VCL_PINKO
ID VCL_PINKO Reviewed; 463 AA.
AC V9VGU0; W5IDC2;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Vicilin Pin k 2.0101 {ECO:0000305};
DE AltName: Full=7S globulin {ECO:0000303|PubMed:18690685};
DE AltName: Full=7S seed storage protein {ECO:0000303|PubMed:24328105};
DE AltName: Full=Allergen Pin k 2 {ECO:0000303|PubMed:29195881};
DE AltName: Full=Vicilin-type seed storage protein {ECO:0000303|PubMed:18084088, ECO:0000303|PubMed:18690685};
DE AltName: Allergen=Pin k 2.0101 {ECO:0000305};
DE Flags: Precursor;
OS Pinus koraiensis (Korean pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Strobus.
OX NCBI_TaxID=88728 {ECO:0000312|EMBL:AHC94918.1};
RN [1] {ECO:0000312|EMBL:AHC94918.1, ECO:0007744|PDB:4LEJ}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF
RP 57-463 IN COMPLEX WITH COPPER, AND SUBUNIT.
RC TISSUE=Cone {ECO:0000303|PubMed:24328105};
RX PubMed=24328105; DOI=10.1021/jf4039887;
RA Jin T., Wang Y., Chen Y.W., Fu T.J., Kothary M.H., McHugh T.H., Zhang Y.;
RT "Crystal structure of Korean pine (Pinus koraiensis) 7S seed storage
RT protein with copper ligands.";
RL J. Agric. Food Chem. 62:222-228(2014).
RN [2]
RP PROTEIN SEQUENCE OF 56-72; 261-271 AND 354-371, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE,
RP AND CIRCULAR DICHROISM ANALYSIS.
RC TISSUE=Seed {ECO:0000303|PubMed:18690685};
RX PubMed=18690685; DOI=10.1021/jf801138q;
RA Jin T., Albillos S.M., Chen Y.W., Kothary M.H., Fu T.J., Zhang Y.Z.;
RT "Purification and characterization of the 7S vicilin from Korean pine
RT (Pinus koraiensis).";
RL J. Agric. Food Chem. 56:8159-8165(2008).
RN [3]
RP CRYSTALLIZATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18084088; DOI=10.1107/s1744309107054310;
RA Jin T., Fu T.J., Kothary M.H., Howard A., Zhang Y.Z.;
RT "Crystallization and initial crystallographic characterization of a
RT vicilin-type seed storage protein from Pinus koraiensis.";
RL Acta Crystallogr. F 63:1041-1043(2007).
RN [4]
RP SUBUNIT, AND ALLERGEN.
RX PubMed=29195881; DOI=10.1016/j.foodres.2016.10.043;
RA Zhang Y., Du W.X., Fan Y., Yi J., Lyu S.C., Nadeau K.C., McHugh T.H.;
RT "Identification, characterization, and initial epitope mapping of pine nut
RT allergen Pin k 2.";
RL Food Res. Intern. 90:268-274(2016).
CC -!- FUNCTION: Seed storage protein. {ECO:0000305|PubMed:18084088,
CC ECO:0000305|PubMed:18690685}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Stable up to 80 degrees Celsius. {ECO:0000269|PubMed:18690685};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:24328105,
CC ECO:0000269|PubMed:29195881}.
CC -!- TISSUE SPECIFICITY: Expressed in seed. {ECO:0000269|PubMed:18084088,
CC ECO:0000269|PubMed:18690685}.
CC -!- DEVELOPMENTAL STAGE: During seed development.
CC {ECO:0000269|PubMed:18084088, ECO:0000269|PubMed:18690685}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 29% of
CC the 14 patients tested allergic to pine nuts.
CC {ECO:0000269|PubMed:29195881}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KF530834; AHC94918.1; -; mRNA.
DR PDB; 4LEJ; X-ray; 2.40 A; A=57-463.
DR PDBsum; 4LEJ; -.
DR AlphaFoldDB; V9VGU0; -.
DR SMR; V9VGU0; -.
DR Allergome; 10723; Pin k 2.
DR Allergome; 11977; Pin k 2.0101.
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; IC: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; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Copper; Direct protein sequencing; Glycoprotein;
KW Metal-binding; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..463
FT /note="Vicilin Pin k 2.0101"
FT /evidence="ECO:0000255"
FT /id="PRO_5004783281"
FT DOMAIN 74..226
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 268..435
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 40..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 338
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:24328105,
FT ECO:0007744|PDB:4LEJ"
FT BINDING 340
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:24328105,
FT ECO:0007744|PDB:4LEJ"
FT BINDING 379
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:24328105,
FT ECO:0007744|PDB:4LEJ"
FT SITE 55..56
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:18690685"
FT SITE 260..261
FT /note="Cleavage; partial"
FT /evidence="ECO:0000269|PubMed:18690685"
FT SITE 353..354
FT /note="Cleavage; partial"
FT /evidence="ECO:0000269|PubMed:18690685"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 57
FT /note="G -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="E -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="R -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="D -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 120..132
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:4LEJ"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:4LEJ"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:4LEJ"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4LEJ"
SQ SEQUENCE 463 AA; 52131 MW; 4FF67746706ED571 CRC64;
MAFVSLLTIL LAISSSSVAL TEPVASMADQ GVFPEQHGRG HHGVFPEEHG RGHHRGGREE
EREENPYVFH SDRFRIRASS EAGEIRALPN FGEVSELLEG ISRYRVTCIE MKPNTVMLPH
YIDAKWILYV TGGRGYIAYV QQNELVKRKL EEGDVFGVPS GHTFYLVNND DHNSLRIASL
LRTESTMRGE YEPFYVAGGR NPETVYSAFS DDVLEAAFNT DVQKLEHIFG AHRRGVIFYA
NEEQIREMMR RGGFSAESTS ASEQPKPFNL RNQKPDFEND NGRFTRAGPK DNPFLDSVDV
TVGFGVLNPG TMTAPSHNTK ATSIAIVMEG EGRIEMACPH LGQEHGWSSP RERGHQDINY
ERVRARLRTG TVYVVPAGHP ITEIASTNGR LEILWFDINT SGNEREFLAG KNNVLQTLEK
EVRHLSFNIP RGEEIEEVLQ AQKDQVILRG PQRQRRDEPR SSS
