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Database: UniProt
Entry: A0A2R9BW62_PANPA
LinkDB: A0A2R9BW62_PANPA
Original site: A0A2R9BW62_PANPA 
ID   A0A2R9BW62_PANPA        Unreviewed;       320 AA.
AC   A0A2R9BW62;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   28-JAN-2026, entry version 35.
DE   RecName: Full=Bardet-Biedl syndrome 5 protein homolog {ECO:0000256|PIRNR:PIRNR010072};
GN   Name=BBS5 {ECO:0000313|Ensembl:ENSPPAP00000033922.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000033922.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000033922.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000033922.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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|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   EMBL; AJFE02085449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008976294.1; XM_008978046.4.
DR   AlphaFoldDB; A0A2R9BW62; -.
DR   SMR; A0A2R9BW62; -.
DR   Ensembl; ENSPPAT00000056803.1; ENSPPAP00000033922.1; ENSPPAG00000039822.1.
DR   GeneID; 100981691; -.
DR   CTD; 129880; -.
DR   GeneTree; ENSGT00390000002753; -.
DR   Proteomes; UP000240080; Unplaced.
DR   Bgee; ENSPPAG00000039822; Expressed in testis and 6 other cell types or tissues.
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   InterPro; IPR006606; BBL5.
DR   InterPro; IPR030804; BBS5/fem-3.
DR   InterPro; IPR014003; BBS5_PH.
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:UP000240080};
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   320 AA;  36397 MW;  843BC731AE686410 CRC64;
     MSVLDALWED RDVRFDLSAQ QMKTRPGEVL IDCLDSIEDT KGNNGDRGRL LVTNLRILWH
     SLALSRVNVS VGYNCILNIT TRTANSKLRG QTEALYILTK CNSTRFEFIF TNLVPGSPRL
     FTSVMAVHRA YETSKMYRDF KLRSALIQNK QLRLLPQEHV YDKINGVWNL SSDQGNLGTF
     FITNVRIVWH ANMNDSFNVS IPYLQISGGY VLGFKIDPVE KLQESVKEIN SLHKVYSASP
     IFGVDYEMEE KPQPLEALTV EQIQDDVEID SDGHTDAFVA YFADGNKQQD REPVFSEELG
     LAIEKLKDGF TLQGLWEVMS
//
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