CBAR1_BOVIN
ID CBAR1_BOVIN Reviewed; 288 AA.
AC Q3SZG6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=CBY1-interacting BAR domain-containing protein 1 {ECO:0000250|UniProtKB:A1XBS5};
DE Flags: Precursor;
GN Name=CIBAR1 {ECO:0000250|UniProtKB:A1XBS5}; Synonyms=FAM92A, FAM92A1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling
CC (By similarity). Probable regulator of ciliogenesis involved in limb
CC morphogenesis. In cooperation with CBY1 it is involved in the
CC recruitment and fusion of endosomal vesicles at distal appendages
CC during early stages of ciliogenesis (By similarity). Plays an important
CC role in the mitochondrial function and is essential for maintaining
CC mitochondrial morphology and inner membrane ultrastructure (By
CC 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:0000250|UniProtKB:Q8BP22}.
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 -!- 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:0000250|UniProtKB:A1XBS5}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:Q8BP22}. 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}. 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. {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; BC102866; AAI02867.1; -; mRNA.
DR RefSeq; NP_001030519.1; NM_001035442.1.
DR AlphaFoldDB; Q3SZG6; -.
DR SMR; Q3SZG6; -.
DR STRING; 9913.ENSBTAP00000017833; -.
DR PaxDb; Q3SZG6; -.
DR PRIDE; Q3SZG6; -.
DR Ensembl; ENSBTAT00000081243; ENSBTAP00000065967; ENSBTAG00000013405.
DR GeneID; 614070; -.
DR KEGG; bta:614070; -.
DR CTD; 137392; -.
DR VEuPathDB; HostDB:ENSBTAG00000013405; -.
DR eggNOG; ENOG502QQ0N; Eukaryota.
DR GeneTree; ENSGT00390000010285; -.
DR InParanoid; Q3SZG6; -.
DR OrthoDB; 1324464at2759; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000013405; Expressed in spermatid and 111 other tissues.
DR ExpressionAtlas; Q3SZG6; 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:0035108; P:limb morphogenesis; 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..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT CHAIN 48..288
FT /note="CBY1-interacting BAR domain-containing protein 1"
FT /id="PRO_0000287079"
FT REGION 10..220
FT /note="BAR-like"
FT /evidence="ECO:0000250|UniProtKB:A1XBS5"
FT REGION 266..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..176
FT /evidence="ECO:0000255"
FT COMPBIAS 272..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 33524 MW; 5DD0C5C1D3A358F4 CRC64;
MLRRSLENRD AQTRQLQDAV TNVEKHFGEL CQIFAAYVRK TARLRDKADL LVNEINVYAS
TETPHLKQGL KNFADEFAKL QDYRQAEVER LEAKVVEPLK AYGTIVKMKR DDLKATLTAR
NREAKQLTQL ERTRQRNPSD RHVISQAETE LQRATMDATR TTRHLEETID NFEKQKIKDI
KTIFSEFITI EMLFHGKALE VYTAAYQNIQ KIDEEEDLEV FRHSLYPQDY SSRLDIVRAN
SKSPLQRSLS AKCVSGTGQV LTCRLRKDHQ TEDDDEEDED LDVTEEEN
