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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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