ID   BBS10_PONAB             Reviewed;         723 AA.
AC   Q5R8P3; Q5RFC0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Bardet-Biedl syndrome 10 protein homolog;
GN   Name=BBS10;
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=Kidney;
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. Involved in adipogenic differentiation.
CC       {ECO:0000250|UniProtKB:Q8TAM1}.
CC   -!- SUBUNIT: Component of a complex composed at least of MKKS, BBS10,
CC       BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC       {ECO:0000250|UniProtKB:Q8TAM1}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q8TAM1}. Note=Located within the basal body of
CC       the primary cilium of differentiating preadipocytes.
CC       {ECO:0000250|UniProtKB:Q8TAM1}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH89537.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR857240; CAH89537.1; ALT_INIT; mRNA.
DR   EMBL; CR859708; CAH91867.1; -; mRNA.
DR   RefSeq; NP_001126082.1; NM_001132610.1.
DR   AlphaFoldDB; Q5R8P3; -.
DR   STRING; 9601.ENSPPYP00000005455; -.
DR   PRIDE; Q5R8P3; -.
DR   GeneID; 100173034; -.
DR   KEGG; pon:100173034; -.
DR   CTD; 79738; -.
DR   eggNOG; KOG0357; Eukaryota.
DR   eggNOG; KOG0360; Eukaryota.
DR   InParanoid; Q5R8P3; -.
DR   OrthoDB; 1411586at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:InterPro.
DR   Gene3D; 1.10.560.10; -; 2.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR042619; BBS10.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   PANTHER; PTHR14667; PTHR14667; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   SUPFAM; SSF48592; SSF48592; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell projection; Chaperone; Cilium; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..723
FT                   /note="Bardet-Biedl syndrome 10 protein homolog"
FT                   /id="PRO_0000235274"
FT   CONFLICT        42
FT                   /note="T -> A (in Ref. 1; CAH89537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="A -> T (in Ref. 1; CAH89537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="Q -> R (in Ref. 1; CAH89537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="P -> S (in Ref. 1; CAH89537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696
FT                   /note="T -> A (in Ref. 1; CAH89537)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   723 AA;  80596 MW;  A2D197963926F6D2 CRC64;
     MLSSMVAAGS VKAALQVAEV LEAIVSCCVG PEGRQVLCTK PTGEVLLSRN GGRLLEALHL
     EHPIARMIVD CVSSHLKKTG DGAKTFIIFL CHLLRGLHAI TDSEKDPLMC ENIQTHGRHW
     KNCSQWKCIS QALLTFQTQI LDGIMDQYLS RHFLSIFSSA KEKTLCRSSL ELLLEAYFCG
     RVGRNNHKFI SQLMCDYFFK CMTCESGIGV FELVDDYFVE LNVGVTGLPV SDSRIIAGLV
     LQKDFSVYCP ADGDIRMVIV TETVQPLFST SGSEFILNSE AQFQTSQFWI MEKTQAIMKH
     LHSQNVKLLI SSVKQPDLVI YYAGVNGISV VECLSSEEVS LIRRIIGLSP FVPPQAFSQC
     EIPNTALVKF CKPLILRSKR YVHLGLISTC AFIPHSIVLC GPLQGLIEQH EDALHGAFKM
     LRQLFKDLDL SYITQTNDQN GTSSLFIYKN SGESYQAPDT GNGSIQRPYQ DTVVENKDEL
     EKTQTYLKVH SNLVISDVEL ETYIPYSTPT LTPTDTFQTV ETLTCLSLER NRLTDYYEPL
     LKNNSTAYST RGNRIEISYE NLQVTNITGK GSMLPVSCKL QNMGTSQSYL SSSMPAGCVL
     PVGGNFEILL HYYLLNYAKK CHQPEETMVS MIIANALLGI PKVLYKSKTG KYSFPHTYIR
     AVHALQTNQP LVSSQTGLES VTGKYQLLTS VLQCLTKILT IDVVITVKRD PQKVHNQDSE
     DEL