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CRTSO_ARATH
ID   CRTSO_ARATH             Reviewed;         595 AA.
AC   Q9M9Y8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Prolycopene isomerase, chloroplastic;
DE            Short=CrtISO;
DE            EC=5.2.1.13;
DE   AltName: Full=Carotenoid and chloroplast regulation protein 2;
DE   AltName: Full=Carotenoid isomerase;
DE   Flags: Precursor;
GN   Name=CRTISO; Synonyms=CCR2; OrderedLocusNames=At1g06820; ORFNames=F4H5.10;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   FUNCTION, PATHWAY, AND ENZYME ACTIVITY.
RX   PubMed=11884677; DOI=10.1105/tpc.010302;
RA   Park H., Kreunen S.S., Cuttriss A.J., DellaPenna D., Pogson B.J.;
RT   "Identification of the carotenoid isomerase provides insight into
RT   carotenoid biosynthesis, prolamellar body formation, and
RT   photomorphogenesis.";
RL   Plant Cell 14:321-332(2002).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-57, CLEAVAGE OF TRANSIT PEPTIDE
RP   [LARGE SCALE ANALYSIS] AFTER SER-56, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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: Carotene cis-trans-isomerase that converts 7,9,9'-tri-cis-
CC       neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene
CC       (also known as prolycopene) into all-trans-lycopene. Isomerization
CC       requires redox-active components, suggesting that isomerization is
CC       achieved by a reversible redox reaction acting at specific double
CC       bonds. Isomerizes adjacent cis-double bonds at C7 and C9 pairwise into
CC       the trans-configuration, but is incapable of isomerizing single cis-
CC       double bonds at C9 and C9'. Carotenoid biosynthesis is partly required
CC       to form the prolamellar bodies of etioplasts.
CC       {ECO:0000269|PubMed:11884677}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,7',9,9'-tetra-cis-lycopene = all-trans-lycopene;
CC         Xref=Rhea:RHEA:30971, ChEBI:CHEBI:15948, ChEBI:CHEBI:62466;
CC         EC=5.2.1.13; Evidence={ECO:0000269|PubMed:11884677};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC       {ECO:0000269|PubMed:11884677}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF63149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC011001; AAF63149.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28042.1; -; Genomic_DNA.
DR   EMBL; BX813870; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A86203; A86203.
DR   RefSeq; NP_172167.2; NM_100559.4.
DR   AlphaFoldDB; Q9M9Y8; -.
DR   SMR; Q9M9Y8; -.
DR   BioGRID; 22434; 1.
DR   STRING; 3702.AT1G06820.1; -.
DR   iPTMnet; Q9M9Y8; -.
DR   PaxDb; Q9M9Y8; -.
DR   PRIDE; Q9M9Y8; -.
DR   ProteomicsDB; 220335; -.
DR   EnsemblPlants; AT1G06820.1; AT1G06820.1; AT1G06820.
DR   GeneID; 837193; -.
DR   Gramene; AT1G06820.1; AT1G06820.1; AT1G06820.
DR   KEGG; ath:AT1G06820; -.
DR   Araport; AT1G06820; -.
DR   TAIR; locus:2033055; AT1G06820.
DR   eggNOG; KOG4254; Eukaryota.
DR   HOGENOM; CLU_019722_4_1_1; -.
DR   InParanoid; Q9M9Y8; -.
DR   OMA; INYPKGG; -.
DR   OrthoDB; 873686at2759; -.
DR   PhylomeDB; Q9M9Y8; -.
DR   BioCyc; ARA:AT1G06820-MON; -.
DR   BioCyc; MetaCyc:AT1G06820-MON; -.
DR   UniPathway; UPA00803; -.
DR   PRO; PR:Q9M9Y8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M9Y8; baseline and differential.
DR   Genevisible; Q9M9Y8; AT.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046608; F:carotenoid isomerase activity; IMP:TAIR.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009662; P:etioplast organization; IMP:TAIR.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR014101; CrtISO.
DR   InterPro; IPR045892; CrtISO-like.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR46313; PTHR46313; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02730; carot_isom; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Carotenoid biosynthesis; Chloroplast; FAD; Flavoprotein;
KW   Isomerase; Membrane; NAD; NADP; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           57..595
FT                   /note="Prolycopene isomerase, chloroplastic"
FT                   /id="PRO_0000225670"
FT   MOD_RES         57
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   595 AA;  65428 MW;  01437095DF054001 CRC64;
     MDLCFQNPVK CGDRLFSALN TSTYYKLGTS NLGFNGPVLE NRKKKKKLPR MVTVKSVSSS
     VVASTVQGTK RDGGESLYDA IVIGSGIGGL VAATQLAVKE ARVLVLEKYL IPGGSSGFYE
     RDGYTFDVGS SVMFGFSDKG NLNLITQALK AVGRKMEVIP DPTTVHFHLP NNLSVRIHRE
     YDDFIAELTS KFPHEKEGIL GFYGDCWKIF NSLNSLELKS LEEPIYLFGQ FFQKPLECLT
     LAYYLPQNAG AIARKYIKDP QLLSFIDAEC FIVSTVNALQ TPMINASMVL CDRHYGGINY
     PVGGVGGIAK SLAEGLVDQG SEIQYKANVK SIILDHGKAV GVRLADGREF FAKTIISNAT
     RWDTFGKLLK GEKLPKEEEN FQKVYVKAPS FLSIHMGVKA EVLPPDTDCH HFVLEDDWKN
     LEEPYGSIFL SIPTILDSSL APDGRHILHI FTTSSIEDWE GLPPKEYEAK KEDVAARIIQ
     RLEKKLFPGL SSSITFKEVG TPRTHRRFLA RDKGTYGPMP RGTPKGLLGM PFNTTAIDGL
     YCVGDSCFPG QGVIAVAFSG VMCAHRVAAD IGLEKKSRVL DVGLLGLLGW LRTLA
 
 
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