CAND1_ARATH
ID CAND1_ARATH Reviewed; 1219 AA.
AC Q8L5Y6; O64720;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
DE Short=AtCAND1;
DE AltName: Full=Protein ENHANCER OF TIR1-1 AUXIN RESISTANCE 2;
DE AltName: Full=Protein HEMIVENATA;
GN Name=CAND1; Synonyms=ETA2, HVE; OrderedLocusNames=At2g02560;
GN ORFNames=T8K22.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, INTERACTION WITH CUL1, AND DISRUPTION PHENOTYPE.
RX PubMed=15208391; DOI=10.1105/tpc.021949;
RA Feng S., Shen Y., Sullivan J.A., Rubio V., Xiong Y., Sun T.P., Deng X.W.;
RT "Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in
RT multiple developmental pathways controlled by ubiquitin/proteasome-mediated
RT protein Degradation.";
RL Plant Cell 16:1870-1882(2004).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-1069.
RX PubMed=15208392; DOI=10.1105/tpc.021923;
RA Chuang H.W., Zhang W., Gray W.M.;
RT "Arabidopsis ETA2, an apparent ortholog of the human cullin-interacting
RT protein CAND1, is required for auxin responses mediated by the SCF(TIR1)
RT ubiquitin ligase.";
RL Plant Cell 16:1883-1897(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15181201; DOI=10.1104/pp.104.044495;
RA Cheng Y., Dai X., Zhao Y.;
RT "AtCAND1, a HEAT-repeat protein that participates in auxin signaling in
RT Arabidopsis.";
RL Plant Physiol. 135:1020-1026(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16943276; DOI=10.1242/dev.02554;
RA Alonso-Peral M.M., Candela H., del Pozo J.C., Martinez-Laborda A.,
RA Ponce M.R., Micol J.L.;
RT "The HVE/CAND1 gene is required for the early patterning of leaf venation
RT in Arabidopsis.";
RL Development 133:3755-3766(2006).
RN [8]
RP INTERACTION WITH CUL4.
RX PubMed=16844902; DOI=10.1105/tpc.106.043224;
RA Chen H., Shen Y., Tang X., Yu L., Wang J., Guo L., Zhang Y., Zhang H.,
RA Feng S., Strickland E., Zheng N., Deng X.-W.;
RT "Arabidopsis CULLIN4 forms an E3 ubiquitin ligase with RBX1 and the CDD
RT complex in mediating light control of development.";
RL Plant Cell 18:1991-2004(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH CUL1.
RX PubMed=18550827; DOI=10.1073/pnas.0804144105;
RA Zhang W., Ito H., Quint M., Huang H., Noel L.D., Gray W.M.;
RT "Genetic analysis of CAND1-CUL1 interactions in Arabidopsis supports a role
RT for CAND1-mediated cycling of the SCFTIR1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8470-8475(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(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 (By similarity). Required for SCF(TIR1) function.
CC Modulates SCF(TIR1) function through its interactions with the CUL1
CC subunit. Represses photomorphogenesis by promoting HY5 degradation in
CC darkness. {ECO:0000250, ECO:0000269|PubMed:15181201,
CC ECO:0000269|PubMed:15208391, ECO:0000269|PubMed:15208392,
CC ECO:0000269|PubMed:16943276, ECO:0000269|PubMed:18550827}.
CC -!- SUBUNIT: Interacts with CUL1 and CUL4. Binds unneddylated CUL1, but
CC cannot bind CUL1 once it has been neddylated.
CC {ECO:0000269|PubMed:15208391, ECO:0000269|PubMed:16844902,
CC ECO:0000269|PubMed:18550827}.
CC -!- INTERACTION:
CC Q8L5Y6; Q94AH6: CUL1; NbExp=7; IntAct=EBI-602912, EBI-532411;
CC Q8L5Y6; Q8LGH4: CUL4; NbExp=2; IntAct=EBI-602912, EBI-541750;
CC Q8L5Y6; Q8GXL7: GATA24; NbExp=3; IntAct=EBI-602912, EBI-4426127;
CC Q8L5Y6; P46639: KNAT1; NbExp=4; IntAct=EBI-602912, EBI-530486;
CC Q8L5Y6; Q9SK33: WRKY60; NbExp=3; IntAct=EBI-602912, EBI-2112777;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L5Y6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L5Y6-2; Sequence=VSP_039624;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed in stems,
CC flowers and siliques. {ECO:0000269|PubMed:15208392}.
CC -!- DISRUPTION PHENOTYPE: Developmental phenotypes such as dwarfism, organ
CC defects, short inflorescences and mishaped leaves. Low fertility and
CC reduced responses to hormones. {ECO:0000269|PubMed:15181201,
CC ECO:0000269|PubMed:15208391, ECO:0000269|PubMed:16943276}.
CC -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
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DR EMBL; AC004136; AAC18930.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05595.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05596.1; -; Genomic_DNA.
DR EMBL; AY099857; AAM20708.1; -; mRNA.
DR EMBL; BT010134; AAQ22603.1; -; mRNA.
DR PIR; T00607; T00607.
DR RefSeq; NP_001030954.1; NM_001035877.2. [Q8L5Y6-2]
DR RefSeq; NP_178360.2; NM_126312.3. [Q8L5Y6-1]
DR AlphaFoldDB; Q8L5Y6; -.
DR SMR; Q8L5Y6; -.
DR BioGRID; 188; 14.
DR DIP; DIP-33719N; -.
DR IntAct; Q8L5Y6; 14.
DR STRING; 3702.AT2G02560.1; -.
DR iPTMnet; Q8L5Y6; -.
DR SwissPalm; Q8L5Y6; -.
DR PaxDb; Q8L5Y6; -.
DR PRIDE; Q8L5Y6; -.
DR ProteomicsDB; 222780; -. [Q8L5Y6-1]
DR EnsemblPlants; AT2G02560.1; AT2G02560.1; AT2G02560. [Q8L5Y6-1]
DR EnsemblPlants; AT2G02560.2; AT2G02560.2; AT2G02560. [Q8L5Y6-2]
DR GeneID; 814786; -.
DR Gramene; AT2G02560.1; AT2G02560.1; AT2G02560. [Q8L5Y6-1]
DR Gramene; AT2G02560.2; AT2G02560.2; AT2G02560. [Q8L5Y6-2]
DR KEGG; ath:AT2G02560; -.
DR Araport; AT2G02560; -.
DR TAIR; locus:2065279; AT2G02560.
DR eggNOG; KOG1824; Eukaryota.
DR InParanoid; Q8L5Y6; -.
DR OMA; MGGTQDD; -.
DR OrthoDB; 194023at2759; -.
DR PhylomeDB; Q8L5Y6; -.
DR PRO; PR:Q8L5Y6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L5Y6; baseline and differential.
DR Genevisible; Q8L5Y6; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0010265; P:SCF complex assembly; IBA:GO_Central.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1219
FT /note="Cullin-associated NEDD8-dissociated protein 1"
FT /id="PRO_0000396859"
FT REPEAT 44..81
FT /note="HEAT 1"
FT REPEAT 83..119
FT /note="HEAT 2"
FT REPEAT 209..244
FT /note="HEAT 3"
FT REPEAT 248..288
FT /note="HEAT 4"
FT REPEAT 327..363
FT /note="HEAT 5"
FT REPEAT 367..404
FT /note="HEAT 6"
FT REPEAT 423..460
FT /note="HEAT 7"
FT REPEAT 464..503
FT /note="HEAT 8"
FT REPEAT 599..636
FT /note="HEAT 9"
FT REPEAT 639..676
FT /note="HEAT 10"
FT REPEAT 808..848
FT /note="HEAT 11"
FT REPEAT 850..883
FT /note="HEAT 12"
FT REPEAT 927..964
FT /note="HEAT 13"
FT REPEAT 966..998
FT /note="HEAT 14"
FT REPEAT 1002..1039
FT /note="HEAT 15"
FT REPEAT 1043..1079
FT /note="HEAT 16"
FT REPEAT 1101..1137
FT /note="HEAT 17"
FT REPEAT 1141..1180
FT /note="HEAT 18"
FT REGION 311..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 13..14
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039624"
FT MUTAGEN 1069
FT /note="G->D: In eta2-1; reduced response to auxin."
FT /evidence="ECO:0000269|PubMed:15208392"
SQ SEQUENCE 1219 AA; 134897 MW; B0F5769754DE6040 CRC64;
MANLQVSGIL EKFQMTGKDK DYRYMATSDL LNELNKDSFK IDLDLEVRLS SIILQQLDDV
AGDVSGLAVK CLAPLVKKVG EERIVEMTNK LCDKLLHGKD QHRDTASIAL RTVVAQIAPT
LAPSILVTLT PQMIGGISGQ GMSSGIKCEC LEIMCDVVQK YGSLMTDDHE KLLNTLLLQL
GCNQATVRKK TVTCIASLAS SLSDDLLAKA TVEVVKNLSN RNAKSEITRT NIQMIGALCR
AVGYRFGTHL GNTVPVLINY CTSASENDEE LREYSLQALE SFLLRCPRDI SPYCDEILNL
TLEYISYDPN FTDNMEEDTD NETLEDEEDD ESANEYTDDE DASWKVRRAA AKCLAGLIVS
RSEMLTKVYQ EACPKLIDRF KEREENVKMD VFNTFIDLLR QTGNVTKGQT DTDESSPKWL
LKQEVSKIVK SINRQLREKS VKTKVGAFSV LRELVVVLPD CLADHIGSLV PGIERALNDK
SSTSNLKIEA LVFTKLVLAS HAPPVFHPYI KALSSPVLAA VGERYYKVTA EALRVCGELV
RVVRPSTAGM GFDFKPFVHP IYNAIMSRLT NQDQDQEVKE CAITCMGLVI STFGDQLRAE
LPSCLPVLVD RMGNEITRLT AVKAFSVIAT SPLHINLSCV LDHLIAELTG FLRKANRVLR
QATLITMNTL VTAYGDKIGS EAYEVILVEL SSLISVSDLH MTALALELCC TLMTGKSCSE
NISLAVRNKV LPQALTLVKS PLLQGQALLD LQKFFEALVY HANTSFYTLL ESLLSCAKPS
PQSGGVPKQA LYSIAQCVAV LCLAAGDKNC SSTVKMLMEI LKDDSGTNSA KQHLALLSLG
EIGRRKDLSA HAGIETIVIE SFQSPFEEIK SAASYALGNI AVGNLSNYLP FILDQIDNQQ
KKQYILLHSL KEVIVRQSVD KADFQNSSVE KILALLFNHC ESEEEGVRNV VAECLGKMAL
IEPEKLVPAL QVRTTSPAAF TRATVVTAVK YSVVERPEKL DEIIFPQISS FLMLIKDGDR
HVRRAAVSAL STFAHYKPNL IKGLLPELLP LLYDQTVIKK ELIRTVDLGP FKHVVDDGLE
LRKAAFECVF TLVDSCLDQV NPSSFIVPFL KSGLEDHYDL KMLCHLILSL LADKCPSAVL
AVLDSLVEPL HKTISFKPKQ DAVKQEHDRN EDMIRSALRA ISSLDRINGV DYSHKFKGLM
GDMKRSVPLW EKFQTIRNE
