ID A0A6J3J2Z7_SAPAP Unreviewed; 319 AA.
AC A0A6J3J2Z7;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Bardet-Biedl syndrome 5 protein homolog {ECO:0000256|PIRNR:PIRNR010072};
GN Name=BBS5 {ECO:0000313|RefSeq:XP_032148948.1};
OS Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Sapajus.
OX NCBI_TaxID=9515 {ECO:0000313|Proteomes:UP000504640, ECO:0000313|RefSeq:XP_032148948.1};
RN [1] {ECO:0000313|RefSeq:XP_032148948.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_032148948.1};
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 ECO:0000256|PIRNR:PIRNR010072}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Binds to phosphoinositides. Interacts
CC with CCDC28B. Interacts with SMO; the interaction is indicative for the
CC association of SMO with the BBsome complex to facilitate ciliary
CC localization of SMO. Interacts with PKD1. Interacts with DLEC1.
CC {ECO:0000256|ARBA:ARBA00066146}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000256|ARBA:ARBA00004309, ECO:0000256|PIRNR:PIRNR010072}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000256|ARBA:ARBA00004607}.
CC -!- SIMILARITY: Belongs to the BBS5 family. {ECO:0000256|ARBA:ARBA00005822,
CC ECO:0000256|PIRNR:PIRNR010072}.
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DR RefSeq; XP_032148948.1; XM_032293057.1.
DR AlphaFoldDB; A0A6J3J2Z7; -.
DR GeneID; 116561211; -.
DR CTD; 129880; -.
DR Proteomes; UP000504640; Unplaced.
DR GO; GO:0034464; C:BBSome; IEA:UniProtKB-UniRule.
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 GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 2.
DR PIRSF; PIRSF010072; DUF1448; 1.
DR SMART; SM00683; DM16; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR010072};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273,
KW ECO:0000256|PIRNR:PIRNR010072};
KW Cilium {ECO:0000256|ARBA:ARBA00023069, ECO:0000256|PIRNR:PIRNR010072};
KW Cilium biogenesis/degradation {ECO:0000256|PIRNR:PIRNR010072};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR010072};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR010072};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR010072};
KW Protein transport {ECO:0000256|PIRNR:PIRNR010072};
KW Reference proteome {ECO:0000313|Proteomes:UP000504640};
KW Transport {ECO:0000256|PIRNR:PIRNR010072}.
FT DOMAIN 28..60
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
FT DOMAIN 136..190
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
SQ SEQUENCE 319 AA; 36298 MW; F1656FE2A2726CE0 CRC64;
MSVLDALWED RDVRFDLSAQ QMKTRPGEVL IDCLDSIEDT KGNNGDRAVG YNCILNITTR
TANSKLRGQT EALYILTKCN STRFEFIFTN LVPGSPRLFT SVMAVHRAYE TSKMYRDFKL
RSALIQNKQL RLLPQEHVYD KINGVWNLSS DQGNLGTFFI TNVRIVWHAN MNDSFNVSIP
YLQIRSIKIR DSKFGLALVI ESSQQSGGYV LGFKIDPVEK LQESVKEINS LHKIYSASPI
FGVDYEMEEK PQPLEALTVE QIQDDVEIDS DDHTDAFVAY FADGNKQQDR EPVFSEELGL
AIEKLKDGFT LQGLWEVMS
//
