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VCL6_JUGRE
ID   VCL6_JUGRE              Reviewed;         502 AA.
AC   A0A2I4E5L6;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Vicilin Jug r 6.0101 {ECO:0000305};
DE   AltName: Full=Allergen Jug r 6 {ECO:0000303|PubMed:30054513};
DE   AltName: Full=Vicilin Jug r 6 {ECO:0000303|PubMed:30054513};
DE   AltName: Allergen=Jug r 6.0101 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=LOC108986502 {ECO:0000312|RefSeq:XP_018814692.1};
OS   Juglans regia (English walnut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Juglandaceae; Juglans.
OX   NCBI_TaxID=51240 {ECO:0000312|Proteomes:UP000235220};
RN   [1] {ECO:0000312|Proteomes:UP000235220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chandler {ECO:0000312|Proteomes:UP000235220};
RX   PubMed=27145194; DOI=10.1111/tpj.13207;
RA   Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA   Stevens K.A., Paul R., Butterfield T.S., Britton M.T., Reagan R.L.,
RA   Chakraborty S., Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R.A.,
RA   Pratt K., Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M.,
RA   Salzberg S.L., Wegrzyn J.L., Langley C.H., Neale D.B.;
RT   "The walnut (Juglans regia) genome sequence reveals diversity in genes
RT   coding for the biosynthesis of non-structural polyphenols.";
RL   Plant J. 87:507-532(2016).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-37; 45-65; 74-80; 81-124; 131-160; 161-210; 211-240;
RP   241-260; 261-290; 291-320; 321-343; 344-354; 358-384; 394-400; 401-480 AND
RP   481-502, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, PTM,
RP   IDENTIFICATION BY MASS SPECTROMETRY, MASS SPECTROMETRY, ALLERGEN,
RP   BIOTECHNOLOGY, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-340, AND CIRCULAR
RP   DICHROISM ANALYSIS.
RX   PubMed=30054513; DOI=10.1038/s41598-018-29656-4;
RA   Dubiela P., Kabasser S., Smargiasso N., Geiselhart S., Bublin M.,
RA   Hafner C., Mazzucchelli G., Hoffmann-Sommergruber K.;
RT   "Jug r 6 is the allergenic vicilin present in walnut responsible for IgE
RT   cross-reactivities to other tree nuts and seeds.";
RL   Sci. Rep. 8:11366-11366(2018).
CC   -!- FUNCTION: Seed storage protein. {ECO:0000305|PubMed:30054513}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Denaturation starts at 45 degrees Celsius. At temperatures above 75
CC         degrees Celsius, begins to precipitate, and eventually becomes
CC         irreversibly denatured. Cannot be resolubilized in aqueous solution
CC         after being heated up to 95 degrees Celsius and then cooled down to
CC         25 degrees Celsius. {ECO:0000269|PubMed:30054513};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:30054513}.
CC   -!- TISSUE SPECIFICITY: Expressed in seed (at protein level).
CC       {ECO:0000269|PubMed:30054513}.
CC   -!- PTM: N-glycosylated; paucimannose-type structures containing xylose.
CC       {ECO:0000269|PubMed:30054513}.
CC   -!- MASS SPECTROMETRY: Mass=47155; Method=MALDI; Note=Non-glycosylated.;
CC       Evidence={ECO:0000269|PubMed:30054513};
CC   -!- MASS SPECTROMETRY: Mass=48829; Method=Electrospray; Note=Glycosylated.;
CC       Evidence={ECO:0000269|PubMed:30054513};
CC   -!- ALLERGEN: Causes an allergic reaction in human. Natural protein binds
CC       to IgE in 26% of the 77 walnut-allergic patients tested. IgE-binding is
CC       reduced by simulated gastric fluid and in vitro duodenal digestion, but
CC       not by heat treatment. Cross-reacts with its counterparts from hazelnut
CC       (Cor a 11), pistachio and sesame. {ECO:0000269|PubMed:30054513}.
CC   -!- BIOTECHNOLOGY: Could be used as a marker of IgE cross-reactivity among
CC       the vicilins of tree nuts in component resolved diagnosis.
CC       {ECO:0000305|PubMed:30054513}.
CC   -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC       {ECO:0000305}.
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DR   RefSeq; XP_018814692.1; XM_018959147.1.
DR   AlphaFoldDB; A0A2I4E5L6; -.
DR   SMR; A0A2I4E5L6; -.
DR   STRING; 51240.A0A2I4E5L6; -.
DR   Allergome; 12005; Jug r 6.
DR   Allergome; 12006; Jug r 6.0101.
DR   EnsemblPlants; Jr08_13930_p1; cds.Jr08_13930_p1; Jr08_13930.
DR   GeneID; 108986502; -.
DR   Gramene; Jr08_13930_p1; cds.Jr08_13930_p1; Jr08_13930.
DR   KEGG; jre:108986502; -.
DR   OrthoDB; 1072107at2759; -.
DR   Proteomes; UP000235220; Chromosome 8.
DR   GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR   GO; GO:0045735; F:nutrient reservoir activity; IC:UniProtKB.
DR   GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR   GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
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; Reference proteome;
KW   Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:30054513"
FT   CHAIN           28..502
FT                   /note="Vicilin Jug r 6.0101"
FT                   /evidence="ECO:0000305|PubMed:30054513"
FT                   /id="PRO_5014181227"
FT   DOMAIN          101..259
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          302..475
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          67..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            73..74
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000269|PubMed:30054513"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:30054513"
SQ   SEQUENCE   502 AA;  57400 MW;  2736C0C0334522B5 CRC64;
     MAFKPKIPIA LLLLTSLLAI CAGLALAMQD PELKQCKHQC RHQRQFDEQE KEHCQRSCDE
     YHIEKKARER AERRRSEEGS SREEGYEEEE LGGEREEENP YVFEDEDFET RVRTDEGRIQ
     VLEKFTKRSK LLRGIENFRV AILEANPQTF ISPAHFDAEL VVFVAKGRAT ITTVREEKRE
     NFNVEQGDIM RIPAGTPVYL INRDENEKLY IVKILRPVSV PGHFEAFHGS GGEDPESFYR
     AFSWEVLEAA LKTRRDQLEK LFGKQTQGVI IKASKEQIRS MSKHEETTPR IWPFGGDSTH
     PFNLFHKRPS QSNQFGRLFE TDPKECKQLQ DLDLMVSFAN ITKGSMAGPY YNSRATKISV
     VIEGEGYFEM ACPHLSSSGS RGQREGSGSS RRRSRSGPSY QQIRGRLRPG MVFVAPAGHP
     VAVIASRNKN LQVLCFDVNA QGNIRFPLAG KNNIVNEFEK EAKELAFNFP AREVEKIFRN
     QDQEFFFPGP SRQPEEGGRA FE
 
 
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