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Database: UniProt
Entry: A0AAA9RVF2_BOVIN
LinkDB: A0AAA9RVF2_BOVIN
Original site: A0AAA9RVF2_BOVIN 
ID   A0AAA9RVF2_BOVIN        Unreviewed;       544 AA.
AC   A0AAA9RVF2;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   RecName: Full=BBSome complex member BBS5 {ECO:0000256|ARBA:ARBA00047191};
GN   Name=BBS5 {ECO:0000313|Ensembl:ENSBTAP00000076289.1};
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 {ECO:0000313|Ensembl:ENSBTAP00000076289.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000076289.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000076289.1};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000076289.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000076289.1};
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSBTAP00000076289.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000076289.1};
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC       required for sorting of specific membrane proteins to the primary
CC       cilia. The BBSome complex is required for ciliogenesis but is
CC       dispensable for centriolar satellite function. This ciliogenic function
CC       is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC       localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC       the primary cilium and promotes extension of the ciliary membrane.
CC       Firstly the BBSome associates with the ciliary membrane and binds to
CC       RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC       Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC       carrier vesicles to the base of the ciliary membrane. The BBSome
CC       complex, together with the LTZL1, controls SMO ciliary trafficking and
CC       contributes to the sonic hedgehog (SHH) pathway regulation. Required
CC       for BBSome complex ciliary localization but not for the proper complex
CC       assembly. {ECO:0000256|ARBA:ARBA00054242}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC       {ECO:0000256|ARBA:ARBA00004309}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriolar satellite
CC       {ECO:0000256|ARBA:ARBA00004607}.
CC   -!- SIMILARITY: Belongs to the BBS5 family.
CC       {ECO:0000256|ARBA:ARBA00005822}.
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DR   AlphaFoldDB; A0AAA9RVF2; -.
DR   Ensembl; ENSBTAT00000110893.1; ENSBTAP00000076289.1; ENSBTAG00000010736.7.
DR   GeneTree; ENSGT00940000158859; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   GO; GO:0034464; C:BBSome; IEA:InterPro.
DR   GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00900; PH-like; 1.
DR   FunFam; 2.30.29.30:FF:000232; Bardet-Biedl syndrome 5 isoform 1; 1.
DR   FunFam; 2.120.10.80:FF:000025; Kelch-like family member 41; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR006606; BBL5.
DR   InterPro; IPR014003; BBS5_PH.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR21351:SF0; BARDET-BIEDL SYNDROME 5 PROTEIN; 1.
DR   PANTHER; PTHR21351; BARDET-BIEDL SYNDROME PROTEIN 5; 1.
DR   Pfam; PF07289; BBL5; 1.
DR   Pfam; PF24681; Kelch_KLHDC2_KLHL20_DRC7; 1.
DR   SMART; SM00683; DM16; 2.
DR   SMART; SM00612; Kelch; 3.
DR   SUPFAM; SSF117281; Kelch motif; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   DOMAIN          28..82
FT                   /note="BBSome complex member BBS5 PH"
FT                   /evidence="ECO:0000259|SMART:SM00683"
FT   DOMAIN          158..212
FT                   /note="BBSome complex member BBS5 PH"
FT                   /evidence="ECO:0000259|SMART:SM00683"
SQ   SEQUENCE   544 AA;  61062 MW;  3A4A7C4380E73D20 CRC64;
     MSVLDALWED RDVRFDVSSQ QMKTRPGEVL IDCLDSVEDT KGNNGDRGRL LVTNLRIVWH
     SLALPRVNLS IGYNCILNIT TRTANSKLRG QTEALYVLTK CNSTRFEFIF TNLVPGSPRL
     YTSLIAVHRA YETSKMYRDF KLRSALIQNK QLRLLPQENV YNKINGVWNL SSDQGNLGTF
     FITNVRIVWH ANMNDSFNVS IPYLQIRSVK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV
     EKLQESVKEI NSLHKVYSAN PIFGVDYEME EKPQPLEALT VKQIQDDVEI DSDDHTDAFV
     AYFADGNKLD NVASEWVGLP PLPSARCLFG LGEIDDKIYV VAGKDLQTEA SLDTVLCYDP
     AAAKWNEVKK LPIKVYGHSV ISHKGMIYCL GGKTDDKKCT NRVFIYNPKK GDWKDLAPMK
     IPRSMFGVAV HKGKIVIAGG VTEDGLSASV EAFDLNTNKW EVMTEFPQER SSISLVSLAG
     SLYAIGGFAM IQLESKEFAP TEVNDIWKYE DDKKEWAGML KEIRYASGAS CLATRLNLFK
     LSKL
//
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