CYT1_ARATH
ID CYT1_ARATH Reviewed; 101 AA.
AC Q945Q1; O48589;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Cysteine proteinase inhibitor 1;
DE Short=AtCYS-1;
GN Name=CYS1; Synonyms=CYS; OrderedLocusNames=At5g12140; ORFNames=MXC9.10;
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 [GENOMIC DNA].
RA Belenghi B., Zelasco S., D'Angelo M., Delledonne M.;
RT "Characterization of a genomic sequence encoding cysteine proteinase
RT inhibitor from arabidopsis.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 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, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12787025; DOI=10.1046/j.1432-1033.2003.03630.x;
RA Belenghi B., Acconcia F., Trovato M., Perazzolli M., Bocedi A.,
RA Polticelli F., Ascenzi P., Delledonne M.;
RT "AtCYS1, a cystatin from Arabidopsis thaliana, suppresses hypersensitive
RT cell death.";
RL Eur. J. Biochem. 270:2593-2604(2003).
RN [7]
RP GENE FAMILY.
RX PubMed=15887031; DOI=10.1007/s00438-005-1147-4;
RA Martinez M., Abraham Z., Carbonero P., Diaz I.;
RT "Comparative phylogenetic analysis of cystatin gene families from
RT arabidopsis, rice and barley.";
RL Mol. Genet. Genomics 273:423-432(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 -!- FUNCTION: Involved in suppression of hypersensitive cell death
CC activated by either avirulent pathogen or oxidative stress.
CC {ECO:0000269|PubMed:12787025}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and developing siliques.
CC {ECO:0000269|PubMed:12787025}.
CC -!- INDUCTION: By wounding, nitric oxide and infection by avirulent
CC pathogen. {ECO:0000269|PubMed:12787025}.
CC -!- SIMILARITY: Belongs to the cystatin family. Phytocystatin subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ000110; CAA03929.1; -; Genomic_DNA.
DR EMBL; AB007727; BAB10032.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91767.1; -; Genomic_DNA.
DR EMBL; AF411786; AAL06476.1; -; mRNA.
DR EMBL; AY113053; AAM47361.1; -; mRNA.
DR EMBL; AY088332; AAM65871.1; -; mRNA.
DR RefSeq; NP_196775.1; NM_121252.3.
DR AlphaFoldDB; Q945Q1; -.
DR SMR; Q945Q1; -.
DR BioGRID; 16365; 3.
DR IntAct; Q945Q1; 1.
DR STRING; 3702.AT5G12140.1; -.
DR MEROPS; I25.958; -.
DR iPTMnet; Q945Q1; -.
DR PaxDb; Q945Q1; -.
DR PRIDE; Q945Q1; -.
DR ProteomicsDB; 224658; -.
DR EnsemblPlants; AT5G12140.1; AT5G12140.1; AT5G12140.
DR GeneID; 831087; -.
DR Gramene; AT5G12140.1; AT5G12140.1; AT5G12140.
DR KEGG; ath:AT5G12140; -.
DR Araport; AT5G12140; -.
DR TAIR; locus:2177063; AT5G12140.
DR eggNOG; ENOG502SC50; Eukaryota.
DR HOGENOM; CLU_113093_1_3_1; -.
DR InParanoid; Q945Q1; -.
DR OMA; RSGICRS; -.
DR OrthoDB; 1565344at2759; -.
DR PhylomeDB; Q945Q1; -.
DR PRO; PR:Q945Q1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q945Q1; baseline and differential.
DR Genevisible; Q945Q1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0070417; P:cellular response to cold; IEP:TAIR.
DR GO; GO:0034605; P:cellular response to heat; IEP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR027214; Cystatin.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR PANTHER; PTHR11413; PTHR11413; 1.
DR Pfam; PF16845; SQAPI; 1.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00287; CYSTATIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Plant defense; Protease inhibitor; Reference proteome;
KW Thiol protease inhibitor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..101
FT /note="Cysteine proteinase inhibitor 1"
FT /id="PRO_0000277493"
FT DOMAIN 11..99
FT /note="Cystatin"
FT MOTIF 55..59
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT SITE 11
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 98
FT /note="L -> H (in Ref. 4; AAL06476/AAM47361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 101 AA; 11256 MW; 1F8D5557D59321D9 CRC64;
MADQQAGTIV GGVRDIDANA NDLQVESLAR FAVDEHNKNE NLTLEYKRLL GAKTQVVAGT
MHHLTVEVAD GETNKVYEAK VLEKAWENLK QLESFNHLHD V
