CBAR1_DANRE
ID CBAR1_DANRE Reviewed; 295 AA.
AC Q1LU86; Q6DC30;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=CBY1-interacting BAR domain-containing protein 1;
DE Flags: Precursor;
GN Name=cibar1; Synonyms=fam92a, fam92a1;
GN ORFNames=si:dkey-98l21.1, zgc:100998;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling
CC (By similarity). Plays a role in ciliogenesis (By similarity). Plays an
CC important role in the mitochondrial function and is essential for
CC maintaining mitochondrial morphology and inner membrane ultrastructure
CC (By similarity). {ECO:0000250|UniProtKB:A1XBS5,
CC ECO:0000250|UniProtKB:Q8BP22}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A1XBS5}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:A1XBS5}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q8BP22}. Nucleus {ECO:0000250|UniProtKB:A1XBS5}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:A1XBS5}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:A1XBS5}; Matrix side
CC {ECO:0000250|UniProtKB:A1XBS5}.
CC -!- DOMAIN: The BAR-like domain displays limited similarity to other BAR
CC domains. {ECO:0000250|UniProtKB:A1XBS5}.
CC -!- SIMILARITY: Belongs to the CIBAR family. {ECO:0000305}.
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DR EMBL; BX957357; CAK11277.1; -; Genomic_DNA.
DR EMBL; BC078261; AAH78261.1; -; mRNA.
DR RefSeq; NP_001003604.1; NM_001003604.2.
DR AlphaFoldDB; Q1LU86; -.
DR SMR; Q1LU86; -.
DR STRING; 7955.ENSDARP00000006153; -.
DR PaxDb; Q1LU86; -.
DR DNASU; 445210; -.
DR Ensembl; ENSDART00000114714; ENSDARP00000101836; ENSDARG00000004436.
DR GeneID; 445210; -.
DR KEGG; dre:445210; -.
DR CTD; 137392; -.
DR ZFIN; ZDB-GENE-040801-123; cibar1.
DR eggNOG; ENOG502QQ0N; Eukaryota.
DR GeneTree; ENSGT00390000010285; -.
DR HOGENOM; CLU_072172_1_0_1; -.
DR InParanoid; Q1LU86; -.
DR OrthoDB; 1324464at2759; -.
DR PhylomeDB; Q1LU86; -.
DR TreeFam; TF324316; -.
DR PRO; PR:Q1LU86; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000004436; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q1LU86; baseline and differential.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS: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 2: Evidence at transcript 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..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT CHAIN 50..295
FT /note="CBY1-interacting BAR domain-containing protein 1"
FT /id="PRO_0000287082"
FT REGION 12..222
FT /note="BAR-like"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT REGION 243..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 111..185
FT /evidence="ECO:0000255"
FT COMPBIAS 243..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 191
FT /note="T -> M (in Ref. 2; AAH78261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 34378 MW; A6B1851F78758ED4 CRC64;
MMSRTPDARA RDTQTKQIQE NITSVEKHFG DLCQLFAAYV RKTARLRDKA DLLVKEINVY
ADTETPNLKC GLKNFADQLA KVQDYRQAEV ERLEVKVIEP LKAYGNIVKT KREDLKQTQS
ARNREAKQMQ QLERMRQRNP SDRQIISQAE SELQRATMDA TRTTRQLEET IDDFEKQKIR
DIKKVLGEFV TVEMAFHAKA LEIYTTAYQH IQNVDEEGDL EVFRNSLHPP DYQSRLEIVR
ANSKLSLNRT GTSMSKSGTM QSRTSSRQRK RDDEEDEEED DEDEDDLEEV TDDEH
