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Database: UniProt
Entry: A0A8B9WNN6_BOSMU
LinkDB: A0A8B9WNN6_BOSMU
Original site: A0A8B9WNN6_BOSMU 
ID   A0A8B9WNN6_BOSMU        Unreviewed;       341 AA.
AC   A0A8B9WNN6;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=Bardet-Biedl syndrome 5 protein homolog {ECO:0000256|PIRNR:PIRNR010072};
GN   Name=BBS5 {ECO:0000313|Ensembl:ENSBGRP00000010355.1};
OS   Bos mutus grunniens (Wild yak) (Bos grunniens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30521 {ECO:0000313|Ensembl:ENSBGRP00000010355.1, ECO:0000313|Proteomes:UP000694520};
RN   [1] {ECO:0000313|Ensembl:ENSBGRP00000010355.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang S., Liu J.;
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBGRP00000010355.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSBGRP00000010355.1}
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|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   AlphaFoldDB; A0A8B9WNN6; -.
DR   Ensembl; ENSBGRT00000011917.1; ENSBGRP00000010355.1; ENSBGRG00000006370.1.
DR   GeneTree; ENSGT00390000002753; -.
DR   Proteomes; UP000694520; Chromosome 2.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
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:UP000694520};
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;  38852 MW;  81272880AC287846 CRC64;
     MSVLDALWED RDVRFDVSSQ QMKTRPGEVL IDCLDSVEDT KGNNGDRGRL LVTNLRIVWH
     SLALPRVNLS IGYNCILNIT TRTANSKLRG QTEALYVLTK CNSTRFEFIF TNLVPGSPRL
     YTSLIAVHRA YETSKMYRDF KLRSALIQNK QLRLLPQENV YNKINGVWNL SSDQGNLGTF
     FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV
     EKLQESVKEI NSLHKVYSAN PIFGVDYEME EKPQPLEALT VKQIQDDVEI DSDDHTDAFV
     AYFADGNKQQ DREPVFSEEL GLAIEKLKDG FTLQGLWEVM N
//
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