ID A0A091CUU3_FUKDA Unreviewed; 815 AA.
AC A0A091CUU3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Anaphase-promoting complex subunit 2 {ECO:0000256|ARBA:ARBA00016068};
GN ORFNames=H920_17101 {ECO:0000313|EMBL:KFO21460.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO21460.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO21460.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO21460.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR EMBL; KN124375; KFO21460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CUU3; -.
DR STRING; 885580.ENSFDAP00000003554; -.
DR eggNOG; KOG2165; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR044554; APC2-like.
DR InterPro; IPR014786; APC2_C.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45957; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR Pfam; PF08672; ANAPC2; 1.
DR Pfam; PF00888; Cullin; 1.
DR SMART; SM01013; APC2; 1.
DR SMART; SM00182; CULLIN; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 495..693
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 443..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 93199 MW; 0E46BDA4E783C4BB CRC64;
MSGDGSAGPG QELFVAWNTV STGLVPPALL GLASSRTSGA VPPKEEELRA AVEVLRGHGL
HSVLEEWFVE VLQSDLQANI SPEFWNAISQ RENTADEPQG LLLLLDAFGL LESRLDPYLR
SLDLLEKWTR LGLLMGTGAQ GLREKVHTML RGVLFFSTPR TFQEMVQRLY GRFLRVYMQS
KRKGEGGTDP ELEGELDSRY ARRRYYRLLQ SPLCAGCGSD KQQCWCRQAL EQFHQLSQVL
HRLSLLERVS AEAVTTTLHQ VTRERMEDRC RGEYERSFLR EFHKWIERVV GWLGKVFLQD
GPARAASPEA GNTLRRWRCH VQRFFYRIYA SLRIEELFSI IRDFPDSRPA IEDLKYCLER
TDQRQQLLTS LKAALETRLL HPGVNTCDII TLYISAIKAL RVLDPSMVIL EVACEPIRRY
LRTREDTVRQ IVAGLTGDSD GTGDLAVELS KTDPASLETG QDSEDDSGEP EDWVPDPVDA
DPGKSSSKRR SSDIISLLVS IYGSKDLFIN EYRSLLADRL LHQFSFSPER EIRNVELLKL
RFGEAPMHFC EVMLKDMADS RRINANIREE DEKRPVEEQP PFGVYAVILS SEFWPPFKEE
KLEVPEDIRV ALEVYCKKYE KLKAMRTLSW KHTLGLVTMD VELADRTLSV AVTPVQAVVL
LYFQDQASWT LEELSKVVKM PVALLRRRMS VWLQQGVLRE EPPGTFSVIE EERPQDRDNM
VLIDSDEESD SGMASQADQK EEELLLFWTY IHAMLTNLES LSLERIYSML RMFVMTGPAL
AEIDLQELQG YLQKKVRDQQ LIYSAGVYRL PKSCS
//