL NTKDDRVKII NERINITERH LMEMCSSFAL VTRKMAKYRD SFDELAKSVK
SYADDEEINE SLCQGLKSFT NAVTIMGDYM DINVHRLEHK IVNELAQFEQ LCKSTRDNLR
LAVIARDKEV LRQRQMLELK SKFSANNSAA DSELFKAKME VQRTNKEIDD IIGNFEQRKL
RDLKQIISDF ILIAMKQHTK ALEILSASYY DIGTIDERDD FIEFQKLMKT KEELASRKTA
LKKGLRSQSM DSLEHEHLVS PLKRRPKLSR SNRNLTGAGI NHGSKTEPED ETDEQDEEED
DEDEETEQSG EEDEESGTAT DDEREPTQPG NQVPPRENVF GAKIRSASKD IATPSTSASA
TSAPSKPSRQ TVKHPFKAVA STHVRLQKQF HVPQH
