ID   CUL1_DICDI              Reviewed;         770 AA.
AC   O60999; Q54DW6;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Cullin-1;
DE            Short=CUL-1;
DE   AltName: Full=Cullin-A;
GN   Name=culA; Synonyms=cul1; ORFNames=DDB_G0291972;
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], FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=AX3;
RX   PubMed=11390363; DOI=10.1101/gad.871101;
RA   Mohanty S., Lee S., Yadava N., Dealy M.J., Johnson R.S., Firtel R.A.;
RT   "Regulated protein degradation controls PKA function and cell-type
RT   differentiation in Dictyostelium.";
RL   Genes Dev. 15:1435-1448(2001).
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). Required at several
CC       stages during development. CulA and fbxA regulate multicellular
CC       development by targeting regA for degradation via a pathway that
CC       requires erkB function, leading to an increase in cAMP and PKA
CC       activity. {ECO:0000250, ECO:0000269|PubMed:11390363}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a complex that includes culA, fbxA and regA. Formation
CC       of this complex is dependent on the MAP kinase erkB.
CC       {ECO:0000269|PubMed:11390363}.
CC   -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF.
CC       {ECO:0000250|UniProtKB:Q13616}.
CC   -!- DISRUPTION PHENOTYPE: Cells are defective in inducing cell-type-
CC       specific gene expression and exhibit defects during aggregation,
CC       including reduced chemotaxis. {ECO:0000269|PubMed:11390363}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
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DR   EMBL; AF020287; AAC15412.1; -; mRNA.
DR   EMBL; AAFI02000187; EAL61342.1; -; Genomic_DNA.
DR   RefSeq; XP_629756.1; XM_629754.1.
DR   AlphaFoldDB; O60999; -.
DR   SMR; O60999; -.
DR   STRING; 44689.DDB0185191; -.
DR   PaxDb; O60999; -.
DR   PRIDE; O60999; -.
DR   EnsemblProtists; EAL61342; EAL61342; DDB_G0291972.
DR   GeneID; 8628431; -.
DR   KEGG; ddi:DDB_G0291972; -.
DR   dictyBase; DDB_G0291972; culA.
DR   eggNOG; KOG2166; Eukaryota.
DR   HOGENOM; CLU_004747_6_1_1; -.
DR   InParanoid; O60999; -.
DR   OMA; DSFKERM; -.
DR   PhylomeDB; O60999; -.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O60999; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:dictyBase.
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:0004842; F:ubiquitin-protein transferase activity; ISS:dictyBase.
DR   GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
DR   GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS: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   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
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   Isopeptide bond; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..770
FT                   /note="Cullin-1"
FT                   /id="PRO_0000345010"
FT   CROSSLNK        714
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in NEDD8)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13616"
SQ   SEQUENCE   770 AA;  89335 MW;  4D14FFE07A0A08E4 CRC64;
     MSMMTSTPTK RSVKLDDIWP ELEEGIYKII TDLNKGFPKQ KWIALYTHVY DYCAASQSKS
     SAKVGMPKQQ ASGANYVGED LYNRLNLFLK KHMSQLLKLT ETKMDEPLLN YYYTEWDRYT
     SAMKYINNIF QYMNRYWIKR EIDDGKKEVY EIFILSLVIW RDCLFTPLKQ RLTNSLLDII
     ESERNGYQIN THLIKGVING YVSLGLNREK PKETILQVYK SGFEELFLTA TENYYTNESA
     KFISENSVAD YMKKVETRLN EEVKRVQQYL HQNTESELIA KCEKVLIEKH VEVIWNEFQT
     LLEKDKIPDL TRMYSLLSRI PRGLEPLRTT LEKHVQNVGL QAVSSIATNG VIEPKVYIET
     LLKVFKKYNE LVTGAFRSDT GFVASLDKAC RRFINENAVT IAAKSSSKSP ELLARFTDFL
     LKKSPNNPEE SEMEQLLNDV MIVFKYIEDK DVFQDFYSKM LAKRLIHGTS TSEDLEGTMI
     GKLKSTCGYE YTSKLQRMFT DMSLSRELLD RFNNHIEQVE RSSLNIDFSV LVLATGSWPL
     QPPSTNFSIP KELQACEQLF QKFYQNQHSG RKLNWLHHLS KGELKTKYLQ TSKSGYTLQC
     STYQIGVLLQ FNQYETLTSE EIQESTQLID SVLKGTLTSL AKSKILLADP PLDDEEIAKT
     TKFSLNKQFK NKKTKIFINV PVLTQVKEEI DSIHKTVEED RKLQIQAAIV RIMKMRKQLA
     HSGLMTEVIS QLQTRFNPKV NIIKKCIDIL IEKEYLMRVE GKKDHYSYVA