PRU01_PRUDU
ID PRU01_PRUDU Reviewed; 551 AA.
AC E3SH28;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Prunin 1 Pru du 6.0101 {ECO:0000303|PubMed:21720172};
DE Short=Pru1 Pru du 6.0101 {ECO:0000303|PubMed:21720172};
DE AltName: Full=11S globulin {ECO:0000303|PubMed:21720172, ECO:0000303|PubMed:23498967};
DE AltName: Full=11S seed storage protein {ECO:0000303|PubMed:21720172};
DE AltName: Full=Allergen Pru du 6.01 {ECO:0000303|PubMed:21720172, ECO:0000303|PubMed:23498967};
DE AltName: Full=Amandin Pru du 6.0101 {ECO:0000303|PubMed:21720172};
DE AltName: Allergen=Pru du 6.0101 {ECO:0000303|PubMed:21720172};
DE Contains:
DE RecName: Full=Prunin 1 Pru du 6.0101 acidic chain {ECO:0000305};
DE Contains:
DE RecName: Full=Prunin 1 Pru du 6.0101 basic chain {ECO:0000305};
DE Flags: Precursor;
OS Prunus dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755 {ECO:0000312|EMBL:ADN39440.1};
RN [1] {ECO:0000312|EMBL:ADN39440.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP ALLERGEN, AND REGIONS.
RC TISSUE=Immature seed {ECO:0000303|PubMed:21720172};
RX PubMed=21720172; DOI=10.1159/000323887;
RA Willison L.N., Tripathi P., Sharma G., Teuber S.S., Sathe S.K., Roux K.H.;
RT "Cloning, expression and patient IgE reactivity of recombinant Pru du 6, an
RT 11S globulin from almond.";
RL Int. Arch. Allergy Immunol. 156:267-281(2011).
RN [2]
RP TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=23498967; DOI=10.1016/j.molimm.2013.02.004;
RA Willison L.N., Zhang Q., Su M., Teuber S.S., Sathe S.K., Roux K.H.;
RT "Conformational epitope mapping of Pru du 6, a major allergen from almond
RT nut.";
RL Mol. Immunol. 55:253-263(2013).
CC -!- FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681,
CC ECO:0000305|PubMed:21720172, ECO:0000305|PubMed:23498967}.
CC -!- SUBUNIT: Hexamer of two trimers; each subunit is composed of an acidic
CC and a basic chain derived from a single precursor and linked by a
CC disulfide bond. {ECO:0000305|PubMed:23498967}.
CC -!- TISSUE SPECIFICITY: Expressed in seed (at protein level)
CC (PubMed:21720172, PubMed:23498967). {ECO:0000269|PubMed:21720172,
CC ECO:0000269|PubMed:23498967}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed development.
CC {ECO:0000269|PubMed:21720172}.
CC -!- PTM: Proteolytically processed from a single precursor to produce an
CC acidic and a basic chain that are linked by a disulfide bond.
CC {ECO:0000305|PubMed:21720172, ECO:0000305|PubMed:23498967}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to almonds (PubMed:21720172, PubMed:23498967). Binds
CC to IgE in 50% of the 18 patients tested. Treatment with denaturing
CC agents, such as 6 M urea, reducing buffer or 10% SDS, have little
CC effect on IgE-binding intensity in a subset of these patients
CC (PubMed:21720172). The mouse IgG monoclonal antibody (mAb) 4C10 reacts
CC with non-reduced, but not the reduced form of this protein, and
CC competes with patient IgE-binding. The conformational binding site of
CC the antibody on this protein is in close proximity with a subset (118-
CC 132, 145-159 and 281-295) of patient sequential IgE-binding epitopes
CC suggesting that these regions may be highly immunogenic
CC (PubMed:23498967). {ECO:0000269|PubMed:21720172,
CC ECO:0000269|PubMed:23498967}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000255|RuleBase:RU003681, ECO:0000305}.
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DR EMBL; GU059260; ADN39440.1; -; mRNA.
DR AlphaFoldDB; E3SH28; -.
DR SMR; E3SH28; -.
DR Allergome; 1078; Pru du 6.
DR Allergome; 8426; Pru du 6.0101.
DR ABCD; E3SH28; 2 sequenced antibodies.
DR GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IC:UniProtKB.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR GO; GO:0048316; P:seed development; IEP:UniProtKB.
DR Gene3D; 2.60.120.10; -; 3.
DR InterPro; IPR022379; 11S_seedstore_CS.
DR InterPro; IPR006044; 11S_seedstore_pln.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR PRINTS; PR00439; 11SGLOBULIN.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE 1: Evidence at protein level;
KW Allergen; Disulfide bond; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|RuleBase:RU003681"
FT CHAIN 21..367
FT /note="Prunin 1 Pru du 6.0101 acidic chain"
FT /id="PRO_5007749900"
FT CHAIN 368..551
FT /note="Prunin 1 Pru du 6.0101 basic chain"
FT /evidence="ECO:0000250|UniProtKB:Q43607"
FT /id="PRO_0000448061"
FT DOMAIN 37..312
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 380..529
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 111..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..132
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21720172"
FT REGION 145..159
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21720172"
FT REGION 161..175
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21720172"
FT REGION 225..239
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21720172"
FT REGION 238..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..295
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21720172"
FT REGION 311..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..524
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21720172"
FT MOTIF 367..372
FT /note="NGXEET; peptidase recognition motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 111..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 32..65
FT /evidence="ECO:0000250|UniProtKB:Q43607"
FT DISULFID 108..374
FT /note="Interchain (between acidic and basic chains)"
FT /evidence="ECO:0000250|UniProtKB:Q43607"
SQ SEQUENCE 551 AA; 63052 MW; 8499EF9CFEDD55C3 CRC64;
MAKAFVFSLC LLLVFNGCLA ARQSQLSPQN QCQLNQLQAR EPDNRIQAEA GQIETWNFNQ
EDFQCAGVAA SRITIQRNGL HLPSYSNAPQ LIYIVQGRGV LGAVFSGCPE TFEESQQSSQ
QGRQQEQEQE RQQQQQGEQG RQQGQQEQQQ ERQGRQQGRQ QQEEGRQQEQ QQGQQGRPQQ
QQQFRQFDRH QKTRRIREGD VVAIPAGVAY WSYNDGDQEL VAVNLFHVSS DHNQLDQNPR
KFYLAGNPEN EFNQQGQSQP RQQGEQGRPG QHQQPFGRPR QQEQQGSGNN VFSGFNTQLL
AQALNVNEET ARNLQGQNDN RNQIIRVRGN LDFVQPPRGR QEREHEERQQ EQLQQERQQQ
GGQLMANGLE ETFCSLRLKE NIGNPERADI FSPRAGRIST LNSHNLPILR FLRLSAERGF
FYRNGIYSPH WNVNAHSVVY VIRGNARVQV VNENGDAILD QEVQQGQLFI VPQNHGVIQQ
AGNQGFEYFA FKTEENAFIN TLAGRTSFLR ALPDEVLANA YQISREQARQ LKYNRQETIA
LSSSQQRRAV V
