CUT1C_ARATH
ID CUT1C_ARATH Reviewed; 156 AA.
AC Q9M812; A8MRU7; F4ICU6; Q8LDB5;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein CURVATURE THYLAKOID 1C, chloroplastic;
DE Flags: Precursor;
GN Name=CURT1C; OrderedLocusNames=At1g52220; ORFNames=F9I5.10;
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH PSAD2, AND SUBCELLULAR LOCATION.
RX PubMed=18813226; DOI=10.1038/cr.2008.286;
RA Yu Q.B., Li G., Wang G., Sun J.C., Wang P.C., Wang C., Mi H.L., Ma W.M.,
RA Cui J., Cui Y.L., Chong K., Li Y.X., Li Y.H., Zhao Z., Shi T.L., Yang Z.N.;
RT "Construction of a chloroplast protein interaction network and functional
RT mining of photosynthetic proteins in Arabidopsis thaliana.";
RL Cell Res. 18:1007-1019(2008).
RN [6]
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. Interacts with PSAD2.
CC {ECO:0000269|PubMed:18813226, ECO:0000269|PubMed:23839788}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18813226, ECO:0000269|PubMed:23839788}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18813226,
CC ECO:0000269|PubMed:23839788}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9M812-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M812-2; Sequence=VSP_053422;
CC Name=3;
CC IsoId=Q9M812-3; Sequence=VSP_053423;
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; AC022354; AAF29409.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32769.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32770.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32771.1; -; Genomic_DNA.
DR EMBL; AF410269; AAK95255.1; -; mRNA.
DR EMBL; AY097365; AAM19881.1; -; mRNA.
DR EMBL; AY086098; AAM63306.1; -; mRNA.
DR PIR; B96562; B96562.
DR RefSeq; NP_001031173.1; NM_001036096.1. [Q9M812-2]
DR RefSeq; NP_001077703.1; NM_001084234.1. [Q9M812-3]
DR RefSeq; NP_564603.1; NM_104101.2. [Q9M812-1]
DR AlphaFoldDB; Q9M812; -.
DR BioGRID; 26877; 2.
DR IntAct; Q9M812; 5.
DR STRING; 3702.AT1G52220.1; -.
DR TCDB; 8.A.155.1.3; the curt protein (curtp) family.
DR iPTMnet; Q9M812; -.
DR PaxDb; Q9M812; -.
DR PRIDE; Q9M812; -.
DR ProteomicsDB; 220373; -. [Q9M812-1]
DR EnsemblPlants; AT1G52220.1; AT1G52220.1; AT1G52220. [Q9M812-1]
DR EnsemblPlants; AT1G52220.2; AT1G52220.2; AT1G52220. [Q9M812-2]
DR EnsemblPlants; AT1G52220.3; AT1G52220.3; AT1G52220. [Q9M812-3]
DR GeneID; 841652; -.
DR Gramene; AT1G52220.1; AT1G52220.1; AT1G52220. [Q9M812-1]
DR Gramene; AT1G52220.2; AT1G52220.2; AT1G52220. [Q9M812-2]
DR Gramene; AT1G52220.3; AT1G52220.3; AT1G52220. [Q9M812-3]
DR KEGG; ath:AT1G52220; -.
DR Araport; AT1G52220; -.
DR TAIR; locus:2037435; AT1G52220.
DR eggNOG; ENOG502S1DZ; Eukaryota.
DR InParanoid; Q9M812; -.
DR OMA; KYVTSSF; -.
DR PhylomeDB; Q9M812; -.
DR PRO; PR:Q9M812; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M812; baseline and differential.
DR Genevisible; Q9M812; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA: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 Alternative splicing; Chloroplast; Membrane; Plastid; Reference proteome;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..156
FT /note="Protein CURVATURE THYLAKOID 1C, chloroplastic"
FT /id="PRO_0000424360"
FT TOPO_DOM 56..83
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:23839788"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..109
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:23839788"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..156
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:23839788"
FT VAR_SEQ 76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053422"
FT VAR_SEQ 77..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053423"
SQ SEQUENCE 156 AA; 16946 MW; FD19F61803E95053 CRC64;
MASISATLPS PLLLTQRKSN LTSIQKLPFS LTRGTNDLSP LSLTRNPSSI SLMVKASGES
SDSSTDLDVV STIQNVWDKS EDRLGLIGLG FAGIVALWAS LNLITAIDKL PVISSGFELV
GILFSTWFTY RYLLFKPDRQ ELSKIVKKSV ADILGQ
