LOCUS       NP_001402631             825 aa            linear   ROD 01-APR-2024
DEFINITION  cell division cycle protein 27 homolog isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001402631 XP_006247597
VERSION     NP_001402631.1
DBSOURCE    REFSEQ: accession NM_001415702.1
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 825)
  AUTHORS   Mansfeld,J., Collin,P., Collins,M.O., Choudhary,J.S. and Pines,J.
  TITLE     APC15 drives the turnover of MCC-CDC20 to make the spindle assembly
            checkpoint responsive to kinetochore attachment
  JOURNAL   Nat Cell Biol 13 (10), 1234-1243 (2011)
   PUBMED   21926987
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Song,M.S., Carracedo,A., Salmena,L., Song,S.J., Egia,A.,
            Malumbres,M. and Pandolfi,P.P.
  TITLE     Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a
            phosphatase-independent manner
  JOURNAL   Cell 144 (2), 187-199 (2011)
   PUBMED   21241890
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Jin,L., Williamson,A., Banerjee,S., Philipp,I. and Rape,M.
  TITLE     Mechanism of ubiquitin-chain formation by the human
            anaphase-promoting complex
  JOURNAL   Cell 133 (4), 653-665 (2008)
   PUBMED   18485873
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Dube,P., Herzog,F., Gieffers,C., Sander,B., Riedel,D., Muller,S.A.,
            Engel,A., Peters,J.M. and Stark,H.
  TITLE     Localization of the coactivator Cdh1 and the cullin subunit Apc2 in
            a cryo-electron microscopy model of vertebrate APC/C
  JOURNAL   Mol Cell 20 (6), 867-879 (2005)
   PUBMED   16364912
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Dec 23, 2022 this sequence version replaced XP_006247597.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.36380.1,
                                           SRR26643429.39346.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..825
                     /product="cell division cycle protein 27 homolog isoform
                     1"
                     /note="cell division cycle protein 27 homolog"
                     /calculated_mol_wt=91662
     Region          17..92
                     /region_name="ANAPC3"
                     /note="Anaphase-promoting complex, cyclosome, subunit 3;
                     pfam12895"
                     /db_xref="CDD:463743"
     Region          84..114
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          115..148
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          251..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          285..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          346..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          449..>672
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          500..533
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          502..528
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          562..>732
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          568..601
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          568..596
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(569,572..573,576..577,579,603,606..607,610..611,
                     613..614,637,640..641,644..645,648)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          601..631
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          603..635
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          636..669
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          636..664
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <666..805
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          670..697
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          671..703
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          704..732
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          705..737
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          738..771
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Region          738..766
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          782..825
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A2.1)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30260; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A2.1)"
     CDS             1..825
                     /gene="Cdc27"
                     /coded_by="NM_001415702.1:124..2601"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:360643"
                     /db_xref="RGD:1304921"
ORIGIN      
        1 mtvlqepvqa aiwqalnhya yrdavflaer lyaevhseea lfllatcyyr sgkaykayrl
       61 lkghscttpq ckyllakccv dlsklaegeq ilsggvfnkq kshddlvtef gdsacftlsl
      121 lghvycktdr lakgsecyqk slslnpflws pfeslceige kpdpdqtfkl tslqnfsscl
      181 pntctalvsn hslshrqpet vltetpqdti elnrlnless nskyslntds svsyidsavi
      241 spdnvplgtg psilskqvqn kpktgrsllg gptalspltp sfgilpletp spgdgsylqn
      301 ytntpsvidv pstgaptkks varmghtgak svfsqsgnsr eatpvlvaqt qssgpqtstt
      361 pqvlsptits ppnalprrss rlftsdsstt kenskklkmk fppkipnrkt ksktnkggit
      421 qpnindslei tkldssiise gkistitpqi qafnlqkaaa eglmsllrem gkgylalcsy
      481 nckeainils hlpshhystg wvlcqigray felseymqae rifsevrrie sfrvegmeiy
      541 sttlwhlqkd valsvlskdl tdmdknspea wcaagncfsl qrehdiaikf fqraiqvdpn
      601 yayaytllgh efvlteeldk alacfrnair vnprhynawy glgmiyykqe kfslaemhfq
      661 kaldinpqss vllchigvvq halkksekal dtlnkaivid pknplckfhr asvlfaneky
      721 ksalqeleel kqivpkeslv yfligkvykk lgqthlalmn fswamdldpk gannqikeai
      781 dkrylpddee pitqeeqimg tdesqessmt daddtqlhaa esdef
//
