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 04-NOV-2026, entry version 170. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 1EQK; NMR; -; A=39-140. DR AlphaFoldDB; P09229; -. DR BMRB; P09229; -. DR SMR; P09229; -. DR FunCoup; P09229; 117. DR STRING; 39947.P09229; -. DR MEROPS; I25.052; -. DR PaxDb; 39947-P09229; -. DR EnsemblPlants; Os01t0803200-01; Os01t0803200-01; Os01g0803200. DR Gramene; Os01t0803200-01; Os01t0803200-01; Os01g0803200. DR KEGG; dosa:Os01g0803200; -. DR eggNOG; ENOG502SC50; Eukaryota. DR InParanoid; P09229; -. DR OMA; AMCWVVG; -. DR OrthoDB; 1908104at2759; -. DR EvolutionaryTrace; P09229; -. DR Proteomes; UP000059680; Chromosome 1. DR ExpressionAtlas; P09229; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro. DR CDD; cd00042; CY; 1. DR FunFam; 3.10.450.10:FF:000025; Cysteine proteinase inhibitor; 1. DR Gene3D; 3.10.450.10; -; 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; CYSTATIN FAMILY MEMBER; 1. DR PANTHER; PTHR11413:SF110; CYSTEINE PROTEINASE INHIBITOR 6; 1. DR Pfam; PF16845; SQAPI; 1. DR SMART; SM00043; CY; 1. DR SUPFAM; SSF54403; Cystatin/monellin; 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 FT 13-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 //