CSTM6_ARATH
ID CSTM6_ARATH Reviewed; 71 AA.
AC Q9SKX9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 6 {ECO:0000303|PubMed:29272523};
DE Short=AthCYSTM6 {ECO:0000303|PubMed:29272523};
GN Name=CYSTM6 {ECO:0000303|PubMed:29272523};
GN OrderedLocusNames=At2g32210 {ECO:0000312|Araport:AT2G32210};
GN ORFNames=F22D22.4 {ECO:0000312|EMBL:AAD15384.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Southwick A., Karlin-Neumann G., Nguyen M., Lam B., Miranda M., Palm C.J.,
RA Theologis A., Ecker J., Davis R.W.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH CYSTM4; CYSTM7; CYSTM11;
RP CYSTM12 AND WIH1/CYSTM13, TISSUE SPECIFICITY, INDUCTION BY HEAT; COLD;
RP DROUGHT; OXIDATION AND SALT, 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: Involved in resistance to abiotic stress.
CC {ECO:0000303|PubMed:29272523}.
CC -!- SUBUNIT: Homodimer and heterodimers (PubMed:29272523). Interacts with
CC CYSTM7 and WIH1/CYSTM13 (PubMed:29272523).
CC {ECO:0000269|PubMed:29272523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29272523};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:29272523}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, stems, rosette leaves
CC and siliques and, to a lower extent, in flowers and cauline leaves.
CC {ECO:0000269|PubMed:29272523}.
CC -!- INDUCTION: Induced by heat in roots, but suppressed in shoots
CC (PubMed:29272523). Accumulates in response to cold, drought, oxidation
CC stress and salt (PubMed:29272523). {ECO:0000269|PubMed:29272523}.
CC -!- SIMILARITY: Belongs to the CYSTM1 family. {ECO:0000305}.
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DR EMBL; AC006223; AAD15384.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08650.1; -; Genomic_DNA.
DR EMBL; AF325079; AAK17147.1; -; mRNA.
DR EMBL; AY074358; AAL67054.1; -; mRNA.
DR EMBL; AY096443; AAM20083.1; -; mRNA.
DR EMBL; AY087099; AAM67322.1; -; mRNA.
DR PIR; C84730; C84730.
DR RefSeq; NP_565740.1; NM_128780.3.
DR AlphaFoldDB; Q9SKX9; -.
DR STRING; 3702.AT2G32210.1; -.
DR PaxDb; Q9SKX9; -.
DR PRIDE; Q9SKX9; -.
DR EnsemblPlants; AT2G32210.1; AT2G32210.1; AT2G32210.
DR GeneID; 817780; -.
DR Gramene; AT2G32210.1; AT2G32210.1; AT2G32210.
DR Araport; AT2G32210; -.
DR TAIR; locus:2045492; AT2G32210.
DR eggNOG; ENOG502S924; Eukaryota.
DR HOGENOM; CLU_128451_2_2_1; -.
DR InParanoid; Q9SKX9; -.
DR OMA; QNSPHAQ; -.
DR OrthoDB; 1607719at2759; -.
DR PhylomeDB; Q9SKX9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKX9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR InterPro; IPR028144; CYSTM_dom.
DR InterPro; IPR044850; WIH2-like.
DR PANTHER; PTHR31568; PTHR31568; 1.
DR Pfam; PF12734; CYSTM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..71
FT /note="Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 6"
FT /id="PRO_0000454803"
FT TRANSMEM 48..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 71 AA; 7337 MW; 7BD8F5612539CA5F CRC64;
MSQYSQNQSS GAYPTPPVST GPYVAPPPLG YPTNDTSHAT VATVETKSKG DGFLKGCLAA
MCCCCVLDAC F
