ID A0A667H969_LYNCA Unreviewed; 918 AA.
AC A0A667H969;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=BBSome complex member BBS5 {ECO:0000256|ARBA:ARBA00047191};
DE AltName: Full=Kelch repeat and BTB domain-containing protein 10 {ECO:0000256|ARBA:ARBA00076804};
DE AltName: Full=Kelch-like protein 41 {ECO:0000256|ARBA:ARBA00069965};
GN Name=BBS5 {ECO:0000313|Ensembl:ENSLCNP00005017038.1};
OS Lynx canadensis (Canada lynx) (Felis canadensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=61383 {ECO:0000313|Ensembl:ENSLCNP00005017038.1, ECO:0000313|Proteomes:UP000472241};
RN [1] {ECO:0000313|Ensembl:ENSLCNP00005017038.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLCNP00005017038.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Involved in skeletal muscle development and differentiation.
CC Regulates proliferation and differentiation of myoblasts and plays a
CC role in myofibril assembly by promoting lateral fusion of adjacent thin
CC fibrils into mature, wide myofibrils. Required for pseudopod elongation
CC in transformed cells. {ECO:0000256|ARBA:ARBA00053582}.
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}. Cell projection, pseudopodium
CC {ECO:0000256|ARBA:ARBA00037818}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000256|ARBA:ARBA00004607}. Sarcoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004449}.
CC -!- SIMILARITY: Belongs to the BBS5 family.
CC {ECO:0000256|ARBA:ARBA00005822}.
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DR AlphaFoldDB; A0A667H969; -.
DR Ensembl; ENSLCNT00005019113.1; ENSLCNP00005017038.1; ENSLCNG00005011205.1.
DR Proteomes; UP000472241; 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:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum 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; cd18517; BACK_KLHL41_KBTBD10; 1.
DR CDD; cd18341; BTB_POZ_KLHL41_KBTBD10; 1.
DR CDD; cd00900; PH-like; 1.
DR FunFam; 2.30.29.30:FF:000232; Bardet-Biedl syndrome 5 isoform 1; 1.
DR FunFam; 3.30.710.10:FF:000006; Kelch repeat and BTB domain-containing 6; 1.
DR FunFam; 1.25.40.420:FF:000001; Kelch-like family member 12; 1.
DR FunFam; 2.120.10.80:FF:000025; Kelch-like family member 41; 1.
DR Gene3D; 1.25.40.420; -; 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 Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR006606; BBL5.
DR InterPro; IPR014003; BBS5_PH.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030571; KLHL41_KL41B_BTB_POZ_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR21351:SF0; BARDET-BIEDL SYNDROME 5 PROTEIN; 1.
DR PANTHER; PTHR21351; BARDET-BIEDL SYNDROME PROTEIN 5; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF07289; BBL5; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF24681; Kelch_KLHDC2_KLHL20_DRC7; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00683; DM16; 2.
DR SMART; SM00612; Kelch; 4.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 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:UP000472241};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 345..412
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
SQ SEQUENCE 918 AA; 103608 MW; 240EAE3C7A319317 CRC64;
MSVLDALWED RDVRFDVSSQ QMKTRPGEAL IDCLDSIEDT KGNNGDRGRL LVTNLRIIWH
SLALPRVNLS IGYNCILNIT TRTANSKLRG QSEALYILTK CNSTRFEFIF TNLVPGSPRL
FTSVIAVHRA YETSKMYRDF KLRSALIQNK QLRLLPQEHV YDKINGVWNL SSDQGNLGTF
FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV
EKLQESVKEI NSLHKVYSAS PIFGVDYEME EKPQPLEALT VEQIQDDVEI DSDDHTDAFV
AYFADGNKVT HKMDSQRELT EELRLYQSTL LQDGLKDLLD EKKFIDCTLK AGDKSLPCHR
LILSACSPYF REYFLSEIDE GKKKEVVLDN VDPAVLDLII KYLYSASIDL NDGNVQDIFA
LASRFQIPSV FTVCVSYLQK RLAPGNCLAI LRLGLLLDCP RLAISAREFV SDRFVQICKE
EDFMQLSPQE LISVISNDSL NVEKEEAVFE AVMKWVRTDK ENRVKNLSEV FDCIRFRLMT
EKYFKDHVEK DDIIKSNPEL QKKIKVLKDA FAGKLPEPSK NAEKSGAGEV NGDVGDEDLL
PGYLNDIPRH GMFVKDLILL VNDTAAVAYD PTENECYLTA LAEQIPRNHS SIVTQQNQVY
VVGGLYVDEE NKDQPLQSYF FQLDNIASEW VGLPPLPSAR CLFGLGEVDD KIYVVAGKDL
QTEASLDSVL CYDPVTAKWN EVKKLPIKVY GHSVISHKGM IYCLGGKTDD KKCTNRVFIY
NPKKGDWKDV APMKTPRSMF GVAIHKGKIV IAGGVTEDGL SASVEAFDLI TNKWEVMTEF
PQERSSISLV SLAGSLYAIG GFAMIQLESK EFAPTEVNDI WKYEDDKKEW AGMLKEIRYA
SGASCLATRL NLFKLSKL
//
