CAND1_SCHPO
ID CAND1_SCHPO Reviewed; 1220 AA.
AC Q9P3A8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
GN Name=knd1; ORFNames=SPAC1565.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=19748355; DOI=10.1016/j.molcel.2009.07.024;
RA Schmidt M.W., McQuary P.R., Wee S., Hofmann K., Wolf D.A.;
RT "F-box-directed CRL complex assembly and regulation by the CSN and CAND1.";
RL Mol. Cell 35:586-597(2009).
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:19748355}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
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DR EMBL; CU329670; CAB99274.1; -; Genomic_DNA.
DR RefSeq; NP_593286.1; NM_001018716.2.
DR AlphaFoldDB; Q9P3A8; -.
DR SMR; Q9P3A8; -.
DR BioGRID; 279217; 60.
DR STRING; 4896.SPAC1565.07c.1; -.
DR MaxQB; Q9P3A8; -.
DR PaxDb; Q9P3A8; -.
DR PRIDE; Q9P3A8; -.
DR EnsemblFungi; SPAC1565.07c.1; SPAC1565.07c.1:pep; SPAC1565.07c.
DR GeneID; 2542767; -.
DR KEGG; spo:SPAC1565.07c; -.
DR PomBase; SPAC1565.07c; knd1.
DR VEuPathDB; FungiDB:SPAC1565.07c; -.
DR eggNOG; KOG1824; Eukaryota.
DR HOGENOM; CLU_007157_0_0_1; -.
DR InParanoid; Q9P3A8; -.
DR OMA; MGGTQDD; -.
DR PhylomeDB; Q9P3A8; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-917937; Iron uptake and transport.
DR PRO; PR:Q9P3A8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0045116; P:protein neddylation; ISS:PomBase.
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; IPR013932; TATA-bd_TIP120.
DR PANTHER; PTHR12696; PTHR12696; 1.
DR Pfam; PF08623; TIP120; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..1220
FT /note="Cullin-associated NEDD8-dissociated protein 1"
FT /id="PRO_0000374019"
FT REPEAT 1..35
FT /note="HEAT 1"
FT REPEAT 42..79
FT /note="HEAT 2"
FT REPEAT 121..157
FT /note="HEAT 3"
FT REPEAT 259..295
FT /note="HEAT 4"
FT REPEAT 365..410
FT /note="HEAT 5"
FT REPEAT 615..650
FT /note="HEAT 6"
FT REPEAT 680..700
FT /note="HEAT 7"
FT REPEAT 701..737
FT /note="HEAT 8"
FT REPEAT 738..775
FT /note="HEAT 9"
FT REPEAT 810..847
FT /note="HEAT 10"
FT REPEAT 850..887
FT /note="HEAT 11"
FT REPEAT 1020..1057
FT /note="HEAT 12"
SQ SEQUENCE 1220 AA; 137883 MW; E9F81C96B9DA193B CRC64;
MEEGILLKKY VESSDKDIRY MALSDLAARL NDANHLKNLK LESFPDTLDV LLQALSDASP
EVQQEAVRCV AIISSKIPQD KLKSTVENLL SGVAGKKSKN YLSALSLLLS NSNVQPFVNK
FYTSTVFPSF LQILKQYNVA QEEFFAILCV VCDSLEIYHS NLSTLLPNNF ELCIDVFQKC
TTQCQRELII KKACYLLSDV SLYGPRFAYK YIIEVLDRGL GPSTQMSEVN ISIKLLNEIL
LSSKKEKDSS TSFISTAVAD YTNKILSLLK KEEAPDELTQ KLLEVLGLLL EYQQVNILKI
WPELHGLLIS KISYDPNLIS DTNDEDDIAD FLEEMSDYSS IYEDEEDVSW IVRRESLKVV
LSVILSRLEY LPIVLQALGT SVVSKLNDRE ESVCLISIEV LKQAFLHVPR WIEVYATSND
RKRRYEGLPS DRSAISDTSI YLVSVIGKHV SKLSDKTPLS IVSELLNLVT VIFSSRDLGV
QSEFSNLSSI IYRFPDFSTL DIKIKLNLVR LISAIISCGC EEIENMESKM STILSLAVQN
NYPQLSYEAL ITELSFCKYI HKKQPTNVST DFSTMIDSSL QLLESKISDL KVRLALIDLV
SQYVILFYEP DFDSIFLRRV LIILCKKLQE EPTRSAAARA LCDIFMSVTD ITKIENGTKI
YEEILQDCCR HIDKSGNEFT TAYLELLEVL LKVGQKYLAE SLLEHILGLL IETLKRNTEN
TVAILKCLLI IPLSILLKSK NLLIDTIISH LQSSTIHLNE ESVCLLSRII AVISKEEDLE
LIINSFTCAQ KPVEEMVTLA LIAAQLICIF QSKAIVTSLN KSFMSPKSEV RIKVFTTLIF
GQLDYGKLTL PANEYFDTIA SNLNSPNADV MKAAAIALGS LTSQSEKFIK ELCALYVSDA
YDKELLLISF LTFLKKSKID YETADKIWDI LSKDIENIKD FSTSPFRTLL SECLGLLICN
ESSSLYYKLE LLSSSEASNH MLLSLSVFRF SLTLDCPKLK AYEKQFFEKA YKLFQNPDLE
VSQETLQVII SVIKNRRSCI ADVYNELLQG LISKSSVDSS NVHVVQMGPF QHVVDNSINQ
RQLVFETLYS LLDIPESLNH LTHFLQVSVM GLEDEHYIKL VSLSILEKLV DCSPSIIDEQ
VDTILEALRK IIELRKTEKT LKTDSDNILD LVRSALRVLF TMKLKCDNPV ISEFESQVQK
GPYSLEYEGI KNEIKTTIKT
