ID   CUL2_DICDI              Reviewed;         771 AA.
AC   Q9XZJ3; Q55GH2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Cullin-2;
DE            Short=CUL-2;
DE   AltName: Full=Cullin-B;
GN   Name=culB; Synonyms=cul2; ORFNames=DDB_G0267384;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=AX4;
RX   PubMed=12455979; DOI=10.1128/ec.1.1.126-136.2002;
RA   Wang B., Kuspa A.;
RT   "CulB, a putative ubiquitin ligase subunit, regulates prestalk cell
RT   differentiation and morphogenesis in Dictyostelium spp.";
RL   Eukaryot. Cell 1:126-136(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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. The E3
CC       ubiquitin-protein ligase activity of the complex is dependent on the
CC       neddylation of the cullin subunit (By similarity). Appears to ensure
CC       that the proper number of prestalk cells differentiate at the
CC       appropriate time in development. May govern prestalk cell
CC       differentiation. {ECO:0000250, ECO:0000269|PubMed:12455979}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- PTM: Neddylated; which enhances the ubiquitination activity of E3
CC       ubiquitin-protein ligase complexes. {ECO:0000250|UniProtKB:Q13617,
CC       ECO:0000250|UniProtKB:Q9D4H8}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
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DR   EMBL; AF144717; AAD32222.1; -; mRNA.
DR   EMBL; AAFI02000003; EAL73144.1; -; Genomic_DNA.
DR   RefSeq; XP_647212.1; XM_642120.1.
DR   AlphaFoldDB; Q9XZJ3; -.
DR   SMR; Q9XZJ3; -.
DR   STRING; 44689.DDB0191260; -.
DR   PaxDb; Q9XZJ3; -.
DR   PRIDE; Q9XZJ3; -.
DR   EnsemblProtists; EAL73144; EAL73144; DDB_G0267384.
DR   GeneID; 8616016; -.
DR   KEGG; ddi:DDB_G0267384; -.
DR   dictyBase; DDB_G0267384; culB.
DR   eggNOG; KOG2166; Eukaryota.
DR   HOGENOM; CLU_004747_6_1_1; -.
DR   InParanoid; Q9XZJ3; -.
DR   OMA; WRLYMIE; -.
DR   PhylomeDB; Q9XZJ3; -.
DR   Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR   Reactome; R-DDI-69231; Cyclin D associated events in G1.
DR   Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   Reactome; R-DDI-917937; Iron uptake and transport.
DR   Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9XZJ3; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0031286; P:negative regulation of sorocarp stalk cell differentiation; IMP:dictyBase.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Developmental protein; Isopeptide bond; Reference proteome;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..771
FT                   /note="Cullin-2"
FT                   /id="PRO_0000345011"
FT   REGION          622..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        715
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in NEDD8)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13616"
SQ   SEQUENCE   771 AA;  89921 MW;  896192A3D84F5592 CRC64;
     MMNGLGRQDI DFNTIWKNIA DQVYKILTGS QNVSAMFLYE DVYKLCIAQP QPYCEPLYEN
     IKKFFEQHVD QILLIILDTK SDTISEYLKQ WKLFFSGCEL CNKVIFRYLN LNWINKKILD
     KKFGHPPDVY EIQILGLMIW KERLFFKIKD RVLKCVEILI QKDRDGELVQ HQFISQFMES
     LIKLDSVDKD RTLYLIEYEA SYLENTRQFY TRESVAFIAS SGISSYMKKA ETRIDEEEQR
     SQKYLNSSSH DKMRRLLHSI LIEKHKELLQ SECINYLKDE KLDEIYNMYK LLSRIEGGLA
     PVLETVQKYI QHVGIDAIKS IPDRNNPDPK IYVETLLKIY LQFSSIIKKS FNNDVSFITV
     LDLACHKIFN QNHITRNTTK SPELLAKYCD MLLKKGNKQH EEIELEEKLG QIIVLFKYVD
     DKDVFQKFYS KMLSRRLING TSVSDDIEKF MITGLKQACG FEYTSKFQRM FNDITLSAET
     NEEFKNHLIK NSLSIGKIDF SILVLTSGSW SLHSQTSSFI VPQELTLCIS AFQQYYSTQH
     QGRKLNWLHH LCKAEAKSFF AKKSYDFQVT NFQLGILLIF NTQESVSLEE ITKFTNLNEN
     ELSRTLQSLI EAKILISKKK DQNSINNNNN NNNNNNNNGE GNNSLVDSAN NMQPSSSSSS
     TQEYTVNSAY SNKRSKVKVS SSLQKETPLQ NEETYKGIDE DRKLYLQASI VRIMKARKTM
     NHVSLIQEVI EHSRLRFQPN IPMIKKCIEQ LIEKEYITRA EGESDRYLYA A