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CUT1A_ARATH
ID   CUT1A_ARATH             Reviewed;         164 AA.
AC   O04616; Q38835;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Protein CURVATURE THYLAKOID 1A, chloroplastic;
DE   Flags: Precursor;
GN   Name=CURT1A; OrderedLocusNames=At4g01150; ORFNames=A_IG002N01.18, F2N1.18;
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 [MRNA].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=8580768; DOI=10.1007/bf00197600;
RA   Granot D., Dai N.;
RT   "The 5' untranslated region of Arabidopsis thaliana calmodulin cDNA is an
RT   independent cDNA containing an open reading frame.";
RL   Planta 198:162-163(1996).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=16461379; DOI=10.1104/pp.105.076083;
RA   Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT   "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT   surprising site for differential accumulation of metabolic enzymes.";
RL   Plant Physiol. 140:984-997(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-63, CLEAVAGE OF TRANSIT PEPTIDE
RP   [LARGE SCALE ANALYSIS] AFTER ARG-62, 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).
RN   [9]
RP   FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, SUBUNIT, NOMENCLATURE, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23839788; DOI=10.1105/tpc.113.113118;
RA   Armbruster U., Labs M., Pribil M., Viola S., Xu W., Scharfenberg M.,
RA   Hertle A.P., Rojahn U., Jensen P.E., Rappaport F., Joliot P., Doermann P.,
RA   Wanner G., Leister D.;
RT   "Arabidopsis CURVATURE THYLAKOID1 proteins modify thylakoid architecture by
RT   inducing membrane curvature.";
RL   Plant Cell 25:2661-2678(2013).
CC   -!- FUNCTION: Determines thylakoid architecture by inducing membrane
CC       curvature. {ECO:0000269|PubMed:23839788}.
CC   -!- SUBUNIT: Homo- and heterodimers and trimers.
CC       {ECO:0000269|PubMed:23839788}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC       {ECO:0000269|PubMed:16461379}. Membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}. Plastid, chloroplast thylakoid
CC       membrane; Multi-pass membrane protein. Note=Located almost exclusively
CC       at grana margins. {ECO:0000269|PubMed:23839788}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O04616-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: No effect on growth behavior, leaf coloration,
CC       grana stacks or photochemical efficiency of photosystem II. Curt1a,
CC       curt1b, curt1c and curt1d quadruple mutant shows disorganized
CC       thylakoids with extended stretches of unstacked membranes and broader
CC       stacks made up of fewer layers. {ECO:0000269|PubMed:23839788}.
CC   -!- SIMILARITY: Belongs to the CURT family. {ECO:0000305}.
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DR   EMBL; U19925; AAB00107.1; -; mRNA.
DR   EMBL; AF007269; AAB61025.1; -; Genomic_DNA.
DR   EMBL; AL161491; CAB80924.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE81987.1; -; Genomic_DNA.
DR   EMBL; AY091679; AAM10278.1; -; mRNA.
DR   EMBL; AF389292; AAK63864.1; -; mRNA.
DR   PIR; T01726; T01726.
DR   RefSeq; NP_567210.1; NM_116345.4. [O04616-1]
DR   AlphaFoldDB; O04616; -.
DR   BioGRID; 13470; 2.
DR   IntAct; O04616; 4.
DR   MINT; O04616; -.
DR   STRING; 3702.AT4G01150.1; -.
DR   TCDB; 8.A.155.1.1; the curt protein (curtp) family.
DR   iPTMnet; O04616; -.
DR   PaxDb; O04616; -.
DR   PRIDE; O04616; -.
DR   ProteomicsDB; 220507; -. [O04616-1]
DR   EnsemblPlants; AT4G01150.1; AT4G01150.1; AT4G01150. [O04616-1]
DR   GeneID; 828181; -.
DR   Gramene; AT4G01150.1; AT4G01150.1; AT4G01150. [O04616-1]
DR   KEGG; ath:AT4G01150; -.
DR   Araport; AT4G01150; -.
DR   TAIR; locus:2125018; AT4G01150.
DR   eggNOG; ENOG502S1VH; Eukaryota.
DR   HOGENOM; CLU_095488_1_0_1; -.
DR   InParanoid; O04616; -.
DR   OMA; DKWEDTE; -.
DR   PhylomeDB; O04616; -.
DR   PRO; PR:O04616; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O04616; baseline and differential.
DR   Genevisible; O04616; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009515; C:granal stacked thylakoid; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0090391; P:granum assembly; IMP:TAIR.
DR   GO; GO:0097753; P:membrane bending; IDA:TAIR.
DR   InterPro; IPR025564; CAAD_dom.
DR   InterPro; IPR033344; CURT1.
DR   PANTHER; PTHR33222; PTHR33222; 1.
DR   Pfam; PF14159; CAAD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chloroplast; Coiled coil; Membrane;
KW   Plastid; Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..62
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT   CHAIN           63..164
FT                   /note="Protein CURVATURE THYLAKOID 1A, chloroplastic"
FT                   /id="PRO_0000286547"
FT   TOPO_DOM        63..93
FT                   /note="Stromal"
FT                   /evidence="ECO:0000269|PubMed:23839788"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..116
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:23839788"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..164
FT                   /note="Stromal"
FT                   /evidence="ECO:0000269|PubMed:23839788"
FT   COILED          140..164
FT                   /evidence="ECO:0000255"
FT   MOD_RES         63
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        106
FT                   /note="L -> V (in Ref. 1; AAB00107)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   164 AA;  17698 MW;  8C4780A70CA1FAAE CRC64;
     MAISVAASSS MAVMVPRVPA VSTRCSAVPY LPPRSFGRSS FTVPLKLVSG NGLQKVELLK
     TRASSEETSS IDTNELITDL KEKWDGLENK STVLIYGGGA IVAVWLSSIV VGAINSVPLL
     PKVMELVGLG YTGWFVYRYL LFKSSRKELA EDIESLKKKI AGSE
 
 
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