ID   CUL1_ARATH              Reviewed;         738 AA.
AC   Q94AH6; O22770; Q56W31;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   20-MAY-2008, entry version 51.
DE   Cullin-1.
GN   Name=CUL1; OrderedLocusNames=At4g02570; ORFNames=T10P11.26;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22053474; PubMed=12058059; DOI=10.1091/mbc.E02-02-0077;
RA   Shen W.-H., Parmentier Y., Hellmann H., Lechner E., Dong A.,
RA   Masson J., Granier F., Lepiniec L., Estelle M., Genschik P.;
RT   "Null mutation of AtCUL1 causes arrest in early embryogenesis in
RT   Arabidopsis.";
RL   Mol. Biol. Cell 13:1916-1928(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 491-738.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH TIR1, AND IDENTIFICATION IN A SCF(TIR1) COMPLEX.
RX   MEDLINE=99328894; PubMed=10398681; DOI=10.1101/gad.13.13.1678;
RA   Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T.,
RA   Crosby W.L., Yang M., Ma H., Estelle M.;
RT   "Identification of an SCF ubiquitin-ligase complex required for auxin
RT   response in Arabidopsis thaliana.";
RL   Genes Dev. 13:1678-1691(1999).
RN   [6]
RP   NEDDYLATION AT LYS-682, AND MUTAGENESIS OF LYS-682 AND LYS-712.
RX   MEDLINE=20079655; PubMed=10611386; DOI=10.1073/pnas.96.26.15342;
RA   del Pozo J.C., Estelle M.;
RT   "The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related
RT   protein RUB1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SKP1A; KIN10 AND KIN11.
RX   MEDLINE=21280797; PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA   Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA   Salchert K., del Pozo C., Schell J., Koncz C.;
RT   "SKP1-SnRK protein kinase interactions mediate proteasomal binding of
RT   a plant SCF ubiquitin ligase.";
RL   EMBO J. 20:2742-2756(2001).
RN   [8]
RP   INTERACTION WITH THE CSN COMPLEX.
RX   MEDLINE=21258418; PubMed=11337587; DOI=10.1126/science.1059776;
RA   Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
RA   Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
RT   "Interactions of the COP9 signalosome with the E3 ubiquitin ligase
RT   SCF(TIR1) in mediating auxin response.";
RL   Science 292:1379-1382(2001).
RN   [9]
RP   INTERACTION WITH SKP1A; SKP1B; RBX1A AND RBX1B.
RX   MEDLINE=22370998; PubMed=12381738; DOI=10.1074/jbc.M204254200;
RA   Lechner E., Xie D., Grava S., Pigaglio E., Planchais S.,
RA   Murray J.A.H., Parmentier Y., Mutterer J., Dubreucq B., Shen W.-H.,
RA   Genschik P.;
RT   "The AtRbx1 protein is part of plant SCF complexes, and its down-
RT   regulation causes severe growth and developmental defects.";
RL   J. Biol. Chem. 277:50069-50080(2002).
RN   [10]
RP   NEDDYLATION, AND DENEDDYLATION BY THE CSN COMPLEX.
RX   MEDLINE=21843692; PubMed=11854419; DOI=10.1091/mbc.01-08-0427;
RA   Wang X., Kang D., Feng S., Serino G., Schwechheimer C., Wei N.;
RT   "CSN1 N-terminal-dependent activity is required for Arabidopsis
RT   development but not for Rub1/Nedd8 deconjugation of cullins: a
RT   structure-function study of CSN1 subunit of COP9 signalosome.";
RL   Mol. Biol. Cell 13:646-655(2002).
CC   -!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
CC       degradation of target proteins. Regulator of mitotic processes
CC       which plays a role during gametogenesis and embryogenesis.
CC       Together with SKP1, RBX1 and a F-box protein, it forms a SCF
CC       complex. The functional specificity of this complex depends of the
CC       type of F-box protein. SCF(UFO) is implicated in floral organ
CC       development. SCF(TIR1) is involved in auxin signaling pathway.
CC       SCF(COI1) regulates responses to jasmonates. SCF(EID1) and
CC       SCF(AFR) are implicated in phytochrome A light signaling.
CC       SCF(ADO1/ZTL), SCF(ADO2/LKP2), SCF(ADO3/FKF1) are related to the
CC       circadian clock. SCF(ORE9) seems to be involved in senescence.
CC       SCF(EBF1/EBF2) may regulate ethylene signaling.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of E3 ubiquitin ligase SCF complexes such as
CC       SCF(TIR1) and SCF(COI1). SCF(TIR1) is composed of CUL1, SKP1
CC       (SKP1A or SKP1B), RBX1 (RBX1A or RBX1B) and TIR1, while SCF(COI1)
CC       is composed of CUL1, SKP1, RBX1 and COI1. A SNF1-related protein
CC       kinase (KIN10 and KIN11) can also be part of these SCF complexes.
CC       SCF(TIR1) is able to interact with the COP9 signalosome (CSN)
CC       complex.
CC   -!- INTERACTION:
CC       P43291:ASK1; NbExp=1; IntAct=EBI-532411, EBI-401164;
CC       Q8L5Y6:At2g02560; NbExp=3; IntAct=EBI-532411, EBI-602912;
CC       O04197:COI1; NbExp=2; IntAct=EBI-532411, EBI-401159;
CC       Q9SKK0:EBF1; NbExp=1; IntAct=EBI-532411, EBI-401198;
CC       Q708Y0:EBF2; NbExp=1; IntAct=EBI-532411, EBI-593623;
CC       Q9STX3:GID2; NbExp=1; IntAct=EBI-532411, EBI-619033;
CC       Q38825:IAA7; NbExp=3; IntAct=EBI-532411, EBI-602959;
CC       Q940X7:RBX1A; NbExp=6; IntAct=EBI-532411, EBI-532404;
CC       Q9SDY5:RCE1; NbExp=1; IntAct=EBI-532411, EBI-595116;
CC       Q39255:SKP1A; NbExp=3; IntAct=EBI-532411, EBI-532357;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Spindle. Cytoplasm,
CC       cytoskeleton, phragmoplast. Note=Mainly nuclear during interphase
CC       and preprophase, but also weakly cytoplasmic during interphase.
CC       Associated to mitotic spindle during metaphase, and to the
CC       phragmoplast during telophase.
CC   -!- TISSUE SPECIFICITY: Expressed constitutively in roots, seedlings,
CC       stems, leaves and flowers.
CC   -!- DEVELOPMENTAL STAGE: Strong accumulation in embryos (at protein
CC       level).
CC   -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC       signalosome (CSN) complex.
CC   -!- SIMILARITY: Belongs to the cullin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC78267.1; Type=Erroneous gene model prediction;
CC       Sequence=CAB80750.1; Type=Erroneous gene model prediction;
CC   -!- WEB RESOURCE: Name=PlantsUBQ; Note=A functional genomics database
CC       for the ubiquitin/26S proteasome proteolytic pathway in plants;
CC       URL="http://plantsubq.genomics.purdue.edu/";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ318017; CAC85264.1; -; mRNA.
DR   EMBL; AC002330; AAC78267.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161494; CAB80750.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY046030; AAK76704.1; -; mRNA.
DR   EMBL; AY133878; AAM91812.1; -; mRNA.
DR   EMBL; AK222216; BAD95380.1; -; mRNA.
DR   PIR; T01092; T01092.
DR   RefSeq; NP_001031575.1; -.
DR   RefSeq; NP_001031576.1; -.
DR   RefSeq; NP_567243.1; -.
DR   UniGene; At.24877; -.
DR   HSSP; Q9JLV5; 1IUY.
DR   IntAct; Q94AH6; -.
DR   GeneID; 825648; -.
DR   GenomeReviews; CT486007_GR; AT4G02570.
DR   KEGG; ath:AT4G02570; -.
DR   NMPDR; fig|3702.1.peg.18072; -.
DR   TAIR; At4g02570; -.
DR   GermOnline; AT4G02570; Arabidopsis thaliana.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   Auxin signaling pathway; Cell cycle; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Ethylene signaling pathway;
KW   Nucleus; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    738       Cullin-1.
FT                                /FTId=PRO_0000119804.
FT   CROSSLNK    682    682       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in NEDD8).
FT   MUTAGEN     682    682       K->M: No neddylation.
FT   MUTAGEN     712    712       K->M: No change in neddylation.
SQ   SEQUENCE   738 AA;  86302 MW;  45041357DE8DAD8C CRC64;
     MERKTIDLEQ GWDYMQTGIT KLKRILEGLN EPAFDSEQYM MLYTTIYNMC TQKPPHDYSQ
     QLYDKYREAF EEYINSTVLP ALREKHDEFM LRELFKRWSN HKVMVRWLSR FFYYLDRYFI
     ARRSLPPLNE VGLTCFRDLV YNELHSKVKQ AVIALVDKER EGEQIDRALL KNVLDIYVEI
     GMGQMERYEE DFESFMLQDT SSYYSRKASS WIQEDSCPDY MLKSEECLKK ERERVAHYLH
     SSSEPKLVEK VQHELLVVFA SQLLEKEHSG CRALLRDDKV DDLSRMYRLY HKILRGLEPV
     ANIFKQHVTA EGNALVQQAE DTATNQVANT ASVQEQVLIR KVIELHDKYM VYVTECFQNH
     TLFHKALKEA FEIFCNKTVA GSSSAELLAT FCDNILKKGG SEKLSDEAIE DTLEKVVKLL
     AYISDKDLFA EFYRKKLARR LLFDRSANDD HERSILTKLK QQCGGQFTSK MEGMVTDLTL
     ARENQNSFED YLGSNPAANP GIDLTVTVLT TGFWPSYKSF DINLPSEMIK CVEVFKGFYE
     TKTKHRKLTW IYSLGTCHIN GKFDQKAIEL IVSTYQAAVL LLFNTTDKLS YTEILAQLNL
     SHEDLVRLLH SLSCAKYKIL LKEPNTKTVS QNDAFEFNSK FTDRMRRIKI PLPPVDERKK
     VVEDVDKDRR YAIDAAIVRI MKSRKVLGHQ QLVSECVEQL SRMFKPDIKA IKKRMEDLIT
     RDYLERDKEN PNMFRYLA
//