CUL3A_XENLA
ID CUL3A_XENLA Reviewed; 768 AA.
AC Q6DE95;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cullin-3-A;
DE Short=CUL-3-A;
GN Name=cul3a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH BTBD6.
RX PubMed=18855900; DOI=10.1002/dvdy.21748;
RA Bury F.J., Moers V., Yan J., Souopgui J., Quan X.J., De Geest N.,
RA Kricha S., Hassan B.A., Bellefroid E.J.;
RT "Xenopus BTBD6 and its Drosophila homologue lute are required for neuronal
RT development.";
RL Dev. Dyn. 237:3352-3360(2008).
CC -!- FUNCTION: Probable core component of cullin-based SCF-like E3
CC ubiquitin-protein ligase complexes which mediate the ubiquitination and
CC subsequent proteasomal degradation of target proteins (By similarity).
CC The E3 ubiquitin-protein ligase activity of the complex is dependent on
CC the neddylation of the cullin subunit (By similarity). Involved in ER-
CC Golgi transport by regulating the size of COPII coats, thereby playing
CC a key role in collagen export, which is required for embryonic stem
CC (ES) cells division (By similarity). May play a role in the regulation
CC of mittotic entry via ubiquitination of aurka (By similarity).
CC {ECO:0000250|UniProtKB:Q13618, ECO:0000250|UniProtKB:Q9JLV5}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein
CC ligase complexes formed of cul3, rbx1 and a variable BTB domain-
CC containing protein acting as both, adapter to cullin and substrate
CC recognition subunit (By similarity). Interacts with btbd6
CC (PubMed:18855900). {ECO:0000250|UniProtKB:Q13618,
CC ECO:0000250|UniProtKB:Q9JLV5, ECO:0000269|PubMed:18855900}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13618}.
CC -!- PTM: Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-
CC protein ligase activity of the SCF-like complex.
CC {ECO:0000250|UniProtKB:Q13618}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; BC077239; AAH77239.1; -; mRNA.
DR RefSeq; NP_001086652.1; NM_001093183.1.
DR RefSeq; XP_018117425.1; XM_018261936.1.
DR AlphaFoldDB; Q6DE95; -.
DR SMR; Q6DE95; -.
DR MaxQB; Q6DE95; -.
DR DNASU; 446487; -.
DR GeneID; 446487; -.
DR KEGG; xla:446487; -.
DR CTD; 446487; -.
DR Xenbase; XB-GENE-974989; cul3.L.
DR OMA; MFKDMTI; -.
DR OrthoDB; 1040292at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 446487; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:GOC.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
DR GO; GO:0040016; P:embryonic cleavage; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0017145; P:stem cell division; ISS:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 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; PTHR11932; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; ER-Golgi transport; Isopeptide bond; Mitosis;
KW Nucleus; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..768
FT /note="Cullin-3-A"
FT /id="PRO_0000380252"
FT REGION 677..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 712
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 768 AA; 88951 MW; 84EFA0F5802C0468 CRC64;
MSNLGKSTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN
AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR
DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR
GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR
INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLACMY
KLFSRVPNGL KTMCECMSLY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLQESF
SNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVES ILDKAMVLFR
FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS
NTTMDEFRQH LQTTGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL
AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
ILMLFNNRDK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIESGHMFT
VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN
VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA
