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Database: UniProt
Entry: A0A9W3H451_CAMBA
LinkDB: A0A9W3H451_CAMBA
Original site: A0A9W3H451_CAMBA 
ID   A0A9W3H451_CAMBA        Unreviewed;       341 AA.
AC   A0A9W3H451;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2025, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   RecName: Full=Bardet-Biedl syndrome 5 protein homolog {ECO:0000256|PIRNR:PIRNR010072};
GN   Name=BBS5 {ECO:0000313|RefSeq:XP_010969733.1};
OS   Camelus bactrianus (Bactrian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9837 {ECO:0000313|Proteomes:UP001732780, ECO:0000313|RefSeq:XP_010969733.1};
RN   [1] {ECO:0000313|RefSeq:XP_010969733.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_010969733.1};
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. {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}.
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DR   RefSeq; XP_010969733.1; XM_010971431.2.
DR   AlphaFoldDB; A0A9W3H451; -.
DR   GeneID; 105081984; -.
DR   KEGG; cbai:105081984; -.
DR   CTD; 129880; -.
DR   OrthoDB; 10261999at2759; -.
DR   Proteomes; UP001732780; Chromosome 5.
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:UP001732780};
KW   Transport {ECO:0000256|PIRNR:PIRNR010072}.
SQ   SEQUENCE   341 AA;  38869 MW;  30AF464565E9A708 CRC64;
     MSVLDALWED RDVRFDVSSQ QMKTRPGEVL IDCLDSIEDT KGNNGDRGRL LVTNLRIIWH
     SLALPRVNLS IGYNCILNIT TRTANSKLRG QTEALYILTK CNSTRFEFIF TNLVPGSPRL
     FTSVIAVHRA YETSKMYRDF KLRSALIQNK QLRLLPQEHV YDKINGVWNL SSDQGNLGTF
     FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV
     EKLQESVKEI NSFHKVYSAS PIFGVDYEME EKPQPLEALT VEQIQDDVEI DSDDHTDAFV
     AYFADGNKQQ DREPVFSEEL GLAIEKLKDG FTLQGLWEVM S
//
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