AP25_ORYSJ
ID AP25_ORYSJ Reviewed; 438 AA.
AC Q6F4N5;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Aspartyl protease 25 {ECO:0000305};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Protein RICE ANTHER DOWN-REGULATED BY CHILLING 1 {ECO:0000303|PubMed:15215597};
DE Flags: Precursor;
GN Name=AP25 {ECO:0000303|PubMed:23385589};
GN Synonyms=RADC1 {ECO:0000303|PubMed:15215597};
GN OrderedLocusNames=Os03g0186900 {ECO:0000312|EMBL:BAF11119.1},
GN LOC_Os03g08790 {ECO:0000312|EMBL:ABF94364.1};
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], AND INDUCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=15215597; DOI=10.1271/bbb.68.1315;
RA Yamaguchi T., Nakayama K., Hayashi T., Yazaki J., Kishimoto N., Kikuchi S.,
RA Koike S.;
RT "cDNA microarray analysis of rice anther genes under chilling stress at the
RT microsporogenesis stage revealed two genes with DNA transposon Castaway in
RT the 5'-flanking region.";
RL Biosci. Biotechnol. Biochem. 68:1315-1323(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
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].
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 FUNCTION.
RX PubMed=23385589; DOI=10.1038/ncomms2396;
RA Niu N., Liang W., Yang X., Jin W., Wilson Z.A., Hu J., Zhang D.;
RT "EAT1 promotes tapetal cell death by regulating aspartic proteases during
RT male reproductive development in rice.";
RL Nat. Commun. 4:1445-1445(2013).
CC -!- FUNCTION: Anther-specific aspartic protease involved in tapetal
CC programmed cell death (PCD). Directly regulated by the transcription
CC factor EAT1/DTD in anthers during tapetum PCD and degeneration.
CC {ECO:0000269|PubMed:23385589}.
CC -!- INDUCTION: Down-regulated by chilling. {ECO:0000269|PubMed:15215597}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; AB122090; BAD26705.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF94364.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11119.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82681.1; -; Genomic_DNA.
DR EMBL; AK062232; BAG88249.1; -; mRNA.
DR EMBL; AK120050; BAG99854.1; -; mRNA.
DR RefSeq; XP_015632334.1; XM_015776848.1.
DR AlphaFoldDB; Q6F4N5; -.
DR SMR; Q6F4N5; -.
DR STRING; 4530.OS03T0186900-01; -.
DR PaxDb; Q6F4N5; -.
DR PRIDE; Q6F4N5; -.
DR EnsemblPlants; Os03t0186900-01; Os03t0186900-01; Os03g0186900.
DR GeneID; 4331874; -.
DR Gramene; Os03t0186900-01; Os03t0186900-01; Os03g0186900.
DR KEGG; osa:4331874; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_1_1; -.
DR InParanoid; Q6F4N5; -.
DR OMA; YCLPSYR; -.
DR OrthoDB; 753343at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:UniProtKB.
DR GO; GO:0009627; P:systemic acquired resistance; IEA:EnsemblPlants.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..438
FT /note="Aspartyl protease 25"
FT /id="PRO_5007211852"
FT DOMAIN 79..433
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 107..113
FT /evidence="ECO:0000250|UniProtKB:P42210"
FT DISULFID 352..394
FT /evidence="ECO:0000250|UniProtKB:P42210"
SQ SEQUENCE 438 AA; 45077 MW; D2C35C4EAE6EAE3A CRC64;
MAATTTIPLL LLLLAATVAA AAAELSVYHN VHPSSPSPLE SIIALARDDD ARLLFLSSKA
ATAGVSSAPV ASGQAPPSYV VRAGLGSPSQ QLLLALDTSA DATWAHCSPC GTCPSSSLFA
PANSSSYASL PCSSSWCPLF QGQACPAPQG GGDAAPPPAT LPTCAFSKPF ADASFQAALA
SDTLRLGKDA IPNYTFGCVS SVTGPTTNMP RQGLLGLGRG PMALLSQAGS LYNGVFSYCL
PSYRSYYFSG SLRLGAGGGQ PRSVRYTPML RNPHRSSLYY VNVTGLSVGH AWVKVPAGSF
AFDAATGAGT VVDSGTVITR WTAPVYAALR EEFRRQVAAP SGYTSLGAFD TCFNTDEVAA
GGAPAVTVHM DGGVDLALPM ENTLIHSSAT PLACLAMAEA PQNVNSVVNV IANLQQQNIR
VVFDVANSRV GFAKESCN
