ID F6R900_MACMU Unreviewed; 768 AA.
AC F6R900;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Cullin-3 {ECO:0000313|EMBL:AFE64560.1, ECO:0000313|Ensembl:ENSMMUP00000037501.1};
GN Name=CUL3 {ECO:0000313|EMBL:AFE64560.1,
GN ECO:0000313|Ensembl:ENSMMUP00000037501.1,
GN ECO:0000313|VGNC:VGNC:71567};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000037501.1, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|EMBL:AFE64560.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE64560.1}, Testis
RC {ECO:0000313|EMBL:AFI35679.1}, and Thymus
RC {ECO:0000313|EMBL:AFH29569.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
RN [3] {ECO:0000313|Ensembl:ENSMMUP00000037501.1}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000037501.1};
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JU320804; AFE64560.1; -; mRNA.
DR EMBL; JU472765; AFH29569.1; -; mRNA.
DR EMBL; JV045608; AFI35679.1; -; mRNA.
DR RefSeq; NP_001253581.1; NM_001266652.1.
DR STRING; 9544.ENSMMUP00000037501; -.
DR PaxDb; 9544-ENSMMUP00000037501; -.
DR Ensembl; ENSMMUT00000044483.3; ENSMMUP00000037501.1; ENSMMUG00000022259.4.
DR GeneID; 707550; -.
DR KEGG; mcc:707550; -.
DR CTD; 8452; -.
DR VEuPathDB; HostDB:ENSMMUG00000022259; -.
DR VGNC; VGNC:71567; CUL3.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00940000155066; -.
DR HOGENOM; CLU_004747_7_1_1; -.
DR OMA; MFKDMTI; -.
DR OrthoDB; 21270at2759; -.
DR TreeFam; TF105858; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006718; Chromosome 12.
DR Bgee; ENSMMUG00000022259; Expressed in spermatid and 22 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005827; C:polar microtubule; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005112; F:Notch binding; IEA:Ensembl.
DR GO; GO:0031208; F:POZ domain binding; IEA:Ensembl.
DR GO; GO:0160072; F:ubiquitin ligase complex scaffold activity; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:Ensembl.
DR GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0072576; P:liver morphogenesis; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; IEA:Ensembl.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IEA:Ensembl.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IEA:Ensembl.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0140252; P:regulation protein catabolic process at postsynapse; IEA:Ensembl.
DR GO; GO:0017145; P:stem cell division; IEA:Ensembl.
DR GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
DR GO; GO:0001831; P:trophectodermal cellular morphogenesis; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 383..635
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
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"
SQ SEQUENCE 768 AA; 88930 MW; A1A02022480BF099 CRC64;
MSNLSKGTGS 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 GKTEDLGCMY
KLFSRVPNGL KTMCECMSSY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLLESF
NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR
FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS
NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL
AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIENGHIFT
VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN
VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA
//
