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CCD8_ARATH
ID   CCD8_ARATH              Reviewed;         570 AA.
AC   Q8VY26; Q9M079;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Carotenoid cleavage dioxygenase 8, chloroplastic;
DE            Short=AtCCD8;
DE            EC=1.13.11.69 {ECO:0000269|PubMed:22422982};
DE            EC=1.13.11.70 {ECO:0000269|PubMed:18637791};
DE   AltName: Full=AtNCED8;
DE   AltName: Full=Protein MORE AXILLARY BRANCHING 4;
DE   AltName: Full=Protein MORE AXILLARY GROWTH 4;
DE   Flags: Precursor;
GN   Name=CCD8; Synonyms=MAX4, NCED8; OrderedLocusNames=At4g32810;
GN   ORFNames=T16I18.20;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., 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., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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].
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, TISSUE SPECIFICITY, AND INDUCTION BY AUXIN.
RX   PubMed=12815068; DOI=10.1101/gad.256603;
RA   Sorefan K., Booker J., Haurogne K., Goussot M., Bainbridge K., Foo E.,
RA   Chatfield S., Ward S., Beveridge C., Rameau C., Leyser O.;
RT   "MAX4 and RMS1 are orthologous dioxygenase-like genes that regulate shoot
RT   branching in Arabidopsis and pea.";
RL   Genes Dev. 17:1469-1474(2003).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15342640; DOI=10.1074/jbc.m409004200;
RA   Schwartz S.H., Qin X., Loewen M.C.;
RT   "The biochemical characterization of two carotenoid cleavage enzymes from
RT   Arabidopsis indicates that a carotenoid-derived compound inhibits lateral
RT   branching.";
RL   J. Biol. Chem. 279:46940-46945(2004).
RN   [6]
RP   INDUCTION BY AUXIN.
RX   PubMed=16262707; DOI=10.1111/j.1365-313x.2005.02548.x;
RA   Bainbridge K., Sorefan K., Ward S., Leyser O.;
RT   "Hormonally controlled expression of the Arabidopsis MAX4 shoot branching
RT   regulatory gene.";
RL   Plant J. 44:569-580(2005).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16507088; DOI=10.1111/j.1365-313x.2006.02666.x;
RA   Auldridge M.E., Block A., Vogel J.T., Dabney-Smith C., Mila I.,
RA   Bouzayen M., Magallanes-Lundback M., DellaPenna D., McCarty D.R.,
RA   Klee H.J.;
RT   "Characterization of three members of the Arabidopsis carotenoid cleavage
RT   dioxygenase family demonstrates the divergent roles of this multifunctional
RT   enzyme family.";
RL   Plant J. 45:982-993(2006).
RN   [8]
RP   CATALYTIC ACTIVITY.
RX   PubMed=18637791; DOI=10.1042/bj20080568;
RA   Alder A., Holdermann I., Beyer P., Al-Babili S.;
RT   "Carotenoid oxygenases involved in plant branching catalyse a highly
RT   specific conserved apocarotenoid cleavage reaction.";
RL   Biochem. J. 416:289-296(2008).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=21243360; DOI=10.1007/s00299-010-0999-1;
RA   Liang Y.S., Jeon Y.A., Lim S.H., Kim J.K., Lee J.Y., Kim Y.M., Lee Y.H.,
RA   Ha S.H.;
RT   "Vascular-specific activity of the Arabidopsis carotenoid cleavage
RT   dioxygenase 7 gene promoter.";
RL   Plant Cell Rep. 30:973-980(2011).
RN   [10]
RP   CATALYTIC ACTIVITY.
RX   PubMed=22422982; DOI=10.1126/science.1218094;
RA   Alder A., Jamil M., Marzorati M., Bruno M., Vermathen M., Bigler P.,
RA   Ghisla S., Bouwmeester H., Beyer P., Al-Babili S.;
RT   "The path from beta-carotene to carlactone, a strigolactone-like plant
RT   hormone.";
RL   Science 335:1348-1351(2012).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23204501; DOI=10.1093/mp/sss138;
RA   Fukui K., Ito S., Asami T.;
RT   "Selective mimics of strigolactone actions and their potential use for
RT   controlling damage caused by root parasitic weeds.";
RL   Mol. Plant 6:88-99(2013).
CC   -!- FUNCTION: Involved in strigolactones biosynthesis by cleaving the C(27)
CC       9-cis-10'-apo-beta-carotenal produced by CCD7. Produces the C(19)
CC       carlactone and a C(8) hydroxyaldehyde. Also shows lower activity with
CC       all-trans-10'-apo-beta-carotenal producing a C(9) dialdehyde and the
CC       C(18) 13-apo-beta-carotenone. Strigolactones are hormones that inhibit
CC       tillering and shoot branching through the MAX-dependent pathway,
CC       contribute to the regulation of shoot architectural response to
CC       phosphate-limiting conditions and function as rhizosphere signal that
CC       stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger
CC       seed germination of root parasitic weeds. Also active on other
CC       carotenoid substrates like licopene or zeaxanthin.
CC       {ECO:0000269|PubMed:12815068, ECO:0000269|PubMed:15342640,
CC       ECO:0000269|PubMed:16507088}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-cis-10'-apo-beta-carotenal + 2 O2 = (2E,4E,6E)-7-hydroxy-4-
CC         methylhepta-2,4,6-trienal + carlactone; Xref=Rhea:RHEA:34403,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:67190, ChEBI:CHEBI:67191,
CC         ChEBI:CHEBI:67192; EC=1.13.11.69;
CC         Evidence={ECO:0000269|PubMed:22422982};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-10'-apo-beta-carotenal + O2 = (2E,4E,6E)-4-
CC         methylocta-2,4,6-trienedial + 13-apo-beta-carotenone;
CC         Xref=Rhea:RHEA:26401, ChEBI:CHEBI:15379, ChEBI:CHEBI:53153,
CC         ChEBI:CHEBI:53175, ChEBI:CHEBI:53176; EC=1.13.11.70;
CC         Evidence={ECO:0000269|PubMed:21243360};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:16507088}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, inflorescence
CC       stems, petiole and leaves, and at a much higher level in roots.
CC       {ECO:0000269|PubMed:12815068, ECO:0000269|PubMed:16507088,
CC       ECO:0000269|PubMed:21243360}.
CC   -!- INDUCTION: Up-regulated by auxin in the root and hypocotyl.
CC       {ECO:0000269|PubMed:12815068, ECO:0000269|PubMed:16262707}.
CC   -!- DISRUPTION PHENOTYPE: Increased shoot branching.
CC       {ECO:0000269|PubMed:15342640, ECO:0000269|PubMed:23204501}.
CC   -!- MISCELLANEOUS: The branching phenotypes of the max1, ccd7/max3 and
CC       ccd8/max4 mutants can be rescued by exogenous treatment with the
CC       synthetic strigolactone analogs GR24 and 4BD.
CC       {ECO:0000305|PubMed:23204501}.
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB79998.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL161582; CAB79998.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86121.1; -; Genomic_DNA.
DR   EMBL; AY074264; AAL66961.1; -; mRNA.
DR   EMBL; AY133732; AAM91666.1; -; mRNA.
DR   PIR; T10688; T10688.
DR   RefSeq; NP_195007.2; NM_119434.4.
DR   AlphaFoldDB; Q8VY26; -.
DR   SMR; Q8VY26; -.
DR   STRING; 3702.AT4G32810.1; -.
DR   PaxDb; Q8VY26; -.
DR   ProteomicsDB; 223915; -.
DR   EnsemblPlants; AT4G32810.1; AT4G32810.1; AT4G32810.
DR   GeneID; 829417; -.
DR   Gramene; AT4G32810.1; AT4G32810.1; AT4G32810.
DR   KEGG; ath:AT4G32810; -.
DR   Araport; AT4G32810; -.
DR   TAIR; locus:2134093; AT4G32810.
DR   eggNOG; KOG1285; Eukaryota.
DR   HOGENOM; CLU_016472_1_2_1; -.
DR   InParanoid; Q8VY26; -.
DR   OMA; RAHGKVC; -.
DR   PhylomeDB; Q8VY26; -.
DR   BioCyc; ARA:AT4G32810-MON; -.
DR   BioCyc; MetaCyc:AT4G32810-MON; -.
DR   BRENDA; 1.13.11.69; 399.
DR   BRENDA; 1.13.11.70; 399.
DR   PRO; PR:Q8VY26; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8VY26; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0102396; F:9-cis-10'-apo-beta-carotenal cleavage oxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102251; F:all-trans-beta-apo-10'-carotenal cleavage oxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010436; F:carotenoid dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR   GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR   GO; GO:0016121; P:carotene catabolic process; IDA:UniProtKB.
DR   GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR   GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR   GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
DR   GO; GO:1901601; P:strigolactone biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016124; P:xanthophyll catabolic process; IDA:TAIR.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543; PTHR10543; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..570
FT                   /note="Carotenoid cleavage dioxygenase 8, chloroplastic"
FT                   /id="PRO_0000285997"
FT   BINDING         254
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         372
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         563
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   570 AA;  63957 MW;  C5772A31914477CF CRC64;
     MASLITTKAM MSHHHVLSST RITTLYSDNS IGDQQIKTKP QVPHRLFARR IFGVTRAVIN
     SAAPSPLPEK EKVEGERRCH VAWTSVQQEN WEGELTVQGK IPTWLNGTYL RNGPGLWNIG
     DHDFRHLFDG YSTLVKLQFD GGRIFAAHRL LESDAYKAAK KHNRLCYREF SETPKSVIIN
     KNPFSGIGEI VRLFSGESLT DNANTGVIKL GDGRVMCLTE TQKGSILVDH ETLETIGKFE
     YDDVLSDHMI QSAHPIVTET EMWTLIPDLV KPGYRVVRME AGSNKREVVG RVRCRSGSWG
     PGWVHSFAVT ENYVVIPEMP LRYSVKNLLR AEPTPLYKFE WCPQDGAFIH VMSKLTGEVV
     ASVEVPAYVT FHFINAYEED KNGDGKATVI IADCCEHNAD TRILDMLRLD TLRSSHGHDV
     LPDARIGRFR IPLDGSKYGK LETAVEAEKH GRAMDMCSIN PLYLGQKYRY VYACGAQRPC
     NFPNALSKVD IVEKKVKNWH EHGMIPSEPF FVPRPGATHE DDGVVISIVS EENGGSFAIL
     LDGSSFEEIA RAKFPYGLPY GLHGCWIPKD
 
 
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