VCL_CARIL
ID VCL_CARIL Reviewed; 792 AA.
AC B3STU4;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Vicilin Car i 2.0101 {ECO:0000305};
DE AltName: Full=7S globulin {ECO:0000303|PubMed:25084379, ECO:0000303|PubMed:27128197};
DE AltName: Full=7S seed storage protein {ECO:0000303|PubMed:25084379, ECO:0000303|PubMed:27128197};
DE AltName: Full=Allergen Car i 2 {ECO:0000303|PubMed:27128197};
DE AltName: Full=Cariv {ECO:0000303|PubMed:27128197};
DE AltName: Allergen=Car i 2.0101 {ECO:0000305};
DE Flags: Precursor;
GN Name=pec2a1a {ECO:0000312|EMBL:ABV49590.1};
GN Synonyms=pec3a1a {ECO:0000312|EMBL:ABV49591.1},
GN pec4a1a {ECO:0000312|EMBL:ABV49592.1};
OS Carya illinoinensis (Pecan).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Carya.
OX NCBI_TaxID=32201 {ECO:0000312|EMBL:ABV49590.1};
RN [1] {ECO:0000312|EMBL:ABV49590.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sharma G.M., Roux K.H., Sathe S.K.;
RT "Characterization of 7S vicilin-like protein from Carya illinoinensis
RT (Pecan).";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5E1R}
RP PROTEIN SEQUENCE OF 312-316, X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF
RP 369-792 IN COMPLEX WITH COPPER, SUBUNIT, TISSUE SPECIFICITY, ALLERGEN, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=27128197; DOI=10.1021/acs.jafc.6b00884;
RA Zhang Y., Lee B., Du W.X., Lyu S.C., Nadeau K.C., Grauke L.J., Zhang Y.,
RA Wang S., Fan Y., Yi J., McHugh T.H.;
RT "Identification and Characterization of a New Pecan [Carya illinoinensis
RT (Wangenh.) K. Koch] Allergen, Car i 2.";
RL J. Agric. Food Chem. 64:4146-4151(2016).
RN [3]
RP CRYSTALLIZATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBUNIT.
RX PubMed=25084379; DOI=10.1107/s2053230x14012369;
RA Lee B., Zhang R., Du W.X., Grauke L.J., McHugh T.H., Zhang Y.Z.;
RT "Expression, purification and crystallization of pecan (Carya
RT illinoinensis) vicilin.";
RL Acta Crystallogr. F Struct. Biol. Commun. 70:1049-1052(2014).
CC -!- FUNCTION: Seed storage protein. {ECO:0000305|PubMed:25084379,
CC ECO:0000305|PubMed:27128197}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:25084379,
CC ECO:0000269|PubMed:27128197}.
CC -!- TISSUE SPECIFICITY: Expressed in seed (at protein level)
CC (PubMed:27128197). Expressed in seed (PubMed:25084379).
CC {ECO:0000269|PubMed:25084379, ECO:0000269|PubMed:27128197}.
CC -!- DEVELOPMENTAL STAGE: Expressed during nut development. Expressed in gel
CC stage of the seed kernel. {ECO:0000269|PubMed:25084379}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to pecan nuts and walnuts. Binds to IgE in 30% of the
CC 27 patients tested by Western blot and in 24% of the 25 patients tested
CC by double-blind, placebo-controlled oral food challenge.
CC {ECO:0000269|PubMed:27128197}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; EF689893; ABV49590.1; -; mRNA.
DR EMBL; EF689894; ABV49591.1; -; mRNA.
DR EMBL; EF689895; ABV49592.1; -; mRNA.
DR PDB; 5E1R; X-ray; 2.65 A; A/B/C/D/E/F=369-792.
DR PDBsum; 5E1R; -.
DR AlphaFoldDB; B3STU4; -.
DR SMR; B3STU4; -.
DR Allergome; 11949; Car i 2.0101.
DR Allergome; 9549; Car i 2.
DR PRIDE; B3STU4; -.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IC:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0048316; P:seed development; IEP: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 InterPro; IPR006792; Vicilin_N.
DR Pfam; PF00190; Cupin_1; 2.
DR Pfam; PF04702; Vicilin_N; 3.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Coiled coil; Copper; Direct protein sequencing;
KW Metal-binding; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..792
FT /note="Vicilin Car i 2.0101"
FT /evidence="ECO:0000255"
FT /id="PRO_5010824428"
FT DOMAIN 384..537
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 582..754
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 132..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 727..754
FT /evidence="ECO:0000255"
FT COMPBIAS 302..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 379
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:27128197,
FT ECO:0007744|PDB:5E1R"
FT BINDING 652
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:27128197,
FT ECO:0007744|PDB:5E1R"
FT BINDING 654
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:27128197,
FT ECO:0007744|PDB:5E1R"
FT BINDING 698
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:27128197,
FT ECO:0007744|PDB:5E1R"
FT SITE 311..312
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:27128197"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 425..445
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 487..498
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 516..519
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 522..529
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:5E1R"
FT TURN 542..545
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 555..560
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 588..593
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 596..601
FT /evidence="ECO:0007829|PDB:5E1R"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:5E1R"
FT TURN 610..613
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 614..621
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 625..634
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 636..643
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 680..686
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 691..694
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 700..704
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 710..717
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 724..729
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 733..736
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 739..746
FT /evidence="ECO:0007829|PDB:5E1R"
FT HELIX 750..757
FT /evidence="ECO:0007829|PDB:5E1R"
FT STRAND 764..769
FT /evidence="ECO:0007829|PDB:5E1R"
SQ SEQUENCE 792 AA; 95169 MW; BF43529DE5DB425A CRC64;
MVTKAKIPLF LFLSALFLAL VCSSLALETE DLSNELNPHH DPESHRWEFQ QCQERCQHEE
RGQRQAQQCQ RRCEEQLRER EREREREEIV DPREPRKQYE QCRETCEKQD PRQQPQCERR
CERQFQEQQE RERRERRRGR DDDDKENPRD PREQYRQCEE HCRRQGQGQR QQQQCQSRCE
ERFEEEQRRQ EERERRRGRD NDDEENPRDP REQYRQCQEH CRRQGQGQRQ QQQCQSRCEE
RLEEEQRKQE ERERRRGRDE DDQNPRDPEQ RYEQCQQQCE RQRRGQEQQL CRRRCEQQRQ
QEERERQRGR DRQDPQQQYH RCQRRCQTQE QSPERQRQCQ QRCERQYKEQ QGREWGPDQA
SPRRESRGRE EEQQRHNPYY FHSQGLRSRH ESGEGEVKYL ERFTERTELL RGIENYRVVI
LEANPNTFVL PYHKDAESVI VVTRGRATLT FVSQERRESF NLEYGDVIRV PAGATEYVIN
QDSNERLEMV KLLQPVNNPG QFREYYAAGA QSTESYLRVF SNDILVAALN TPRDRLERFF
DQQEQREGVI IRASQEKLRA LSQHAMSAGQ RPWGRRSSGG PISLKSQRSS YSNQFGQFFE
ACPEEHRQLQ EMDVLVNYAE IKRGAMMVPH YNSKATVVVY VVEGTGRFEM ACPHDVSSQS
YEYKGRREQE EEESSTGQFQ KVTARLARGD IFVIPAGHPI AITASQNENL RLVGFGINGK
NNQRNFLAGQ NNIINQLERE AKELSFNMPR EEIEEIFERQ VESYFVPMER QSRRGQGRDH
PLASILDFAG FF
