CUCIN_ORYSI
ID CUCIN_ORYSI Reviewed; 470 AA.
AC B8AL97;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cupincin {ECO:0000303|PubMed:23763241};
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 ORFNames=OsI_13867 {ECO:0000312|EMBL:EEC76319.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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 [2]
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).
RN [3]
RP PROTEIN SEQUENCE OF 35-42; 222-226 AND 351-356, IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=cv. IR64;
RX PubMed=27064905; DOI=10.1371/journal.pone.0152819;
RA Sreedhar R., Kaul Tiku P.;
RT "Cupincin: A unique protease purified from rice (Oryza sativa L.) bran is a
RT new member of the cupin superfamily.";
RL PLoS ONE 11:E0152819-E0152819(2016).
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 (PubMed:27064905). {ECO:0000269|PubMed:27064905,
CC ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:27064905};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:27064905};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:27064905};
CC -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:27064905}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:23763241}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; CM000128; EEC76319.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AL97; -.
DR SMR; B8AL97; -.
DR STRING; 39946.B8AL97; -.
DR EnsemblPlants; BGIOSGA013715-TA; BGIOSGA013715-PA; BGIOSGA013715.
DR Gramene; BGIOSGA013715-TA; BGIOSGA013715-PA; BGIOSGA013715.
DR HOGENOM; CLU_018703_2_0_1; -.
DR OMA; ELTGDEC; -.
DR Proteomes; UP000007015; Chromosome 3.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IPI:UniProtKB.
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; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Seed storage protein; Signal; Storage protein; Zinc.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:27064905"
FT CHAIN 35..470
FT /note="Cupincin"
FT /id="PRO_5002864708"
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..57
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:0000305|PubMed:27064905"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:27064905"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:27064905"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 470 AA; 52060 MW; AA485B9935705193 CRC64;
MAKKKTSSSM ARSQLAALLI SLCFLSLASN AVGWSRRGER EEEDERRRHG GEGGRPYHFG
EESFRHWTRT RHGRFSVLER FPDEQVVGAA VGGYRVAVLE AAPRAFLQPS HYDADEVFYV
KEGEGVIVLL REGRKESFCV REGDAMVIPA GAIVYSANTH SSKWFRVVML LNPVSTPGHF
EEYFPVGGDR PESFFSAFSD DVLQAAFNTR REELEKVFER QREGGEITTA PEEQIRELSK
SCSRGGGGGS GSEWEIKPSS LTGKSPYFSN NHGKLFELTG DECRHLKKLD LQIGLANITR
GSMIAPNYNT RATKLAVVLQ GSGYFEMACP HVSGGGSSER REREREHGRR REEEQGEEEH
GERGEKARRY HKVRAQVREG SVIVIPASHP ATIVASEGES LAVVCFFVGA NHDEKVFLAG
RNSPLRQLDD PAKKLVFGGS AAREADRVLA AQPEQILLRG PHGRGSVSDM
