PRU1_PRUDU
ID PRU1_PRUDU Reviewed; 551 AA.
AC Q43607;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Prunin 1 Pru du 6 {ECO:0000305};
DE Short=Pru 1 Pru du 6 {ECO:0000305};
DE AltName: Full=11S globulin {ECO:0000303|PubMed:19694440};
DE AltName: Full=11S seed storage protein {ECO:0000303|PubMed:18553996, ECO:0000303|PubMed:19694440};
DE AltName: Full=Amandin Pru du 6 {ECO:0000305};
DE AltName: Full=Pru du amandin {ECO:0000303|PubMed:18097098};
DE AltName: Allergen=Pru du 6 {ECO:0000305};
DE Contains:
DE RecName: Full=Prunin 1 Pru du 6 acidic chain {ECO:0000305};
DE Contains:
DE RecName: Full=Prunin 1 Pru du 6 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:CAA55009.1};
RN [1] {ECO:0000312|EMBL:CAA55009.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Immature seed {ECO:0000303|PubMed:7865791,
RC ECO:0000312|EMBL:CAA55009.1};
RX PubMed=7865791; DOI=10.1007/bf00019192;
RA Garcia-Mas J., Messeguer R., Arus P., Puigdomenech P.;
RT "Molecular characterization of cDNAs corresponding to genes expressed
RT during almond (Prunus amygdalus Batsch) seed development.";
RL Plant Mol. Biol. 27:205-210(1995).
RN [2]
RP PROTEIN SEQUENCE OF 21-50 AND 368-393, CRYSTALLIZATION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=18553996; DOI=10.1021/jf800529k;
RA Albillos S.M., Jin T., Howard A., Zhang Y., Kothary M.H., Fu T.J.;
RT "Purification, crystallization and preliminary X-ray characterization of
RT prunin-1, a major component of the almond (Prunus dulcis) allergen
RT amandin.";
RL J. Agric. Food Chem. 56:5352-5358(2008).
RN [3]
RP PROTEIN SEQUENCE OF 21-35 AND 368-387, CRYSTALLIZATION, TISSUE SPECIFICITY,
RP AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=18097098; DOI=10.1107/s1744309107064615;
RA Gaur V., Sethi D.K., Salunke D.M.;
RT "Purification, identification and preliminary crystallographic studies of
RT Pru du amandin, an allergenic protein from Prunus dulcis.";
RL Acta Crystallogr. F 64:32-35(2008).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=19374443; DOI=10.1021/jf803977z;
RA Albillos S.M., Menhart N., Fu T.J.;
RT "Structural stability of Amandin, a major allergen from almond (Prunus
RT dulcis), and its acidic and basic polypeptides.";
RL J. Agric. Food Chem. 57:4698-4705(2009).
RN [5] {ECO:0007744|PDB:3EHK}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 21-551, AND DISULFIDE BONDS.
RA Gaur V., Salunke D.M.;
RT "Crystal structure of Pru du amandin, an allergenic protein from prunus
RT dulcis.";
RL Submitted (SEP-2008) to the PDB data bank.
RN [6] {ECO:0007744|PDB:3FZ3}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 21-551, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=19694440; DOI=10.1021/jf9017355;
RA Jin T., Albillos S.M., Guo F., Howard A., Fu T.J., Kothary M.H.,
RA Zhang Y.Z.;
RT "Crystal structure of prunin-1, a major component of the almond (Prunus
RT dulcis) allergen amandin.";
RL J. Agric. Food Chem. 57:8643-8651(2009).
CC -!- FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681,
CC ECO:0000305|PubMed:18097098, ECO:0000305|PubMed:18553996,
CC ECO:0000305|PubMed:19374443, ECO:0000305|PubMed:7865791}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable up to 77 degrees Celsius. Complete thermal denaturation
CC at 90 degrees Celsius. Thermal stability decreases in the presence of
CC a reducing agent, dithiothreitol (DTT). The acidic and basic chains
CC have lower thermal stabilities than the native multimeric protein.
CC {ECO:0000269|PubMed:19374443};
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:0000269|PubMed:18553996,
CC ECO:0000269|PubMed:19694440}.
CC -!- TISSUE SPECIFICITY: Expressed in seed (at protein level)
CC (PubMed:18553996, PubMed:18097098, PubMed:19374443). Expressed in seed
CC (PubMed:7865791). {ECO:0000269|PubMed:18097098,
CC ECO:0000269|PubMed:18553996, ECO:0000269|PubMed:19374443,
CC ECO:0000269|PubMed:7865791}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed development. Expressed in
CC cotyledons 110 and 120 days after flowering (DAF). Not expressed in
CC pericarp, root of 30-day germinating plantlet or young leaf.
CC {ECO:0000269|PubMed:7865791}.
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:18097098, ECO:0000305|PubMed:18553996,
CC ECO:0000305|PubMed:19374443}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to almonds (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000255|RuleBase:RU003681, ECO:0000305}.
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DR EMBL; X78119; CAA55009.1; -; mRNA.
DR PIR; S51941; S51941.
DR PDB; 3EHK; X-ray; 3.20 A; A/B/C/D/E/F=21-551.
DR PDB; 3FZ3; X-ray; 2.40 A; A/B/C/D/E/F=21-551.
DR PDBsum; 3EHK; -.
DR PDBsum; 3FZ3; -.
DR AlphaFoldDB; Q43607; -.
DR SMR; Q43607; -.
DR Allergome; 1078; Pru du 6.
DR ABCD; Q43607; 2 sequenced antibodies.
DR EvolutionaryTrace; Q43607; -.
DR GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IC:UniProtKB.
DR GO; GO:0048825; P:cotyledon development; IEP: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 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|RuleBase:RU003681,
FT ECO:0000305|PubMed:18553996"
FT CHAIN 21..367
FT /note="Prunin 1 Pru du 6 acidic chain"
FT /evidence="ECO:0000255|RuleBase:RU003681,
FT ECO:0000305|PubMed:18097098, ECO:0000305|PubMed:18553996"
FT /id="PRO_5007750930"
FT CHAIN 368..551
FT /note="Prunin 1 Pru du 6 basic chain"
FT /evidence="ECO:0000305|PubMed:18097098,
FT ECO:0000305|PubMed:18553996"
FT /id="PRO_0000448060"
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 238..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 367..372
FT /note="NGXEET; peptidase recognition motif"
FT /evidence="ECO:0000305|PubMed:18553996,
FT ECO:0000305|PubMed:19694440"
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 337..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19694440,
FT ECO:0007744|PDB:3FZ3"
FT DISULFID 32..65
FT /evidence="ECO:0000269|PubMed:19694440,
FT ECO:0007744|PDB:3EHK, ECO:0007744|PDB:3FZ3"
FT DISULFID 108..374
FT /note="Interchain (between acidic and basic chains)"
FT /evidence="ECO:0000269|PubMed:19694440,
FT ECO:0007744|PDB:3EHK, ECO:0007744|PDB:3FZ3"
FT TURN 28..32
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:3EHK"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:3FZ3"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:3FZ3"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 437..451
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 457..464
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 476..494
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 514..521
FT /evidence="ECO:0007829|PDB:3FZ3"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:3FZ3"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:3FZ3"
SQ SEQUENCE 551 AA; 63017 MW; 70D93418A222BA8F CRC64;
MAKAFVFSLC LLLVFNGCLA ARQSQLSPQN QCQLNQLQAR EPDNRIQAEA GQIETWNFNQ
GDFQCAGVAA SRITIQRNGL HLPSYSNAPQ LIYIVQGRGV LGAVFSGCPE TFEESQQSSQ
QGRQQEQEQE RQQQQQGEQG RQQGQQEQQQ ERQGRQQGRQ QQEEGRQQEQ QQGQQGRPQQ
QQQFRQLDRH QKTRRIREGD VVAIPAGVAY WSYNDGDQEL VAVNLFHVSS DHNQLDQNPR
KFYLAGNPEN EFNQQGQSQP RQQGEQGRPG QHQQPFGRPR QQEQQGNGNN VFSGFNTQLL
AQALNVNEET ARNLQGQNDN RNQIIQVRGN LDFVQPPRGR QEREHEERQQ EQLQQERQQQ
GEQLMANGLE ETFCSLRLKE NIGNPERADI FSPRAGRIST LNSHNLPILR FLRLSAERGF
FYRNGIYSPH WNVNAHSVVY VIRGNARVQV VNENGDAILD QEVQQGQLFI VPQNHGVIQQ
AGNQGFEYFA FKTEENAFIN TLAGRTSFLR ALPDEVLANA YQISREQARQ LKYNRQETIA
LSSSQQRRAV V
