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CYSP1_ORYSJ
ID   CYSP1_ORYSJ             Reviewed;         490 AA.
AC   Q7XR52; Q0J960;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Cysteine protease 1;
DE            EC=3.4.22.-;
DE   AltName: Full=OsCP1;
DE   Flags: Precursor;
GN   Name=CP1; OrderedLocusNames=Os04g0670500, LOC_Os04g57490;
GN   ORFNames=OSJNBa0043A12.33;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15356393; DOI=10.1023/b:plan.0000040904.15329.29;
RA   Lee S., Jung K.-H., An G., Chung Y.-Y.;
RT   "Isolation and characterization of a rice cysteine protease gene, OsCP1,
RT   using T-DNA gene-trap system.";
RL   Plant Mol. Biol. 54:755-765(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=16141453; DOI=10.1105/tpc.105.034090;
RA   Jung K.H., Han M.J., Lee Y.S., Kim Y.W., Hwang I., Kim M.J., Kim Y.K.,
RA   Nahm B.H., An G.;
RT   "Rice undeveloped tapetum1 is a major regulator of early tapetum
RT   development.";
RL   Plant Cell 17:2705-2722(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=17138695; DOI=10.1105/tpc.106.044107;
RA   Li N., Zhang D.S., Liu H.S., Yin C.S., Li X.X., Liang W.Q., Yuan Z., Xu B.,
RA   Chu H.W., Wang J., Wen T.Q., Huang H., Luo D., Ma H., Zhang D.B.;
RT   "The rice tapetum degeneration retardation gene is required for tapetum
RT   degradation and anther development.";
RL   Plant Cell 18:2999-3014(2006).
CC   -!- FUNCTION: Cysteine protease that may play a role in pollen development
CC       (PubMed:15356393). May be regulated by the transcription factor UDT1 in
CC       developing anthers and play a role in tapetum development
CC       (PubMed:16141453). Positively regulated by the transcription factor TDR
CC       in developing anthers and may play a role in tapetum programmed cell
CC       death (PCD) (PubMed:17138695). {ECO:0000269|PubMed:15356393,
CC       ECO:0000269|PubMed:16141453, ECO:0000269|PubMed:17138695}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the tapetum and developing
CC       pollen of the anther locules. Weakly expressed in root and germinating
CC       seed, hardly in the anther-less-flower and not detected in leaf.
CC       {ECO:0000269|PubMed:15356393}.
CC   -!- DISRUPTION PHENOTYPE: Plants show overall delay of growth and
CC       development, and mature plants are dwarf. Panicle of CP1 mutant
CC       contains several flowers which remain unfertilized due to the abnormal
CC       development of the pollen. {ECO:0000269|PubMed:15356393}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; AL606619; CAE02828.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF16127.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS91556.1; -; Genomic_DNA.
DR   EMBL; AK107506; BAG98070.1; -; mRNA.
DR   RefSeq; XP_015637044.1; XM_015781558.1.
DR   AlphaFoldDB; Q7XR52; -.
DR   SMR; Q7XR52; -.
DR   STRING; 4530.OS04T0670500-01; -.
DR   MEROPS; C01.029; -.
DR   PaxDb; Q7XR52; -.
DR   PRIDE; Q7XR52; -.
DR   EnsemblPlants; Os04t0670500-01; Os04t0670500-01; Os04g0670500.
DR   GeneID; 4337353; -.
DR   Gramene; Os04t0670500-01; Os04t0670500-01; Os04g0670500.
DR   KEGG; osa:4337353; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   eggNOG; KOG4296; Eukaryota.
DR   HOGENOM; CLU_012184_0_2_1; -.
DR   InParanoid; Q7XR52; -.
DR   OMA; LEFEAYN; -.
DR   OrthoDB; 1275401at2759; -.
DR   PlantReactome; R-OSA-8986768; Anther and pollen development.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q7XR52; OS.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 2.10.25.160; -; 1.
DR   InterPro; IPR000118; Granulin.
DR   InterPro; IPR037277; Granulin_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF00396; Granulin; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00277; GRAN; 1.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; Flowering;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   PROPEP          32..154
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026438"
FT   CHAIN           155..378
FT                   /note="Cysteine protease 1"
FT                   /id="PRO_0000026439"
FT   PROPEP          379..490
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000046022"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        339
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        177..220
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        211..253
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        311..364
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        395..407
FT                   /evidence="ECO:0000250|UniProtKB:P25777"
FT   DISULFID        401..422
FT                   /evidence="ECO:0000250|UniProtKB:P25777"
SQ   SEQUENCE   490 AA;  52642 MW;  2204406481285C8A CRC64;
     MAGGGGKSVA AALAMACFLL ILAAFAPPAA AAPPDIMSII RYNAEHGVRG LERTEAEARA
     AYDLWLARHR RGGGGGSRNG FIGEHERRFR VFWDNLKFVD AHNARADERG GFRLGMNRFA
     DLTNGEFRAT YLGTTPAGRG RRVGEAYRHD GVEALPDSVD WRDKGAVVAP VKNQGQCGSC
     WAFSAVAAVE GINKIVTGEL VSLSEQELVE CARNGQNSGC NGGIMDDAFA FIARNGGLDT
     EEDYPYTAMD GKCNLAKRSR KVVSIDGFED VPENDELSLQ KAVAHQPVSV AIDAGGREFQ
     LYDSGVFTGR CGTNLDHGVV AVGYGTDAAT GAAYWTVRNS WGPDWGENGY IRMERNVTAR
     TGKCGIAMMA SYPIKKGPNP KPSPPSPAPS PPQQCDRYSK CPAGTTCCCN YGIRNHCIVW
     GCCPVEGATC CKDHSTCCPK EYPVCNAKAR TCSKSKNSPY NIRTPAAMAR SVPEQPDSIS
     FVVLNREDLV
 
 
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