LOCUS       NP_877966                539 aa            linear   ROD 02-JUN-2024
DEFINITION  T-complex protein 1 subunit delta [Rattus norvegicus].
ACCESSION   NP_877966
VERSION     NP_877966.1
DBSOURCE    REFSEQ: accession NM_182814.2
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 539)
  AUTHORS   Freund,A., Zhong,F.L., Venteicher,A.S., Meng,Z., Veenstra,T.D.,
            Frydman,J. and Artandi,S.E.
  TITLE     Proteostatic control of telomerase function through TRiC-mediated
            folding of TCAB1
  JOURNAL   Cell 159 (6), 1389-1403 (2014)
   PUBMED   25467444
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Sergeeva,O.A., Tran,M.T., Haase-Pettingell,C. and King,J.A.
  TITLE     Biochemical characterization of mutants in chaperonin proteins CCT4
            and CCT5 associated with hereditary sensory neuropathy
  JOURNAL   J Biol Chem 289 (40), 27470-27480 (2014)
   PUBMED   25124038
  REMARK    GeneRIF: C450Y CCT4 is defective in protein stability.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Slater,L.H., Hett,E.C., Clatworthy,A.E., Mark,K.G. and Hung,D.T.
  TITLE     CCT chaperonin complex is required for efficient delivery of
            anthrax toxin into the cytosol of host cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (24), 9932-9937 (2013)
   PUBMED   23716698
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Knee,K.M., Sergeeva,O.A. and King,J.A.
  TITLE     Human TRiC complex purified from HeLa cells contains all eight CCT
            subunits and is active in vitro
  JOURNAL   Cell Stress Chaperones 18 (2), 137-144 (2013)
   PUBMED   23011926
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Seo,S., Baye,L.M., Schulz,N.P., Beck,J.S., Zhang,Q., Slusarski,D.C.
            and Sheffield,V.C.
  TITLE     BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family
            chaperonins and mediate BBSome assembly
  JOURNAL   Proc Natl Acad Sci U S A 107 (4), 1488-1493 (2010)
   PUBMED   20080638
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Hsu,S.H., Lee,M.J., Hsieh,S.C., Scaravilli,F. and Hsieh,S.T.
  TITLE     Cutaneous and sympathetic denervation in neonatal rats with a
            mutation in the delta subunit of the cytosolic
            chaperonin-containing t-complex peptide-1 gene
  JOURNAL   Neurobiol Dis 16 (2), 335-345 (2004)
   PUBMED   15193290
  REMARK    GeneRIF: the mutation in Cct4 underlies cutaneous nerve
            degeneration in mutilated-foot rats.
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Lee,M.J., Stephenson,D.A., Groves,M.J., Sweeney,M.G., Davis,M.B.,
            An,S.F., Houlden,H., Salih,M.A., Timmerman,V., de Jonghe,P.,
            Auer-Grumbach,M., Di Maria,E., Scaravilli,F., Wood,N.W. and
            Reilly,M.M.
  TITLE     Hereditary sensory neuropathy is caused by a mutation in the delta
            subunit of the cytosolic chaperonin-containing t-complex peptide-1
            (Cct4) gene
  JOURNAL   Hum Mol Genet 12 (15), 1917-1925 (2003)
   PUBMED   12874111
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Hynes,G., Kubota,H. and Willison,K.R.
  TITLE     Antibody characterisation of two distinct conformations of the
            chaperonin-containing TCP-1 from mouse testis
  JOURNAL   FEBS Lett 358 (2), 129-132 (1995)
   PUBMED   7828721
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Kubota,H., Hynes,G., Carne,A., Ashworth,A. and Willison,K.
  TITLE     Identification of six Tcp-1-related genes encoding divergent
            subunits of the TCP-1-containing chaperonin
  JOURNAL   Curr Biol 4 (2), 89-99 (1994)
   PUBMED   7953530
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CA340557.1, AY223861.1, BQ200856.1 and CB612673.1.
            
            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##
            Transcript exon combination :: BC079283.1, AY223861.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..539
                     /product="T-complex protein 1 subunit delta"
                     /note="CCT-delta; TCP-1-delta; chaperonin subunit 4
                     (delta); chaperonin containing Tcp1, subunit 4 (delta)"
                     /calculated_mol_wt=57969
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            19
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P80315; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Region          25..538
                     /region_name="TCP1_delta"
                     /note="TCP-1 (CTT or eukaryotic type II) chaperonin
                     family, delta subunit. Chaperonins are involved in
                     productive folding of proteins. They share a common
                     general morphology, a double toroid of 2 stacked rings. In
                     contrast to bacterial group I chaperonins; cd03338"
                     /db_xref="CDD:239454"
     Site            order(25,29,57..60,62,80,82,86,90,93,395,531..537)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239454"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            order(52..54,104,108,169,407,425,465,508,510)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239454"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            302
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            326
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50991; propagated from
                     UniProtKB/Swiss-Prot (Q7TPB1.3)"
     Site            order(445,463,472,474..475,478)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239454"
     CDS             1..539
                     /gene="Cct4"
                     /coded_by="NM_182814.2:135..1754"
                     /db_xref="GeneID:29374"
                     /db_xref="RGD:727937"
ORIGIN      
        1 mpenvasrsg ppaagpgnrg kgayqdrdkp aqirfsnisa akavadairt slgpkgmdkm
       61 iqdgkgdvti tndgatilkq mqvlhpaarm lvelskaqdi eagdgttsvv iiagslldsc
      121 tkllqkgihp tiisesfqka lekgleiltd msrpvqlsdr etllnsatts lnskvvsqys
      181 sllspmsvna vmkvidpata tsvdlrdiki vkklggtidd celveglvlt qkvansgitr
      241 vekakigliq fclsapktdm dnqivvsdya qmdrvlreer ayilnlvkqi kktgcnvlli
      301 qksilrdals dlalhflnkm kimvvkdier ediefickti gtkpvahidq ftpdmlgsae
      361 laeevslngs gklfkitgct spgktvtivv rgsnklviee aersihdalc virclvkkra
      421 liagggapei elalrlteys rtlsgmesyc vrafadamev ipstlaenag lnpistvtel
      481 rnrhaqgekt tginvrkggi snileemvvq pllvsvsalt latetvrsil kiddvvntr
//
