CAND1_CANAL
ID CAND1_CANAL Reviewed; 1195 AA.
AC Q5ADW3; A0A1D8PKT2;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE AltName: Full=CaTIP120;
DE AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
DE Short=TBP-interacting protein 120 homolog;
GN Name=TIP120; OrderedLocusNames=CAALFM_C307610WA;
GN ORFNames=CaO19.14021, CaO19.6729;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22080453; DOI=10.1128/ec.05250-11;
RA Sela N., Atir-Lande A., Kornitzer D.;
RT "Neddylation and CAND1 independently stimulate SCF ubiquitin ligase
RT activity in Candida albicans.";
RL Eukaryot. Cell 11:42-52(2012).
CC -!- FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin ligase complexes that promotes the exchange of the substrate-
CC recognition F-box subunit in SCF complexes, thereby playing a key role
CC in the cellular repertoire of SCF complexes. Acts as a F-box protein
CC exchange factor (Probable). {ECO:0000305|PubMed:22080453}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Cells lacking both RUB1 and
CC CAND1 show defects in morphological, growth and protein degradation,
CC consistent with a reduction in SCF ubiquitin ligase activity.
CC {ECO:0000269|PubMed:22080453}.
CC -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
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DR EMBL; CP017625; AOW28760.1; -; Genomic_DNA.
DR RefSeq; XP_719828.2; XM_714735.2.
DR AlphaFoldDB; Q5ADW3; -.
DR SMR; Q5ADW3; -.
DR STRING; 237561.Q5ADW3; -.
DR GeneID; 3638494; -.
DR KEGG; cal:CAALFM_C307610WA; -.
DR CGD; CAL0000174904; TIP120.
DR VEuPathDB; FungiDB:C3_07610W_A; -.
DR eggNOG; KOG1824; Eukaryota.
DR HOGENOM; CLU_265739_0_0_1; -.
DR InParanoid; Q5ADW3; -.
DR OrthoDB; 194023at2759; -.
DR PRO; PR:Q5ADW3; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010265; P:SCF complex assembly; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039852; CAND1/CAND2.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR013932; TATA-bd_TIP120.
DR PANTHER; PTHR12696; PTHR12696; 1.
DR Pfam; PF08623; TIP120; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..1195
FT /note="Cullin-associated NEDD8-dissociated protein 1"
FT /id="PRO_0000422242"
FT REPEAT 1..37
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 45..83
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 168..206
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 397..434
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 436..474
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 703..742
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 846..885
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 999..1037
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1195 AA; 134467 MW; 69C93194FD5444F1 CRC64;
MHDINFNILK DRAMDVDPDI RFMALEDLRK FLQDESAAST RTTLNQSLEN FFPILLNMLN
DQNPDVQTQA IKSFEPMVKY LSNETFSKLV KKLFALVQQN SSSTGNVTGM KSFTVSVPNI
ALRSLFAQSN SRDKSEFVSD KLSNSNYRFD PHLARYIMDY LIPQIVGNPV TIDSIELLID
LVTEIGYVLT QDELLNLSLY LTKVALTETG LIGKKSMVAL ERVVALVRTE VVIDKLLAQI
NQSIEPTKLF VIFQLYSVCL KRGIKPNSID TIYNTITSNL NIEATEEEDD DDLDFDNLVK
ENSLKDEALT TLIDLVSQHF LPVESKNTVI ALIKSYVNYN PLAQDEDFID DEEDDISFSD
DEQEDDGDGE NDGSWKLRAK ATILTRALLK SFPDTLELLS KEVLPVFSFA DSNDQVVSEV
IKSSIAIVNS TSPRDSTNVS ELFPIIAARM KLAKETQVPL FLKLVESLNR FDNTSLVLEV
FKIIKDRKLI TSGSFDYLQF YSSTLKFHDN LPPLVIERMS SDFIKNLDDK SFNMITDSIK
CLSLLFHQDS LEKLDAIVDL LIYKVENSKQ YPSDLVRQSI IALGEAYGRA DKQKILNVFK
HSIEYEGTSK TTIDVLTQIY STDIPSEYSY LILKKLSTSI MSSTEATSVA SLLLMNKIFE
RLPSGDYDDT AGNLVQLLAV TNKANYECIF HILIKLVGTV LQETHRAPLL QTIVKLVNEG
KIEVADNSFF QFITTACNQI PDLYNFFEDG LNLNSELSAK ILAICASQNK LENKIMERRE
EFQNYYNSNI NDSRLAFDIL FLGYVGTHIE VKELDVQTLI GLLSNSQLTN DDNISAASTA
LGLIAQKHID SAVPIILNAY ESSEKTIIRG SLVDSLSIAA DACNEDQKRV IWDKVFNFPV
EFDHEVITEL KKSGELLGKI PVVDELTINT DNLKTTYLIL VITKSLLNNL QATKVNNTLL
DSLIKSSIEW LNIVNIDIRQ IVVGNLLTGL HSKPDTILPI LDSIILPKIF DQLQAEDSFK
KIITMGPYKY VLDEGLEIRK LCYEFIYSVI SLENAVIKKY NINLEKIASK IIEVGLIDTQ
TDITVLACIN LTNYIELHKD SAVELITRDG GNAFTTMINN LKKQLSKKLS AKASTQDSES
HQERIKSIIK LSKKFASVVE AAESIELAAA IRVWNEYNND LKTNFTIYYN STDGV
