BBS4_BOVIN
ID BBS4_BOVIN Reviewed; 519 AA.
AC Q1JQ97;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Bardet-Biedl syndrome 4 protein homolog;
GN Name=BBS4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be required for the dynein-mediated transport of
CC pericentriolar proteins to the centrosome. Required for microtubule
CC anchoring at the centrosome but not for microtubule nucleation. The
CC BBSome complex is required for ciliogenesis but is dispensable for
CC centriolar satellite function. This ciliogenic function is mediated in
CC part by the Rab8 GDP/GTP exchange factor, which localizes to the basal
CC body and contacts the BBSome. Rab8(GTP) enters the primary cilium and
CC promotes extension of the ciliary membrane. Firstly the BBSome
CC associates with the ciliary membrane and binds to RAB3IP/Rabin8, the
CC guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes
CC to the cilium and promotes docking and fusion of carrier vesicles to
CC the base of the ciliary membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8, BBS9 and BBIP10 (By similarity). Interacts with PCM1 and
CC DCTN1 (By similarity). Interacts with CCDC28B (By similarity).
CC Interacts with ALDOB and C2CD3 (By similarity). Interacts with PKD1 (By
CC similarity). Interacts with CEP290 (By similarity). Interacts with
CC DLEC1 (By similarity). {ECO:0000250|UniProtKB:Q96RK4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cell projection, cilium membrane
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriolar satellite
CC {ECO:0000250}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q8C1Z7}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q8C1Z7}. Note=Localizes to the pericentriolar
CC material. Centrosomal localization requires dynein (By similarity).
CC Localizes to the connecting cilium of photoreceptor cells (By
CC similarity). {ECO:0000250|UniProtKB:Q8C1Z7}.
CC -!- SIMILARITY: Belongs to the BBS4 family. {ECO:0000305}.
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DR EMBL; BC116137; AAI16138.1; -; mRNA.
DR RefSeq; NP_001069424.1; NM_001075956.1.
DR PDB; 6VBU; EM; 3.10 A; 4=1-519.
DR PDB; 6VBV; EM; 3.50 A; 4=1-519.
DR PDB; 6VNW; EM; 3.44 A; E=1-519.
DR PDB; 6VOA; EM; 4.00 A; E=1-519.
DR PDBsum; 6VBU; -.
DR PDBsum; 6VBV; -.
DR PDBsum; 6VNW; -.
DR PDBsum; 6VOA; -.
DR AlphaFoldDB; Q1JQ97; -.
DR SMR; Q1JQ97; -.
DR DIP; DIP-61536N; -.
DR IntAct; Q1JQ97; 2.
DR STRING; 9913.ENSBTAP00000010013; -.
DR PaxDb; Q1JQ97; -.
DR PRIDE; Q1JQ97; -.
DR Ensembl; ENSBTAT00000010013; ENSBTAP00000010013; ENSBTAG00000007614.
DR GeneID; 532120; -.
DR KEGG; bta:532120; -.
DR CTD; 585; -.
DR VEuPathDB; HostDB:ENSBTAG00000007614; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000158166; -.
DR HOGENOM; CLU_033477_1_0_1; -.
DR InParanoid; Q1JQ97; -.
DR OMA; WNNIGAC; -.
DR OrthoDB; 609083at2759; -.
DR TreeFam; TF324966; -.
DR Reactome; R-BTA-5620922; BBSome-mediated cargo-targeting to cilium.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000007614; Expressed in oviduct epithelium and 107 other tissues.
DR ExpressionAtlas; Q1JQ97; baseline and differential.
DR GO; GO:0034464; C:BBSome; IEA:Ensembl.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:GOC.
DR GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR GO; GO:0034452; F:dynactin binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0060324; P:face development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IEA:Ensembl.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl.
DR GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IEA:Ensembl.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR GO; GO:1902855; P:regulation of non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0046548; P:retinal rod cell development; IEA:Ensembl.
DR GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR028786; BBS4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44186; PTHR44186; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Flagellum;
KW Membrane; Protein transport; Reference proteome; Repeat; TPR repeat;
KW Transport.
FT CHAIN 1..519
FT /note="Bardet-Biedl syndrome 4 protein homolog"
FT /id="PRO_0000284042"
FT REPEAT 67..100
FT /note="TPR 1"
FT REPEAT 101..134
FT /note="TPR 2"
FT REPEAT 135..168
FT /note="TPR 3"
FT REPEAT 169..201
FT /note="TPR 4"
FT REPEAT 203..235
FT /note="TPR 5"
FT REPEAT 237..269
FT /note="TPR 6"
FT REPEAT 270..303
FT /note="TPR 7"
FT REPEAT 304..337
FT /note="TPR 8"
FT REPEAT 339..371
FT /note="TPR 9"
FT REPEAT 379..417
FT /note="TPR 10"
FT REGION 1..66
FT /note="Required for localization to centrosomes"
FT /evidence="ECO:0000250"
FT REGION 101..337
FT /note="Interaction with PCM1"
FT /evidence="ECO:0000250"
FT REGION 338..519
FT /note="Required for localization to centrosomes"
FT /evidence="ECO:0000250"
FT REGION 439..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:6VBV"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:6VBU"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:6VBU"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:6VBU"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:6VBU"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 355..367
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:6VBU"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:6VBU"
SQ SEQUENCE 519 AA; 58221 MW; C96333782E9C2769 CRC64;
MAEEKLSART QLPVSAESQK PVLKKAPEFP ILEKQNWLIH LYYIQKDYEA CKAVIKEQLQ
ETHGLCEYAI YVQALIFRLE GNIQESLRLF QMCAFLSPQC ADNLKQVARS LFLLGKHKAA
IEVYNEAAKL NQKDWEICHN LGVCYIYLKQ FDKAQDQLHN ALHLNRHDLT YIMLGKIFLL
KGDLDKAIEI YKKAVEFSPE NTELLTTLGL LYLQLGIYQK AFEHLGNTLT YDPTNYKAIL
AAGSMMQTHG DFDVALTKYK VVACAVIESP PLWNNIGMCF FGKKKYVAAI SCLKRANYLA
PLDWKILYNL GLVHLTMQQY ASAFHFLSAA INFQPKMGEL YMLLAVALTN LEDSENAKRA
YEEAVRLDKC NPLVNLNYAV LLYNQGEKRD ALAQYQEMEK KVNLLKYSSS LEFDPEMVEV
AQKLGAALQV GEALVWTKPV KDPKSKHQTA STSKAAGFQQ PLGSNQALGQ AMSSAATCRK
LSSGAGGTSQ LTKPPSLPLE PEPTVEAQPT EASAQTREK
