ID A0A2K5N496_CERAT Unreviewed; 702 AA.
AC A0A2K5N496;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Cullin 3 {ECO:0000313|Ensembl:ENSCATP00000032150.1};
GN Name=CUL3 {ECO:0000313|Ensembl:ENSCATP00000032150.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000032150.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000032150.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the cullin family.
CC {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC ECO:0000256|RuleBase:RU003829}.
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DR RefSeq; XP_011918095.1; XM_012062705.1.
DR AlphaFoldDB; A0A2K5N496; -.
DR SMR; A0A2K5N496; -.
DR Ensembl; ENSCATT00000056417.1; ENSCATP00000032150.1; ENSCATG00000039150.1.
DR GeneID; 105586984; -.
DR CTD; 8452; -.
DR GeneTree; ENSGT00940000155066; -.
DR OrthoDB; 21270at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000039150; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
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; 4.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; CULLIN; 1.
DR PANTHER; PTHR11932:SF168; CULLIN-3; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 317..569
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 611..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 81093 MW; 2CDE8E7AF43C898A CRC64;
MSNLSKGTGS RKDTKMRIRA FPVREDVLNS LNNNFLQTLN QAWNDHQTAM VMIRDILMYM
DRVYVQQNNV ENVYNLGLII FRDQVVRYGC IRDHLRQTLL DMIARERKGE VVDRGAIRNA
CQMLMILGLE GRSVYEEDFE APFLEMSAEF FQMESQKFLA ENSASVYIKK VEARINEEIE
RVMHCLDKST EEPIVKVVER ELISKHMKTI VEMENSGLVH MLKNGKTEDL GCMYKLFSRV
PNGLKTMCEC MSSYLREQGK ALVSEEGEGK NPVDYIQGLL DLKSRFDRFL LESFNNDRLF
KQTIAGDFEY FLNLNSRSPE YLSLFIDDKL KKGVKGLTEQ EVETILDKAM VLFRFMQEKD
VFERYYKQHL ARRLLTNKSV SDDSEKNMIS KLKTECGCQF TSKLEGMFRD MSISNTTMDE
FRQHLQATGV SLGGVDLTVR VLTTGYWPTQ SATPKCNIPP APRHAFEIFR RFYLAKHSGR
QLTLQHHMGS ADLNATFYGP VKKEDGSEVG VGGAQVTGSN TRKHILQVST FQMTILMLFN
NREKYTFEEI QQETDIPERE LVRALQSLAC GKPTQRVLTK EPKSKEIENG HIFTVNDQFT
SKLHRVKIQT VAAKQGESDP ERKETRQKVD DDRKHEIEAA IVRIMKSRKK MQHNVLVAEV
TQQLKARFLP SPVVIKKRIE GLIEREYLAR TPEDRKVYTY VA
//