ID   CDCA7_BOVIN             Reviewed;         374 AA.
AC   Q32PH1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Cell division cycle-associated protein 7;
GN   Name=CDCA7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in MYC-mediated cell transformation and
CC       apoptosis; induces anchorage-independent growth and clonogenicity in
CC       lymphoblastoid cells. Insufficient to induce tumorigenicity when
CC       overexpressed but contributes to MYC-mediated tumorigenesis. May play a
CC       role as transcriptional regulator (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MYC (via C-terminus), YWHAE and YWHAZ.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly nuclear with some expression also seen in the
CC       cytoplasm. Predominantly cytoplasmic when phosphorylated at Thr-163 (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Thr-163 promotes interaction with YWHAE and
CC       YWHAZ, dissociation from MYC and sequestration in the cytoplasm.
CC       {ECO:0000250}.
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DR   EMBL; BC108118; AAI08119.1; -; mRNA.
DR   RefSeq; NP_001032565.1; NM_001037488.2.
DR   AlphaFoldDB; Q32PH1; -.
DR   STRING; 9913.ENSBTAP00000004495; -.
DR   PaxDb; Q32PH1; -.
DR   PRIDE; Q32PH1; -.
DR   Ensembl; ENSBTAT00000004495; ENSBTAP00000004495; ENSBTAG00000003458.
DR   GeneID; 614893; -.
DR   KEGG; bta:614893; -.
DR   CTD; 83879; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003458; -.
DR   VGNC; VGNC:27086; CDCA7.
DR   eggNOG; ENOG502QQPE; Eukaryota.
DR   GeneTree; ENSGT00940000155436; -.
DR   HOGENOM; CLU_035988_2_0_1; -.
DR   InParanoid; Q32PH1; -.
DR   OMA; NICGSAR; -.
DR   OrthoDB; 1462540at2759; -.
DR   TreeFam; TF101076; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000003458; Expressed in thymus and 102 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR033576; CDCA7.
DR   InterPro; IPR040221; CDCA7/CDA7L.
DR   InterPro; IPR018866; Znf-4CXXC_R1.
DR   PANTHER; PTHR31169; PTHR31169; 1.
DR   PANTHER; PTHR31169:SF2; PTHR31169:SF2; 1.
DR   Pfam; PF10497; zf-4CXXC_R1; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..374
FT                   /note="Cell division cycle-associated protein 7"
FT                   /id="PRO_0000249309"
FT   REGION          53..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..170
FT                   /note="Interaction with MYC"
FT                   /evidence="ECO:0000250"
FT   REGION          250..374
FT                   /note="Mediates transcriptional activity"
FT                   /evidence="ECO:0000250"
FT   MOTIF           160..176
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        53..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWT1"
FT   MOD_RES         163
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWT1"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWT1"
FT   MOD_RES         196
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D0M2"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D0M2"
FT   CROSSLNK        208
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWT1"
SQ   SEQUENCE   374 AA;  42763 MW;  D6D17238D7004E86 CRC64;
     MDARRARQKD CRAKKNFKKF RYVKLISMET PSSSDDSCDS FASDNFANTR LQANREGCRT
     RSQCTRSGPL RVAMKFPPRS TRGAANKRTV PPEPPENSVT DSNSDSEDES GMNFLEKRAL
     NIKQNKAMLA KLMSELESFP GSFPGRRSLP GPSSRPKTPR RRTFPGVACR RNPERRARPL
     TRSRSRVLGS LSALPTEEEE EEEEEEDKYM LVRKRKSMVG YMNEDDMPRS RRPGPMTLPH
     VVRPVDEITE EELENICNNS REKIYNRSLG STCHQCRQKT IDTKTNCRNP ECWGVRGQFC
     GPCLRNRYGE EVKDALLDPN WHCPPCRGIC NCSFCRQRDG RCATGVLVYL AKYHGFGNVH
     AYLKSLKQEF EMQG