MKKS_PONAB
ID MKKS_PONAB Reviewed; 570 AA.
AC Q5R4T7; Q5RD80;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Molecular chaperone MKKS {ECO:0000305};
DE AltName: Full=McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin;
DE AltName: Full=Protein Bbs6 homolog;
GN Name=MKKS; Synonyms=BBS6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable molecular chaperone that assists the folding of
CC proteins upon ATP hydrolysis. Plays a role in the assembly of BBSome, a
CC complex involved in ciliogenesis regulating transports vesicles to the
CC cilia. May play a role in protein processing in limb, cardiac and
CC reproductive system development. May play a role in cytokinesis.
CC {ECO:0000250|UniProtKB:Q9NPJ1}.
CC -!- SUBUNIT: Component of a complex composed at least of MKKS, BBS10,
CC BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Interacts with STUB1.
CC Interacts with BBS2 (via coiled coil domain). Interacts with CCDC28B.
CC Interacts with BBS12. Interacts with SMARCC1, a component of the
CC SWI/SNF complexes; the interaction takes place predominantly in the
CC cytoplasm and may modulate SMARCC1 location (By similarity). Interacts
CC with DLEC1 (By similarity). {ECO:0000250|UniProtKB:Q9NPJ1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q9NPJ1}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NPJ1}. Nucleus {ECO:0000250|UniProtKB:Q9NPJ1}.
CC Note=The majority of the protein resides within the pericentriolar
CC material (PCM), a proteinaceous tube surrounding centrioles. During
CC interphase, the protein is confined to the lateral surfaces of the PCM
CC but during mitosis it relocalizes throughout the PCM and is found at
CC the intercellular bridge. The MKSS protein is highly mobile and rapidly
CC shuttles between the cytosol and centrosome.
CC {ECO:0000250|UniProtKB:Q9NPJ1}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; CR858036; CAH90277.1; -; mRNA.
DR EMBL; CR861155; CAH93229.1; -; mRNA.
DR RefSeq; NP_001125124.1; NM_001131652.1.
DR RefSeq; XP_009231560.1; XM_009233285.1.
DR AlphaFoldDB; Q5R4T7; -.
DR SMR; Q5R4T7; -.
DR STRING; 9601.ENSPPYP00000011971; -.
DR GeneID; 100172008; -.
DR KEGG; pon:100172008; -.
DR CTD; 8195; -.
DR eggNOG; KOG0360; Eukaryota.
DR HOGENOM; CLU_478131_0_0_1; -.
DR InParanoid; Q5R4T7; -.
DR OMA; FVCQKVI; -.
DR OrthoDB; 1539473at2759; -.
DR TreeFam; TF329106; -.
DR Proteomes; UP000001595; Chromosome 20.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:1902636; C:kinociliary basal body; IEA:Ensembl.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl.
DR GO; GO:0060324; P:face development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; 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:0045776; P:negative regulation of blood pressure; 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:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IEA:Ensembl.
DR GO; GO:0051492; P:regulation of stress fiber assembly; 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:0042311; P:vasodilation; IEA:Ensembl.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR028790; MKKS.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR46787; PTHR46787; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..570
FT /note="Molecular chaperone MKKS"
FT /id="PRO_0000128417"
FT REGION 198..370
FT /note="Substrate-binding apical domain"
FT /evidence="ECO:0000250|UniProtKB:Q9NPJ1"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 100
FT /note="C -> R (in Ref. 1; CAH93229)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="N -> D (in Ref. 1; CAH90277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 62436 MW; C2959757F42568CB CRC64;
MSRLEAKKPS LCKSEPLTTE RVRTTLSVFK RIVTSCYGPS GRLKQLHNGF GGYVCTTSQS
SALLSHLLVT HPILKILTTS IQNHVSSFSD CGLFTAILCC NLIENVQRLD LTPTTVIRLN
KHLLSLCISY LKSETCGCRI PVDFGSTQIL LCFVRSVLTS KPACMLTRKE TEHVSALILR
AFLLTIPENA EGHIILGKSL IVPLKGQRVI DSTVLPGILI EMSEVQLMRL LPIKKSTALK
VALFCTTLSG DISDTGEGTV VVSYGVSLEN AALDQLLNLG RQLISDHVDL VLCQKVIHPS
LKQFLNMHRI IAIDRIGVTL MEPLTKMTGT QPIGSLGSIS PNSYGSVKDV CTAKFGSKHF
FHLIPNEATI CSLLLCNRND TAWDELKLTC QTALHVLQLT LKEPWALLGG GCTETHLAAY
IRHKTHNDPE SILKDDECTQ TELQLIAEAF CSALESVVGS LEHDGGEILT DMKYGHLWSV
QADSPCVANW PDLLSQCGCG LYNSQEELNW SFLRSTRRPF VPQTCLPHEA VGSASNLTLD
CLTAKLSGLQ VAVETANLIL DLSYVIEDKN
