CBR1A_XENLA
ID CBR1A_XENLA Reviewed; 284 AA.
AC Q2VR06; A0A1L8FTJ3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=CBY1-interacting BAR domain-containing protein 1-A {ECO:0000250|UniProtKB:A1XBS5};
DE Flags: Precursor;
GN Name=cibar1-a {ECO:0000250|UniProtKB:A1XBS5}; Synonyms=fam921.S, fam92a1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang H.S., Ruan X.Z., Deng H.X.;
RT "Full-length sequence of CV973659.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
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}. Nucleus
CC {ECO:0000250|UniProtKB:A1XBS5}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:A1XBS5}; Peripheral membrane protein
CC {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; AY855078; AAX47337.1; -; mRNA.
DR EMBL; CM004477; OCT74888.1; -; Genomic_DNA.
DR RefSeq; NP_001089128.1; NM_001095659.1.
DR AlphaFoldDB; Q2VR06; -.
DR SMR; Q2VR06; -.
DR STRING; 8355.Q2VR06; -.
DR GeneID; 733428; -.
DR KEGG; xla:733428; -.
DR CTD; 733428; -.
DR Xenbase; XB-GENE-17343261; cibar1.S.
DR OMA; RDDVKNT; -.
DR OrthoDB; 1324464at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 733428; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0097546; C:ciliary base; 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 Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleus;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT CHAIN 49..284
FT /note="CBY1-interacting BAR domain-containing protein 1-A"
FT /id="PRO_0000287083"
FT REGION 11..221
FT /note="BAR-like"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT REGION 242..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..184
FT /evidence="ECO:0000255"
FT COILED 260..284
FT /evidence="ECO:0000255"
FT COMPBIAS 242..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 32872 MW; 7256DC35744030B0 CRC64;
MSQTPEARAR DNQTRQIQES VNNVEKHFGE LCQIFAGYVR KTARLRDKAD LLVREVNTYA
DTETPTVKLG LKNFADELAK LQDYRQAEVE RLESRVVEPL KSYGSIIKLK REDLKVTLTA
RNREAKQMAQ LEKTRQRNPS DRQIISQAET ELQRATMDAS RISQQLEETI DNFEKQKMKD
IKKLFTEFVS IEMVFHGKAL EVLTAAYQHI QDIDEEEDLE VFRNSLHPPD FQSRLDIVRA
NSRTGSTSRG PSVISQPPGN RQKNRIEDED EEEEDDENST EDEN
