CUCIN_ORYSJ
ID CUCIN_ORYSJ Reviewed; 470 AA.
AC Q852L2; Q8L8I0;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cupincin {ECO:0000305};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=52 kDa globulin-like protein {ECO:0000305};
DE AltName: Allergen=Ory s NRA;
DE Flags: Precursor;
GN OrderedLocusNames=Os03g0793700 {ECO:0000312|EMBL:BAF13447.1},
GN LOC_Os03g57960 {ECO:0000312|EMBL:ABF99314.1};
GN ORFNames=OSJNBb0060J21.10 {ECO:0000312|EMBL:AAO37963.2};
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. Zhonghua 11; TISSUE=Seed;
RA Yoon U.H., Kim Y.H.;
RT "Structural analysis of expressed sequence tags in immature seed of Oryza
RT sativa L.";
RL Sigmul Saengmyeong Gong Haghoeji 36:130-136(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang X., Li Q.Z., Huo S.N., Zhang X.S.;
RT "Oryza sativa japonica group globulin-like protein mRNA.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
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 [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 (Probable). Globulin-like protein that
CC acts as zinc metalloprotease. Cleaves specifically between Leu-15 and
CC Tyr-16 of insulin B chain, and Gln-1 and Leu-2 of neurotensin (NT)
CC peptide in vitro. May play a role as an initiating endopeptidase in
CC germinating seeds (By similarity). {ECO:0000250|UniProtKB:B8AL97,
CC ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:B8AL97};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:B8AL97}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; GU120359; ADR66992.1; -; mRNA.
DR EMBL; AY098743; AAM33459.2; -; mRNA.
DR EMBL; AC090871; AAO37963.2; -; Genomic_DNA.
DR EMBL; DP000009; ABF99314.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13447.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86810.1; -; Genomic_DNA.
DR EMBL; AK121667; BAH00598.1; -; mRNA.
DR RefSeq; XP_015628337.1; XM_015772851.1.
DR AlphaFoldDB; Q852L2; -.
DR SMR; Q852L2; -.
DR STRING; 4530.OS03T0793700-01; -.
DR Allergome; 9525; Ory s NRA.
DR Allergome; 9527; Ory s GLP52.
DR CarbonylDB; Q852L2; -.
DR PaxDb; Q852L2; -.
DR PRIDE; Q852L2; -.
DR EnsemblPlants; Os03t0793700-01; Os03t0793700-01; Os03g0793700.
DR GeneID; 4334398; -.
DR Gramene; Os03t0793700-01; Os03t0793700-01; Os03g0793700.
DR KEGG; osa:4334398; -.
DR eggNOG; ENOG502QQEP; Eukaryota.
DR HOGENOM; CLU_018703_2_0_1; -.
DR InParanoid; Q852L2; -.
DR OMA; ELTGDEC; -.
DR OrthoDB; 1072107at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 2.
PE 1: Evidence at protein level;
KW Allergen; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Seed storage protein; Signal;
KW Storage protein; Zinc.
FT SIGNAL 1..34
FT /evidence="ECO:0000250|UniProtKB:B8AL97"
FT CHAIN 35..470
FT /note="Cupincin"
FT /id="PRO_5007214105"
FT DOMAIN 57..215
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 259..445
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 36..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:B8AL97"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:B8AL97"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:B8AL97"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 40
FT /note="R -> Q (in Ref. 2; AAM33459)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="S -> P (in Ref. 2; AAM33459)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="E -> G (in Ref. 2; AAM33459)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="G -> S (in Ref. 2; AAM33459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52126 MW; 571C01DE7E4A4792 CRC64;
MAKKKTSSSM ARSQLAALLI SLCFLSLASN AVGWSRRGER EEEDERRRHG GEGGRPYHLG
EESFRHWTRT RHGRFSVLER FPDEQVVGAA VGGYRVAVLE AAPRAFLQPS HYDADEVFYV
KEGEGVIVLL REGRRESFCV REGDAMVIPA GAIVYSANTH SSKWFRVVML LNPVSTPGHF
EEYFPVGGDR PESFFSAFSD DVLQAAFNTR REELEKVFER QREGGEITTA PEEQIRELSK
SCSRGGGGGS GSEWEIKPSS LTGKSPYFSN NHGKLFELTG DECRHLKKLD LQIGLANITR
GSMIAPNYNT RATKLAVVLQ GSGYFEMACP HVSGGGSSER REREREHGRR REEEQGEEEH
GERGEKARRY HKVRAQVREE SVIVIPASHP ATIVASEGES LAVVCFFVGA NHDEKVFLAG
RNSPLRQLDD PAKKLVFGGS AAREADRVLA AQPEQILLRG PHGRGSVSDM
