APC16_BOVIN
ID APC16_BOVIN Reviewed; 110 AA.
AC Q58DR0; Q1RMH7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Anaphase-promoting complex subunit 16;
DE Short=APC16;
DE AltName: Full=Cyclosome subunit 16;
GN Name=ANAPC16;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5. ANAPC16 associates with the rest of the complex
CC independently of ANAPC2 and ANAPC11. {ECO:0000250|UniProtKB:Q96DE5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96DE5}. Nucleus
CC {ECO:0000250|UniProtKB:Q96DE5}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q96DE5}.
CC -!- SIMILARITY: Belongs to the APC16 family. {ECO:0000305}.
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DR EMBL; BT021537; AAX46384.1; -; mRNA.
DR EMBL; BC114889; AAI14890.1; -; mRNA.
DR RefSeq; NP_001014960.1; NM_001014960.1.
DR RefSeq; XP_005226503.1; XM_005226446.3.
DR RefSeq; XP_005226504.1; XM_005226447.2.
DR RefSeq; XP_005226505.1; XM_005226448.3.
DR AlphaFoldDB; Q58DR0; -.
DR SMR; Q58DR0; -.
DR STRING; 9913.ENSBTAP00000000186; -.
DR PaxDb; Q58DR0; -.
DR Ensembl; ENSBTAT00000000186; ENSBTAP00000000186; ENSBTAG00000000162.
DR GeneID; 540089; -.
DR KEGG; bta:540089; -.
DR CTD; 119504; -.
DR VEuPathDB; HostDB:ENSBTAG00000000162; -.
DR VGNC; VGNC:25883; ANAPC16.
DR eggNOG; ENOG502RZ50; Eukaryota.
DR GeneTree; ENSGT00390000018109; -.
DR HOGENOM; CLU_153312_0_0_1; -.
DR InParanoid; Q58DR0; -.
DR OMA; XGSERFL; -.
DR OrthoDB; 1642213at2759; -.
DR TreeFam; TF332754; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000000162; Expressed in biceps femoris and 105 other tissues.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR InterPro; IPR029641; APC16.
DR PANTHER; PTHR31564; PTHR31564; 1.
DR Pfam; PF17256; ANAPC16; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Kinetochore; Mitosis; Nucleus; Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96DE5"
FT CHAIN 2..110
FT /note="Anaphase-promoting complex subunit 16"
FT /id="PRO_0000089815"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96DE5"
SQ SEQUENCE 110 AA; 11637 MW; EEE38A86B1ACCF0A CRC64;
MAASSSSSSA GGVSGSSVAG SGFSVSDLAP PRKALFTYPK GAGEMLEDGS ERFLCESVFS
YQVASTLKQV KHDQQVARME KLAGLVEELE ADEWRFKPIE QLLGFTPSSG