LOCUS       NP_001100296             520 aa            linear   ROD 03-APR-2024
DEFINITION  Bardet-Biedl syndrome 4 protein [Rattus norvegicus].
ACCESSION   NP_001100296 XP_001074984 XP_217154
VERSION     NP_001100296.1
DBSOURCE    REFSEQ: accession NM_001106826.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,B., Wang,G., Xu,X., Yang,S., Zhuang,T., Wang,G., Ren,H.,
            Cheng,S.Y., Jiang,Q. and Zhang,C.
  TITLE     DAZ-interacting Protein 1 (Dzip1) Phosphorylation by Polo-like
            Kinase 1 (Plk1) Regulates the Centriolar Satellite Localization of
            the BBSome Protein during the Cell Cycle
  JOURNAL   J Biol Chem 292 (4), 1351-1360 (2017)
   PUBMED   27979967
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Agassandian,K., Patel,M., Agassandian,M., Steren,K.E., Rahmouni,K.,
            Sheffield,V.C. and Card,J.P.
  TITLE     Ciliopathy is differentially distributed in the brain of a
            Bardet-Biedl syndrome mouse model
  JOURNAL   PLoS One 9 (4), e93484 (2014)
   PUBMED   24695551
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Chamling,X., Seo,S., Searby,C.C., Kim,G., Slusarski,D.C. and
            Sheffield,V.C.
  TITLE     The centriolar satellite protein AZI1 interacts with BBS4 and
            regulates ciliary trafficking of the BBSome
  JOURNAL   PLoS Genet 10 (2), e1004083 (2014)
   PUBMED   24550735
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Ye,X., Zeng,H., Ning,G., Reiter,J.F. and Liu,A.
  TITLE     C2cd3 is critical for centriolar distal appendage assembly and
            ciliary vesicle docking in mammals
  JOURNAL   Proc Natl Acad Sci U S A 111 (6), 2164-2169 (2014)
   PUBMED   24469809
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Zhang,Y., Seo,S., Bhattarai,S., Bugge,K., Searby,C.C., Zhang,Q.,
            Drack,A.V., Stone,E.M. and Sheffield,V.C.
  TITLE     BBS mutations modify phenotypic expression of CEP290-related
            ciliopathies
  JOURNAL   Hum Mol Genet 23 (1), 40-51 (2014)
   PUBMED   23943788
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Nishimura,D.Y., Fath,M., Mullins,R.F., Searby,C., Andrews,M.,
            Davis,R., Andorf,J.L., Mykytyn,K., Swiderski,R.E., Yang,B.,
            Carmi,R., Stone,E.M. and Sheffield,V.C.
  TITLE     Bbs2-null mice have neurosensory deficits, a defect in social
            dominance, and retinopathy associated with mislocalization of
            rhodopsin
  JOURNAL   Proc Natl Acad Sci U S A 101 (47), 16588-16593 (2004)
   PUBMED   15539463
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Kulaga,H.M., Leitch,C.C., Eichers,E.R., Badano,J.L., Lesemann,A.,
            Hoskins,B.E., Lupski,J.R., Beales,P.L., Reed,R.R. and Katsanis,N.
  TITLE     Loss of BBS proteins causes anosmia in humans and defects in
            olfactory cilia structure and function in the mouse
  JOURNAL   Nat Genet 36 (9), 994-998 (2004)
   PUBMED   15322545
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Mykytyn,K., Mullins,R.F., Andrews,M., Chiang,A.P., Swiderski,R.E.,
            Yang,B., Braun,T., Casavant,T., Stone,E.M. and Sheffield,V.C.
  TITLE     Bardet-Biedl syndrome type 4 (BBS4)-null mice implicate Bbs4 in
            flagella formation but not global cilia assembly
  JOURNAL   Proc Natl Acad Sci U S A 101 (23), 8664-8669 (2004)
   PUBMED   15173597
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Kim,J.C., Badano,J.L., Sibold,S., Esmail,M.A., Hill,J.,
            Hoskins,B.E., Leitch,C.C., Venner,K., Ansley,S.J., Ross,A.J.,
            Leroux,M.R., Katsanis,N. and Beales,P.L.
  TITLE     The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar
            region and is required for microtubule anchoring and cell cycle
            progression
  JOURNAL   Nat Genet 36 (5), 462-470 (2004)
   PUBMED   15107855
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Ansley,S.J., Badano,J.L., Blacque,O.E., Hill,J., Hoskins,B.E.,
            Leitch,C.C., Kim,J.C., Ross,A.J., Eichers,E.R., Teslovich,T.M.,
            Mah,A.K., Johnsen,R.C., Cavender,J.C., Lewis,R.A., Leroux,M.R.,
            Beales,P.L. and Katsanis,N.
  TITLE     Basal body dysfunction is a likely cause of pleiotropic
            Bardet-Biedl syndrome
  JOURNAL   Nature 425 (6958), 628-633 (2003)
   PUBMED   14520415
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473975.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001074984.1, XP_217154.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..520
                     /product="Bardet-Biedl syndrome 4 protein"
                     /note="Bardet-Biedl syndrome 4 homolog"
                     /calculated_mol_wt=58137
     Region          68..95
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..332
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          101..129
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(102,105..106,109..110,112,136,139..140,143..144,
                     146..147,172..173,176..177,180)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          134..164
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..229
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          236..264
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          250..>448
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          270..298
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(271,274..275,278..279,281,305,308..309,312..313,
                     315..316,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          303..333
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          338..366
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          372..397
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..520
                     /gene="Bbs4"
                     /coded_by="NM_001106826.1:30..1592"
                     /db_xref="GeneID:300754"
                     /db_xref="RGD:1309134"
ORIGIN      
        1 maeeklgmkt qvpasiesqk prpkkapefp iveklnwlih lyyirkdyea ckavikeqlq
       61 etqglceyai yvqalifrle gniqeslelf qtcavlspqc adnlkqvars lfllgkhkaa
      121 tevyneaakl nqkdweichn lgvcytylkq fskaqdqlhs alqlnkhdlt yimlgkihll
      181 qgdldkaiei ykkavefspe ntellttlgl lylqlgvyqk afehlgnalt ydpanykail
      241 aagsmmqthg dfdvaltkyr vvacaipesp plwnnigmcf fgkkkyvaai sclkranyla
      301 pfdwkilynl glvhltmqqy asafhflsaa infqpkmgel ymllavaltn ledienakra
      361 yveavrldkc nplvnlnyav llynqgekkg alaqyqemek kvhflkdnnp lefdsemvem
      421 aqklgaalqv gealvwtkpv kdpkskhrtn sgsksatlqq plgsfqalgq amssaaahrk
      481 ipsgavgaql tkppslplep epeptveasp teaseqnkek
//
