CBSX1_ARATH
ID CBSX1_ARATH Reviewed; 236 AA.
AC O23193;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=CBS domain-containing protein CBSX1, chloroplastic;
DE AltName: Full=CBS domain-containing protein 2;
DE Short=AtCDCP2;
DE AltName: Full=Protein LOSS OF THE TIMING OF ET AND JA BIOSYNTHESIS 2;
DE Short=AtLEJ2;
DE Flags: Precursor;
GN Name=CBSX1; Synonyms=CDCP2; OrderedLocusNames=At4g36910;
GN ORFNames=AP22.61, C7A10.450;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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].
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 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 [6]
RP CRYSTALLIZATION.
RX PubMed=18765915; DOI=10.1107/s1744309108025128;
RA Jeong B.C., Yoo K.S., Jung K.W., Shin J.S., Song H.K.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of a cystathionine beta-synthase domain-containing protein, CDCP2, from
RT Arabidopsis thaliana.";
RL Acta Crystallogr. F 64:825-827(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19400948; DOI=10.1186/1471-2164-10-200;
RA Kushwaha H.R., Singh A.K., Sopory S.K., Singla-Pareek S.L., Pareek A.;
RT "Genome wide expression analysis of CBS domain containing proteins in
RT Arabidopsis thaliana (L.) Heynh and Oryza sativa L. reveals their
RT developmental and stress regulation.";
RL BMC Genomics 10:200-200(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-54, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER PRO-53, 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}.
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DR EMBL; Z99707; CAB16799.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80357.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86716.1; -; Genomic_DNA.
DR EMBL; AY085164; AAM61717.1; -; mRNA.
DR EMBL; BT003835; AAO41886.1; -; mRNA.
DR EMBL; BT005190; AAO50723.1; -; mRNA.
DR PIR; H85435; H85435.
DR RefSeq; NP_195409.1; NM_119855.4.
DR PDB; 4GQV; X-ray; 2.39 A; A=72-236.
DR PDB; 4GQW; X-ray; 2.20 A; A=72-134, A=150-236.
DR PDBsum; 4GQV; -.
DR PDBsum; 4GQW; -.
DR AlphaFoldDB; O23193; -.
DR SMR; O23193; -.
DR BioGRID; 15125; 4.
DR IntAct; O23193; 4.
DR STRING; 3702.AT4G36910.1; -.
DR iPTMnet; O23193; -.
DR PaxDb; O23193; -.
DR PRIDE; O23193; -.
DR ProteomicsDB; 239097; -.
DR EnsemblPlants; AT4G36910.1; AT4G36910.1; AT4G36910.
DR GeneID; 829844; -.
DR Gramene; AT4G36910.1; AT4G36910.1; AT4G36910.
DR KEGG; ath:AT4G36910; -.
DR Araport; AT4G36910; -.
DR TAIR; locus:2114970; AT4G36910.
DR eggNOG; ENOG502QTH1; Eukaryota.
DR HOGENOM; CLU_040681_4_0_1; -.
DR InParanoid; O23193; -.
DR OMA; HLEAWER; -.
DR OrthoDB; 1373724at2759; -.
DR PhylomeDB; O23193; -.
DR PRO; PR:O23193; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23193; baseline and differential.
DR Genevisible; O23193; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:TAIR.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; CBS domain; Chloroplast; Plastid;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 54..236
FT /note="CBS domain-containing protein CBSX1, chloroplastic"
FT /id="PRO_0000403988"
FT DOMAIN 81..142
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 175..231
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4GQW"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4GQW"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:4GQW"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4GQW"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:4GQW"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4GQW"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:4GQW"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4GQW"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4GQW"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4GQW"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:4GQW"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:4GQW"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4GQW"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:4GQW"
SQ SEQUENCE 236 AA; 25769 MW; AE5D224F42A997D9 CRC64;
MDAVLYSVPL SFTPLRASSS PSSPYLLLPR FLSVQPCHKF TFSRSFPSKS RIPSASSAAG
STLMTNSSSP RSGVYTVGEF MTKKEDLHVV KPTTTVDEAL ELLVENRITG FPVIDEDWKL
VGLVSDYDLL ALDSISGSGR TENSMFPEVD STWKTFNAVQ KLLSKTNGKL VGDLMTPAPL
VVEEKTNLED AAKILLETKY RRLPVVDSDG KLVGIITRGN VVRAALQIKR SGDRNA
