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AI172_ORYSJ
ID   AI172_ORYSJ             Reviewed;         159 AA.
AC   Q7X8H9;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=17kDa alpha-amylase/trypsin inhibitor 2 {ECO:0000305};
DE   AltName: Allergen=Ory s 17kD;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os07g0216700 {ECO:0000312|EMBL:BAF21106.1},
GN   LOC_Os07g11650 {ECO:0000305};
GN   ORFNames=OJ1080_F08.106 {ECO:0000312|EMBL:BAC79577.1},
GN   OJ1779_B07.133 {ECO:0000312|EMBL:BAC79682.1},
GN   OsJ_23556 {ECO:0000312|EMBL:EEE66806.1};
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 [MRNA].
RC   STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA   Yoon U.H., Kim Y.H.;
RT   "Molecular cloning of the trypsin/amylase inhibitor-like protein gene in
RT   rice.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX   PubMed=21300107; DOI=10.1016/j.yrtph.2011.01.008;
RA   Satoh R., Nakamura R., Komatsu A., Oshima M., Teshima R.;
RT   "Proteomic analysis of known and candidate rice allergens between non-
RT   transgenic and transgenic plants.";
RL   Regul. Toxicol. Pharmacol. 59:437-444(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX   PubMed=23763241; DOI=10.1021/pr4002146;
RA   Kurokawa S., Nakamura R., Mejima M., Kozuka-Hata H., Kuroda M.,
RA   Takeyama N., Oyama M., Satoh S., Kiyono H., Masumura T., Teshima R.,
RA   Yuki Y.;
RT   "MucoRice-cholera toxin B-subunit, a rice-based oral cholera vaccine, down-
RT   regulates the expression of alpha-amylase/trypsin inhibitor-like protein
RT   family as major rice allergens.";
RL   J. Proteome Res. 12:3372-3382(2013).
CC   -!- FUNCTION: Seed storage protein. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Five disulfide bonds are present. {ECO:0000250|UniProtKB:Q01883}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:21300107, ECO:0000269|PubMed:23763241}.
CC   -!- SIMILARITY: Belongs to the cereal trypsin/alpha-amylase inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; EU267993; ACA50515.1; -; mRNA.
DR   EMBL; AP003805; BAC79577.1; -; Genomic_DNA.
DR   EMBL; AP003963; BAC79682.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF21106.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT00629.1; -; Genomic_DNA.
DR   EMBL; CM000144; EEE66806.1; -; Genomic_DNA.
DR   EMBL; AK107633; BAG98111.1; -; mRNA.
DR   RefSeq; XP_015645309.1; XM_015789823.1.
DR   AlphaFoldDB; Q7X8H9; -.
DR   SMR; Q7X8H9; -.
DR   STRING; 39947.Q7X8H9; -.
DR   Allergome; 9529; Ory s 17kD.
DR   PaxDb; Q7X8H9; -.
DR   PRIDE; Q7X8H9; -.
DR   EnsemblPlants; Os07t0216700-01; Os07t0216700-01; Os07g0216700.
DR   GeneID; 4342730; -.
DR   Gramene; Os07t0216700-01; Os07t0216700-01; Os07g0216700.
DR   KEGG; osa:4342730; -.
DR   eggNOG; ENOG502R74X; Eukaryota.
DR   HOGENOM; CLU_113497_1_1_1; -.
DR   InParanoid; Q7X8H9; -.
DR   OMA; QHTGFFA; -.
DR   OrthoDB; 1732257at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd00261; AAI_SS; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR044723; AAI_SS_dom.
DR   InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00808; AMLASEINHBTR.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Reference proteome; Secreted;
KW   Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..159
FT                   /note="17kDa alpha-amylase/trypsin inhibitor 2"
FT                   /id="PRO_5007213378"
FT   DISULFID        37..91
FT                   /evidence="ECO:0000250|UniProtKB:Q01883"
FT   DISULFID        51..80
FT                   /evidence="ECO:0000250|UniProtKB:Q01883"
FT   DISULFID        59..123
FT                   /evidence="ECO:0000250|UniProtKB:Q01883"
FT   DISULFID        81..141
FT                   /evidence="ECO:0000250|UniProtKB:Q01883"
FT   DISULFID        93..151
FT                   /evidence="ECO:0000250|UniProtKB:Q01883"
SQ   SEQUENCE   159 AA;  16477 MW;  2D6F75C860FA3849 CRC64;
     MALASDKFVL SAIVLAVLTV AAAAAGYGGY GDVGEYCRVG KAVSRNPVPS CRNYIARWCA
     VAGGRLDSGK QPPRQLLEPC CRELAAVPMQ CRCDALSVLV RGVVTEEGDR VAGMISQHAA
     PGCDAATIAG MASALTDYGR CNLQHTGFFG CPMFGGGMD
 
 
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