CSTM2_ARATH
ID CSTM2_ARATH Reviewed; 62 AA.
AC Q3ECR7; F4IEL4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 2 {ECO:0000303|PubMed:29272523};
DE Short=AthCYSTM2 {ECO:0000303|PubMed:29272523};
DE AltName: Full=Protein CADMIUM TOLERANCE 1 {ECO:0000303|PubMed:19816106};
DE Short=AtCDT1 {ECO:0000303|PubMed:19816106};
DE Short=Cd tolerant 1 {ECO:0000303|PubMed:19816106};
GN Name=CYSTM2 {ECO:0000303|PubMed:29272523};
GN Synonyms=CDT1 {ECO:0000303|PubMed:19816106};
GN OrderedLocusNames=At1g52827 {ECO:0000312|Araport:AT1G52827};
GN ORFNames=F14G24 {ECO:0000312|EMBL:AC019018};
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;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=19017626; DOI=10.1093/pcp/pcn175;
RA Kuramata M., Masuya S., Takahashi Y., Kitagawa E., Inoue C., Ishikawa S.,
RA Youssefian S., Kusano T.;
RT "Novel cysteine-rich peptides from Digitaria ciliaris and Oryza sativa
RT enhance tolerance to cadmium by limiting its cellular accumulation.";
RL Plant Cell Physiol. 50:106-117(2009).
RN [5]
RP FUNCTION, AND GENE FAMILY.
RX PubMed=19816106; DOI=10.4161/psb.4.5.8272;
RA Matsuda T., Kuramata M., Takahashi Y., Kitagawa E., Youssefian S.,
RA Kusano T.;
RT "A novel plant cysteine-rich peptide family conferring cadmium tolerance to
RT yeast and plants.";
RL Plant Signal. Behav. 4:419-421(2009).
RN [6]
RP FUNCTION, INTERACTION WITH CYSTM7 AND WIH1/CYSTM13, TISSUE SPECIFICITY,
RP INDUCTION BY SALT; COLD AND DROUGHT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29272523; DOI=10.1093/pcp/pcx202;
RA Xu Y., Yu Z., Zhang D., Huang J., Wu C., Yang G., Yan K., Zhang S.,
RA Zheng C.;
RT "CYSTM, a novel non-secreted cysteine-rich peptide family, involved in
RT environmental stresses in Arabidopsis thaliana.";
RL Plant Cell Physiol. 59:423-438(2018).
CC -!- FUNCTION: [Isoform 1]: Involved in resistance to abiotic stress.
CC {ECO:0000303|PubMed:29272523}.
CC -!- FUNCTION: [Isoform 2]: Confers resistance to heavy metal ions (e.g.
CC cadmium (CdCl(2)) and copper (CuCl(2))) by chelating them at the plasma
CC membrane of root cells, thus stopping their entry and reducing their
CC accumulation. {ECO:0000269|PubMed:19816106}.
CC -!- SUBUNIT: Heterodimers (PubMed:29272523). Binds weakly to CYSTM7 and
CC WIH1/CYSTM13 (PubMed:29272523). {ECO:0000269|PubMed:29272523}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:29272523}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000269|PubMed:29272523}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000250|UniProtKB:Q5VSB5}; Single-pass membrane protein
CC {ECO:0000255}. Secreted, cell wall {ECO:0000250|UniProtKB:Q5VSB5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1; Synonyms=CYSTM2 {ECO:0000303|PubMed:29272523};
CC IsoId=Q3ECR7-1; Sequence=Displayed;
CC Name=2; Synonyms=CDT1 {ECO:0000303|PubMed:19017626};
CC IsoId=Q3ECR7-2; Sequence=VSP_061394, VSP_061395;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Mostly expressed in stems, siliques,
CC leaves and flowers and, to a lower extent, in roots.
CC {ECO:0000269|PubMed:29272523}.
CC -!- INDUCTION: [Isoform 1]: Induced by salt, cold and drought.
CC {ECO:0000269|PubMed:29272523}.
CC -!- SIMILARITY: Belongs to the CYSTM1 family. {ECO:0000305}.
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DR EMBL; AC019018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE32857.2; -; Genomic_DNA.
DR EMBL; BT025630; ABF74691.1; -; mRNA.
DR RefSeq; NP_974010.3; NM_202281.4.
DR AlphaFoldDB; Q3ECR7; -.
DR PRIDE; Q3ECR7; -.
DR EnsemblPlants; AT1G52827.1; AT1G52827.1; AT1G52827. [Q3ECR7-1]
DR GeneID; 2745823; -.
DR Gramene; AT1G52827.1; AT1G52827.1; AT1G52827. [Q3ECR7-1]
DR KEGG; ath:AT1G52827; -.
DR Araport; AT1G52827; -.
DR TAIR; locus:1006230685; AT1G52827.
DR OMA; FDFYICI; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3ECR7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0140487; F:metal ion sequestering activity; ISS:UniProtKB.
DR GO; GO:1990748; P:cellular detoxification; ISS:UniProtKB.
DR GO; GO:0071585; P:detoxification of cadmium ion; IDA:TAIR.
DR GO; GO:0010273; P:detoxification of copper ion; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Cell membrane; Cell wall; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Secreted; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..62
FT /note="Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 2"
FT /id="PRO_0000454799"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..49
FT /note="MTMSRNGKTNKAAYSQRFTRCSVAVAATRSASVVAAAFDFYICIIISTL ->
FT MKAPPQQEMTYYDNVKKRQDEQGCLFATFYALFCCCCCYEKCKCCCCCV (in
FT isoform 2)"
FT /evidence="ECO:0000305|PubMed:19017626"
FT /id="VSP_061394"
FT VAR_SEQ 50..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:19017626"
FT /id="VSP_061395"
FT TRANSMEM Q3ECR7-2:23..39
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 62 AA; 6680 MW; 91FB625EE6785111 CRC64;
MTMSRNGKTN KAAYSQRFTR CSVAVAATRS ASVVAAAFDF YICIIISTLL SLIVSLASQL
LF
