CYT1_ORYSJ
ID CYT1_ORYSJ Reviewed; 140 AA.
AC P09229; Q0JIG4; Q547V7; Q7F5W6; Q9SBW0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cysteine proteinase inhibitor 1;
DE AltName: Full=Oryzacystatin I;
DE Short=OC-I;
DE AltName: Full=Oryzacystatin-1;
DE AltName: Full=OsCP1;
DE AltName: Full=SPOC-I;
DE Flags: Precursor;
GN OrderedLocusNames=Os01g0803200, LOC_Os01g58890;
GN ORFNames=P0003D09.48, P0034E02.11;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2806916; DOI=10.1016/0378-1119(89)90186-8;
RA Kondo H., Emori Y., Abe K., Suzuki K., Arai S.;
RT "Cloning and sequence analysis of the genomic DNA fragment encoding
RT oryzacystatin.";
RL Gene 81:259-265(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
RA Womack J.S., Randall J., Kemp J.D.;
RT "Oryzacystatin-I has a signal peptide.";
RL (er) Plant Gene Register PGR99-175(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
RX PubMed=10805458; DOI=10.1007/s004250050688;
RA Womack J.S., Randall J., Kemp J.D.;
RT "Identification of a signal peptide for oryzacystatin-I.";
RL Planta 210:844-847(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-140 (ISOFORM 1).
RC TISSUE=Seed;
RX PubMed=8877110;
RA Zhou Z., Zhu Z., Chen R., Liu C., Li X.;
RT "High level expression of oryzacystatin in Escherichia coli.";
RL Chin. J. Biotechnol. 12:17-24(1996).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-140 (ISOFORM 1).
RC STRAIN=cv. Aichi asahi;
RA Peng Y.L., Qin Q.M., Su S.C., Li H.;
RT "OsCPI, a rice blast inducible cysteine proteinase inhibitor.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-140 (ISOFORM 1).
RX PubMed=1422207; DOI=10.1016/1046-5928(92)90054-z;
RA Chen M.S., Johnson B., Wen L., Muthukrishnan S., Kramer K.J., Morgan T.D.,
RA Reeck G.R.;
RT "Rice cystatin: bacterial expression, purification, cysteine proteinase
RT inhibitory activity, and insect growth suppressing activity of a truncated
RT form of the protein.";
RL Protein Expr. Purif. 3:41-49(1992).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-140 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RC STRAIN=cv. Nipponbare; TISSUE=Seed;
RX PubMed=3500172; DOI=10.1016/s0021-9258(18)45453-1;
RA Abe K., Emori Y., Kondo H., Suzuki K., Arai S.;
RT "Molecular cloning of a cysteine proteinase inhibitor of rice
RT (oryzacystatin). Homology with animal cystatins and transient expression in
RT the ripening process of rice seeds.";
RL J. Biol. Chem. 262:16793-16797(1987).
RN [13]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1697595; DOI=10.1016/s0021-9258(18)55473-9;
RA Kondo H., Abe K., Nishimura I., Watanabe H., Emori Y., Arai S.;
RT "Two distinct cystatin species in rice seeds with different specificities
RT against cysteine proteinases. Molecular cloning, expression, and
RT biochemical studies on oryzacystatin-II.";
RL J. Biol. Chem. 265:15832-15837(1990).
RN [14]
RP MUTAGENESIS OF ASP-124.
RX PubMed=7655503; DOI=10.1046/j.1365-313x.1995.08010121.x;
RA Urwin P.E., Atkinson H.J., Waller D.A., McPherson M.J.;
RT "Engineered oryzacystatin-I expressed in transgenic hairy roots confers
RT resistance to Globodera pallida.";
RL Plant J. 8:121-131(1995).
RN [15]
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 [16]
RP STRUCTURE BY NMR OF 39-140.
RX PubMed=11101290; DOI=10.1021/bi0006971;
RA Nagata K., Kudo N., Abe K., Arai S., Tanokura M.;
RT "Three-dimensional solution structure of oryzacystatin-I, a cysteine
RT proteinase inhibitor of the rice, Oryza sativa L. japonica.";
RL Biochemistry 39:14753-14760(2000).
CC -!- FUNCTION: There are two distinct cystatins in rice seeds
CC (Oryzacystatin-1 and -2) with different specificities against cysteine
CC proteinases. May be involved in the control of germination by
CC inhibition of endogenous cysteine proteinases. May play a role in
CC defense by inhibiting exogenous proteases such as those present in
CC digestive tracks of insects and nematodes.
CC {ECO:0000269|PubMed:1697595}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P09229-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09229-2; Sequence=VSP_023023, VSP_023024;
CC -!- DEVELOPMENTAL STAGE: Expressed in rice seeds between 2 and 4 weeks
CC after flowering. {ECO:0000269|PubMed:1697595}.
CC -!- BIOTECHNOLOGY: Introduction by genetic manipulation and expression in
CC potato or banana confers resistance to insects and nematodes.
CC -!- SIMILARITY: Belongs to the cystatin family. Phytocystatin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33903.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA33912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB24010.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB66355.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL30830.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB86438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB92242.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M29259; AAA33912.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP003221; BAB86438.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP003232; BAB92242.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008207; BAF06464.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS74814.1; -; Genomic_DNA.
DR EMBL; AK061770; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF164378; AAF18388.1; -; Genomic_DNA.
DR EMBL; U54702; AAB66355.1; ALT_FRAME; mRNA.
DR EMBL; AF435976; AAL30830.1; ALT_INIT; mRNA.
DR EMBL; S49967; AAB24010.1; ALT_INIT; mRNA.
DR EMBL; J03469; AAA33903.1; ALT_INIT; mRNA.
DR PIR; B28464; A28464.
DR RefSeq; XP_015621143.1; XM_015765657.1. [P09229-1]
DR PDB; 1EQK; NMR; -; A=39-140.
DR PDBsum; 1EQK; -.
DR AlphaFoldDB; P09229; -.
DR BMRB; P09229; -.
DR SMR; P09229; -.
DR STRING; 4530.OS01T0803200-01; -.
DR MEROPS; I25.052; -.
DR PaxDb; P09229; -.
DR PRIDE; P09229; -.
DR EnsemblPlants; Os01t0803200-01; Os01t0803200-01; Os01g0803200. [P09229-1]
DR GeneID; 4327535; -.
DR Gramene; Os01t0803200-01; Os01t0803200-01; Os01g0803200. [P09229-1]
DR KEGG; osa:4327535; -.
DR eggNOG; ENOG502SC50; Eukaryota.
DR InParanoid; P09229; -.
DR OMA; AKVWEQP; -.
DR EvolutionaryTrace; P09229; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; P09229; baseline and differential.
DR Genevisible; P09229; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 3D-structure; Alternative splicing; Direct protein sequencing;
KW Plant defense; Protease inhibitor; Reference proteome; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..140
FT /note="Cysteine proteinase inhibitor 1"
FT /id="PRO_0000207156"
FT DOMAIN 48..135
FT /note="Cystatin"
FT MOTIF 91..95
FT /note="Secondary area of contact"
FT SITE 48
FT /note="Reactive site"
FT VAR_SEQ 77..96
FT /note="NSLLEFEKLVSVKQQVVAGT -> VSAPLYPPPYFSSSQGRSSN (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_023023"
FT VAR_SEQ 97..140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_023024"
FT MUTAGEN 124
FT /note="Missing: Increase in inhibition activity by 13-
FT fold."
FT /evidence="ECO:0000269|PubMed:7655503"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1EQK"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:1EQK"
FT STRAND 80..106
FT /evidence="ECO:0007829|PDB:1EQK"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:1EQK"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1EQK"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1EQK"
SQ SEQUENCE 140 AA; 15355 MW; 541263986E70C8FB CRC64;
MRKYRVAGLV AALLVLHSLA TPSAQAEAHR AGGEGEEKMS SDGGPVLGGV EPVGNENDLH
LVDLARFAVT EHNKKANSLL EFEKLVSVKQ QVVAGTLYYF TIEVKEGDAK KLYEAKVWEK
PWMDFKELQE FKPVDASANA
