CYT6_ARATH
ID CYT6_ARATH Reviewed; 234 AA.
AC Q8H0X6; Q8VZA2; Q9FUB0; Q9LHF9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Cysteine proteinase inhibitor 6;
DE Short=AtCYS-6;
DE AltName: Full=PIP-M;
DE AltName: Full=PRLI-interacting factor M;
DE Flags: Precursor;
GN Name=CYS6; OrderedLocusNames=At3g12490; ORFNames=MQC3.31, T2E22.19;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM 2).
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] OF 10-234 (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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-234 (ISOFORMS 1/2).
RC STRAIN=cv. Columbia;
RX PubMed=9765207; DOI=10.1101/gad.12.19.3059;
RA Nemeth K., Salchert K., Putnoky P., Bhalerao R., Koncz-Kalman Z.,
RA Stankovic-Stangeland B., Bako L., Mathur J., Oekresz L., Stabel S.,
RA Geigenberger P., Stitt M., Redei G.P., Schell J., Koncz C.;
RT "Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD
RT protein, in Arabidopsis.";
RL Genes Dev. 12:3059-3073(1998).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS 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 -!- FUNCTION: Specific inhibitor of cysteine proteinases. Probably involved
CC in the regulation of endogenous processes and in defense against pests
CC and pathogens (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8H0X6; F4IZC5: CAN1; NbExp=3; IntAct=EBI-8760191, EBI-8760221;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H0X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H0X6-2; Sequence=VSP_023022;
CC -!- SIMILARITY: Belongs to the cystatin family. Phytocystatin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL38303.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP002047; BAB03156.1; -; Genomic_DNA.
DR EMBL; AC069474; AAG51028.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75201.1; -; Genomic_DNA.
DR EMBL; AY085950; AAM63160.1; -; mRNA.
DR EMBL; AY065127; AAL38303.1; ALT_INIT; mRNA.
DR EMBL; BT001195; AAN65082.1; -; mRNA.
DR EMBL; AF315737; AAG31653.1; -; mRNA.
DR RefSeq; NP_850570.2; NM_180239.4. [Q8H0X6-1]
DR AlphaFoldDB; Q8H0X6; -.
DR SMR; Q8H0X6; -.
DR BioGRID; 5762; 2.
DR IntAct; Q8H0X6; 1.
DR MINT; Q8H0X6; -.
DR STRING; 3702.AT3G12490.2; -.
DR MEROPS; I25.014; -.
DR iPTMnet; Q8H0X6; -.
DR SwissPalm; Q8H0X6; -.
DR PaxDb; Q8H0X6; -.
DR PRIDE; Q8H0X6; -.
DR ProteomicsDB; 222597; -. [Q8H0X6-1]
DR EnsemblPlants; AT3G12490.2; AT3G12490.2; AT3G12490. [Q8H0X6-1]
DR GeneID; 820428; -.
DR Gramene; AT3G12490.2; AT3G12490.2; AT3G12490. [Q8H0X6-1]
DR KEGG; ath:AT3G12490; -.
DR Araport; AT3G12490; -.
DR TAIR; locus:2092492; AT3G12490.
DR eggNOG; ENOG502QRXR; Eukaryota.
DR InParanoid; Q8H0X6; -.
DR OrthoDB; 1565344at2759; -.
DR PhylomeDB; Q8H0X6; -.
DR PRO; PR:Q8H0X6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H0X6; baseline and differential.
DR Genevisible; Q8H0X6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006972; P:hyperosmotic response; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR CDD; cd00042; CY; 2.
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; 2.
DR PROSITE; PS00287; CYSTATIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Phosphoprotein; Plant defense;
KW Protease inhibitor; Reference proteome; Repeat; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..234
FT /note="Cysteine proteinase inhibitor 6"
FT /id="PRO_0000277498"
FT DOMAIN 38..126
FT /note="Cystatin 1"
FT DOMAIN 145..215
FT /note="Cystatin 2"
FT REGION 133..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 82..86
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT SITE 38
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_023022"
FT CONFLICT 123
FT /note="K -> T (in Ref. 6; AAG31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="V -> A (in Ref. 5; AAN65082)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="L -> V (in Ref. 6; AAG31653)"
FT /evidence="ECO:0000305"
FT INIT_MET Q8H0X6-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q8H0X6-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 234 AA; 26294 MW; 233170F22A899F5F CRC64;
MMRSRFLLFI VFFSLSLFIS SLIASDLGFC NEEMALVGGV GDVPANQNSG EVESLARFAV
DEHNKKENAL LEFARVVKAK EQVVAGTLHH LTLEILEAGQ KKLYEAKVWV KPWLNFKELQ
EFKPASDAPA ITSSDLGCKQ GEHESGWREV PGDDPEVKHV AEQAVKTIQQ RSNSLFPYEL
LEVVHAKAEV TGEAAKYNML LKLKRGEKEE KFKVEVHKNH EGALHLNHAE QHHD
