ID A0A3Q7MLI7_CALUR Unreviewed; 302 AA.
AC A0A3Q7MLI7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=BBSome complex member BBS5 {ECO:0000256|ARBA:ARBA00047191};
GN Name=LOC112808786 {ECO:0000313|RefSeq:XP_025707858.1};
OS Callorhinus ursinus (Northern fur seal).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Otariidae;
OC Callorhinus.
OX NCBI_TaxID=34884 {ECO:0000313|Proteomes:UP000286641, ECO:0000313|RefSeq:XP_025707858.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025707858.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025707858.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_025707858.1; XM_025852073.1.
DR AlphaFoldDB; A0A3Q7MLI7; -.
DR Proteomes; UP000286641; Unplaced.
DR GO; GO:0034464; C:BBSome; IEA:InterPro.
DR GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IEA:TreeGrafter.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:TreeGrafter.
DR GO; GO:0060271; P:cilium assembly; IEA:TreeGrafter.
DR CDD; cd00900; PH-like; 1.
DR FunFam; 2.30.29.30:FF:000232; Bardet-Biedl syndrome 5 isoform 1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR006606; BBL5.
DR InterPro; IPR030804; BBS5/fem-3.
DR InterPro; IPR014003; BBS5_PH.
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 PIRSF; PIRSF010072; DUF1448; 1.
DR SMART; SM00683; DM16; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000286641}.
FT DOMAIN 10..43
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
FT DOMAIN 119..173
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
SQ SEQUENCE 302 AA; 34400 MW; 2887CE9BE867BE1B CRC64;
MSASTSPRSR LLVTNLRIIW HSLALPRVNL SIGYNCILNI TTRTANSKLR GQTEALYILT
KCNSTRFEFI FTNLVPGSPR LFTSVIAVHR AYETSKMYRD FKLRSALIQN KQLRLLPQEH
VYDKINGVWN LSSDQGNLGT FFITNVRIVW HANMNDSFNV SIPYLQIRSI KIRDSKFGLA
LVIESSQQSG GYVLGFKIDP VEKLQESVKE INSLHKVYSA SPIFGVDYEM EEKPQPLEAL
RVEQIQDDVE IDSDDHTDAF VAYFADGNKQ QDREPVFSEE LGLAIEKLKD GFTLQGLWEV
MS
//
