ID A0A2Y9DJ10_TRIMA Unreviewed; 445 AA.
AC A0A2Y9DJ10;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=BBSome complex member BBS5 {ECO:0000256|ARBA:ARBA00047191};
GN Name=BBS5 {ECO:0000313|RefSeq:XP_004375598.2};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004375598.2};
RN [1] {ECO:0000313|RefSeq:XP_004375598.2}
RP IDENTIFICATION.
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_004375598.2; XM_004375541.2.
DR FunCoup; A0A2Y9DJ10; 184.
DR STRING; 127582.A0A2Y9DJ10; -.
DR GeneID; 101350885; -.
DR KEGG; tmu:101350885; -.
DR CTD; 129880; -.
DR InParanoid; A0A2Y9DJ10; -.
DR Proteomes; UP000248480; 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; 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 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:UP000248480}.
FT DOMAIN 132..186
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
FT DOMAIN 262..316
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
SQ SEQUENCE 445 AA; 49911 MW; 79F219E686AF77B4 CRC64;
MGKGVEWLKD VCLEAKKVAR KSCTCLSARA SSPSIRDSSL TSQIGLVRRK CKATSVKART
IPEEAWVSAP AVDVVTEAAC CLGAGETRFG LXSCGERRPR ATIIMSVLDA LWEDRDVRFD
VSSQQMKTRP GEVLIDCLDS IEDTKGNNGD RGRLLVTNLR IIWHSLALPR VNLSVGYNCI
LNITTRTANS KLRGQTEALY ILTKCNSTRF EFIFTNVVPG SPRLFTSVIA VHRAYETSKM
YRDFKLRSAL IQNKQLRLLP QEHVYDKISG VWNLSSDQGN LGTFFITNVR IVWHANMNDS
FNVSIPYLQI RSIKIRDSKF GLALVIESSQ QSGGYVLGFK IDPVEKLQES VKEINSLHKV
YSASPIFGVD YEMEEKPQPL EALTVEQIQD DVEIDSDDHR DAFVAYFADG NKQQDREPVF
SEELGLAIEK LKDGFTLQGL WEVMS
//
