CBAR1_MOUSE
ID CBAR1_MOUSE Reviewed; 286 AA.
AC Q8BP22; A2AVA5; A2AVA6; A2AVA7; Q7TNQ9; Q8C2F8; Q8VDU6; Q9D2J3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=CBY1-interacting BAR domain-containing protein 1 {ECO:0000312|MGI:MGI:1915349};
DE Flags: Precursor;
GN Name=Cibar1 {ECO:0000312|MGI:MGI:1915349}; Synonyms=Fam92a, Fam92a1;
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=C57BL/6J, and NOD; TISSUE=Testis, Thymus, and Wolffian duct;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Eye, and 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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=27528616; DOI=10.1128/mcb.00160-16;
RA Li F.Q., Chen X., Fisher C., Siller S.S., Zelikman K., Kuriyama R.,
RA Takemaru K.I.;
RT "BAR domain-containing FAM92 proteins interact with chibby1 to facilitate
RT ciliogenesis.";
RL Mol. Cell. Biol. 36:2668-2680(2016).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30395363; DOI=10.1002/jbmr.3594;
RA Schrauwen I., Giese A.P., Aziz A., Lafont D.T., Chakchouk I.,
RA Santos-Cortez R.L.P., Lee K., Acharya A., Khan F.S., Ullah A.,
RA Nickerson D.A., Bamshad M.J., Ali G., Riazuddin S., Ansar M., Ahmad W.,
RA Ahmed Z.M., Leal S.M.;
RT "FAM92A underlies nonsyndromic postaxial polydactyly in humans and an
RT abnormal limb and digit skeletal phenotype in mice.";
RL J. Bone Miner. Res. 34:375-386(2019).
RN [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=29459677; DOI=10.1038/s41588-018-0054-7;
RA Breslow D.K., Hoogendoorn S., Kopp A.R., Morgens D.W., Vu B.K.,
RA Kennedy M.C., Han K., Li A., Hess G.T., Bassik M.C., Chen J.K.,
RA Nachury M.V.;
RT "A CRISPR-based screen for Hedgehog signaling provides insights into
RT ciliary function and ciliopathies.";
RL Nat. Genet. 50:460-471(2018).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30404948; DOI=10.1083/jcb.201806191;
RA Wang L., Yan Z., Vihinen H., Eriksson O., Wang W., Soliymani R., Lu Y.,
RA Xue Y., Jokitalo E., Li J., Zhao H.;
RT "FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure
RT and function.";
RL J. Cell Biol. 218:97-111(2019).
CC -!- FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling
CC (PubMed:29459677). Probable regulator of ciliogenesis involved in limb
CC morphogenesis (PubMed:30395363). In cooperation with CBY1 it is
CC involved in the recruitment and fusion of endosomal vesicles at distal
CC appendages during early stages of ciliogenesis (By similarity). Plays
CC an important role in the mitochondrial function and is essential for
CC maintaining mitochondrial morphology and inner membrane ultrastructure
CC (By similarity). In vitro, can generate membrane curvature through
CC preferential interaction with negatively charged phospholipids such as
CC phosphatidylinositol 4,5-bisphosphate and cardiolipin and hence
CC orchestrate cristae shape (By similarity).
CC {ECO:0000250|UniProtKB:A1XBS5, ECO:0000269|PubMed:29459677,
CC ECO:0000269|PubMed:30395363}.
CC -!- SUBUNIT: Homodimer (via BAR-like domain). Heterodimer with FAM92B (via
CC BAR-like domains). Interacts (via BAR-like domain) with CBY1; this
CC interaction is required for targeting FAM92A to centriole and cilium
CC basal body. {ECO:0000250|UniProtKB:A1XBS5}.
CC -!- INTERACTION:
CC Q8BP22; Q60680-1: Chuk; NbExp=4; IntAct=EBI-646638, EBI-646260;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A1XBS5}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:A1XBS5}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000269|PubMed:27528616}. Cell projection,
CC cilium {ECO:0000269|PubMed:29459677}. Nucleus
CC {ECO:0000250|UniProtKB:A1XBS5}. Mitochondrion inner membrane
CC {ECO:0000305|PubMed:30404948}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A1XBS5}; Matrix side
CC {ECO:0000250|UniProtKB:A1XBS5}. Note=Weak punctate vesicular
CC distribution throughout the cytoplasm. Localizes at the distal end of
CC mother centrioles. Extensive colocalization with CBY1 at mother
CC centrioles (PubMed:27528616). Localizes at the transition zone, a
CC region between the basal body and the ciliary axoneme
CC (PubMed:29459677). {ECO:0000250|UniProtKB:A1XBS5,
CC ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:29459677}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart, liver, spleen, lung,
CC kidney, brain and muscle (at protein level) (PubMed:30404948). Strongly
CC expressed throughout the developing limb bud, including the progress
CC zone and the apical ectodermal ridge (PubMed:30395363).
CC {ECO:0000269|PubMed:30395363, ECO:0000269|PubMed:30404948}.
CC -!- DEVELOPMENTAL STAGE: High and steady expression is observed in the
CC developing limb throughout embryonic stages 11.5-15.5 dpc.
CC {ECO:0000269|PubMed:30395363}.
CC -!- DOMAIN: The BAR-like domain displays limited similarity to other BAR
CC domains. {ECO:0000250|UniProtKB:A1XBS5}.
CC -!- DISRUPTION PHENOTYPE: Knockout homozygous mice show uni- or bilateral
CC abnormal bone growth or exostosis on the deltoid tuberosity of the
CC humerus, abnormalities at the left stifle consistent with a tendon
CC calcification, and abnormal digit morphology including polysyndactyly
CC and osteomas on the hind paw metatarsals.
CC {ECO:0000269|PubMed:30395363}.
CC -!- SIMILARITY: Belongs to the CIBAR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37273.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40516.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK019574; BAB31798.1; -; mRNA.
DR EMBL; AK078438; BAC37273.1; ALT_INIT; mRNA.
DR EMBL; AK088705; BAC40516.1; ALT_INIT; mRNA.
DR EMBL; JH584272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020162; AAH20162.1; -; mRNA.
DR EMBL; BC055848; AAH55848.1; -; mRNA.
DR RefSeq; NP_001297672.1; NM_001310743.1.
DR RefSeq; NP_080834.3; NM_026558.5.
DR AlphaFoldDB; Q8BP22; -.
DR BioGRID; 212656; 134.
DR IntAct; Q8BP22; 1.
DR STRING; 10090.ENSMUSP00000103920; -.
DR iPTMnet; Q8BP22; -.
DR PhosphoSitePlus; Q8BP22; -.
DR MaxQB; Q8BP22; -.
DR PaxDb; Q8BP22; -.
DR PRIDE; Q8BP22; -.
DR ProteomicsDB; 271545; -.
DR Antibodypedia; 25708; 127 antibodies from 22 providers.
DR DNASU; 68099; -.
DR GeneID; 68099; -.
DR KEGG; mmu:68099; -.
DR UCSC; uc008saq.2; mouse.
DR CTD; 137392; -.
DR MGI; MGI:1915349; Cibar1.
DR VEuPathDB; HostDB:ENSMUSG00000028218; -.
DR eggNOG; ENOG502QQ0N; Eukaryota.
DR InParanoid; Q8BP22; -.
DR OrthoDB; 1324464at2759; -.
DR PhylomeDB; Q8BP22; -.
DR TreeFam; TF324316; -.
DR BioGRID-ORCS; 68099; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Fam92a; mouse.
DR PRO; PR:Q8BP22; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BP22; protein.
DR Bgee; ENSMUSG00000028218; Expressed in vas deferens and 244 other tissues.
DR ExpressionAtlas; Q8BP22; baseline and differential.
DR Genevisible; Q8BP22; MM.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; ISO:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0030061; C:mitochondrial crista; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISS:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
DR GO; GO:0061024; P:membrane organization; ISO:MGI.
DR GO; GO:0097749; P:membrane tubulation; ISO:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:UniProtKB.
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.
DR SUPFAM; SSF103657; SSF103657; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleus; Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT CHAIN 48..286
FT /note="CBY1-interacting BAR domain-containing protein 1"
FT /id="PRO_0000287081"
FT REGION 10..220
FT /note="BAR-like"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT REGION 258..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..178
FT /evidence="ECO:0000255"
FT COMPBIAS 272..286
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 155
FT /note="T -> P (in Ref. 1; BAB31798)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="N -> K (in Ref. 3; AAH20162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 33119 MW; 330D25DF4466EAE5 CRC64;
MLRRNLDERD AQTKQLQDAV TNVEKHFGEL CQIFAAYVRK TARLRDKADL LVNEINLYAS
TETPNLKQGL KDFADEFAKL QDYRQAEVER LEAKVVEPLK AYGTIVKMKR DDLKATLTAR
NREAKQLSQL ERTRQRNPSD RHVISQAETE LQRATIDATR TSRHLEETID NFEKQKIKDI
KNILSEFITI EMLFHGKALE VFTAAYQNIQ NIDEDEDLEV FRNSLYLSDY PSRLDIVRAN
SKSPLQRSLS TKCTSGTGQI STCRTRKDQQ VEDEDDEELD VTEDEN
