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Database: UniProt
Entry: A0AA40HT93_CNENI
LinkDB: A0AA40HT93_CNENI
Original site: A0AA40HT93_CNENI 
ID   A0AA40HT93_CNENI        Unreviewed;       341 AA.
AC   A0AA40HT93;
DT   24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2024, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   RecName: Full=Bardet-Biedl syndrome 5 protein homolog {ECO:0000256|PIRNR:PIRNR010072};
GN   ORFNames=QTO34_002944 {ECO:0000313|EMBL:KAK1336908.1};
OS   Cnephaeus nilssonii (Northern bat) (Eptesicus nilssonii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC   Cnephaeus.
OX   NCBI_TaxID=3371016 {ECO:0000313|EMBL:KAK1336908.1, ECO:0000313|Proteomes:UP001177744};
RN   [1] {ECO:0000313|EMBL:KAK1336908.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BLF_Eptnil {ECO:0000313|EMBL:KAK1336908.1};
RC   TISSUE=Kidney {ECO:0000313|EMBL:KAK1336908.1};
RA   Laine V.N., Pulliainen A.T., Lilley T.M.;
RT   "Reference genome for the Northern bat (Eptesicus nilssonii), a most
RT   northern bat species.";
RL   Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|PIRNR:PIRNR010072}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAK1336908.1}.
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DR   EMBL; JAULJE010000012; KAK1336908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AA40HT93; -.
DR   Proteomes; UP001177744; Unassembled WGS sequence.
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; 1.
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:UP001177744};
KW   Transport {ECO:0000256|PIRNR:PIRNR010072}.
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   341 AA;  38731 MW;  65B6AABC28E1DC23 CRC64;
     MSVLDALWED RDVRFDVSSQ QMKTRPGEVL IDCLDSIEDT KGNNGDRGRL LVTNLRILWH
     SLALPRVNLS IGYNCILTIT TRTANSKLRG QTEALYILTK CNSTRFEFIF TNLIPGSPRL
     FTSVIAVHRA YETSKMYRDF KLRSALIQNK ELRLLPQEHV YDKINGVWNL SSDQGNLGTF
     FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV
     EKLQASVKEI NSLHKVYSAS PIFGVDYEME EKPQPLEALT VEQIQDDVEI DSDDHPDAFV
     AYCADGNKQQ DREPVFSEEL GLAIEKLKDG FTLQGLWEVM S
//
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