CBR1B_XENLA
ID CBR1B_XENLA Reviewed; 285 AA.
AC Q6GN09; A0A1L8FZI4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=CBY1-interacting BAR domain-containing protein 1-B {ECO:0000250|UniProtKB:A1XBS5};
DE Flags: Precursor;
GN Name=cibar1-b {ECO:0000250|UniProtKB:A1XBS5}; Synonyms=fam921.L, fam92a-b;
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 [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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}. 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; CM004476; OCT77000.1; -; Genomic_DNA.
DR EMBL; BC073713; AAH73713.1; -; mRNA.
DR RefSeq; NP_001086023.1; NM_001092554.1.
DR RefSeq; XP_018121975.1; XM_018266486.1.
DR AlphaFoldDB; Q6GN09; -.
DR SMR; Q6GN09; -.
DR STRING; 8355.Q6GN09; -.
DR DNASU; 444452; -.
DR GeneID; 444452; -.
DR KEGG; xla:444452; -.
DR CTD; 444452; -.
DR Xenbase; XB-GENE-960746; cibar1.L.
DR OMA; HIIAETE; -.
DR OrthoDB; 1324464at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 444452; Expressed in testis 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: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..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT CHAIN 49..285
FT /note="CBY1-interacting BAR domain-containing protein 1-B"
FT /id="PRO_0000287084"
FT REGION 11..221
FT /note="BAR-like"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT REGION 241..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..184
FT /evidence="ECO:0000255"
FT COMPBIAS 241..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 32912 MW; 52C01C72E3FC0DFF CRC64;
MSQTPEARTR DNQTRQIQES VNNVEKHFGE LCQIFAGYVR KTARLRDKAD LLVREVNTYA
DTETPTLKHG LKNFADEFAK LQDYRQAEVE RLESRVVEPL KSYGGIIKLK REDLKVTLSA
RNREAKQMAQ LEKTRQRNPS DRQIISQAET ELQRATMDAA RISQQLEETI DNFEKQKIKD
IKKLFAEFVT IEMVFHGKAL EVLTAAYQHI QDIDEEEDLE VFRNSLHPPD FQSRLDIVRA
NSRSGSTSRA PSVISQPPGN RQKNRMEDDE DGEDDNDENS TEDEN
