ID   CONG7_ARAHY             Reviewed;         172 AA.
AC   Q6PSU2; A1DZE8; A5Z1R1; C0LJJ1; Q647H0; Q6PSU1; Q7Y1C0; Q84TU1; Q8GV20;
AC   Q941R0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   02-SEP-2026, entry version 77.
DE   RecName: Full=Conglutin-7 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
DE   AltName: Full=2S protein 1 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
DE   AltName: Full=Seed storage protein SSP1 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
DE   AltName: Full=Seed storage protein SSP2 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
DE   AltName: Allergen=Ara h 2;
DE   Flags: Precursor;
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAN77576.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 22-31,
RP   AND MASS SPECTROMETRY.
RX   PubMed=12759484; DOI=10.1159/000070429;
RA   Chatel J.-M., Bernard H., Orson F.M.;
RT   "Isolation and characterization of two complete Ara h 2 isoforms cDNA.";
RL   Int. Arch. Allergy Immunol. 131:14-18(2003).
RN   [2] {ECO:0000312|EMBL:AAT00598.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.2};
RC   TISSUE=Cotyledon {ECO:0000269|Ref.2};
RX   AGRICOLA=IND43739496; DOI=10.1016/j.plantsci.2005.04.010;
RA   Yan Y.-S., Lin X.-D., Zhang Y.-S., Wang L., Wu K., Huang S.-Z.;
RT   "Isolation of peanut genes encoding arachins and conglutins by expressed
RT   sequence tags.";
RL   Plant Sci. 169:439-445(2005).
RN   [3] {ECO:0000312|EMBL:ABQ96215.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. F78-1339 {ECO:0000269|PubMed:16614814};
RX   PubMed=16614814; DOI=10.1007/s00438-006-0114-z;
RA   Ramos M.L., Fleming G., Chu Y., Akiyama Y., Gallo M., Ozias-Akins P.;
RT   "Chromosomal and phylogenetic context for conglutin genes in Arachis based
RT   on genomic sequence.";
RL   Mol. Genet. Genomics 275:578-592(2006).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.4};
RA   Yan Y.-S., Wang L., Liao B., Li H., Lin X.-D., Huang S.-Z.;
RT   "cDNA cloning of peanut seed storage protein.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.5};
RA   Fu G., Yan Y.-S., Wang L., Zhong Y., Huang S.-Z.;
RT   "Isolation of peanut genes encoding seed storage proteins and stress
RT   proteins from developing cotyledons by expressed sequence tags.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.6};
RA   Li C., Fu G., Zhong Y., Yan Y., Wang L., Huang S.;
RT   "Cloning and characterization of four genes encoding peanut seed
RT   oleosins.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Radosavljevic J., Dobrijevic D., Blanusa M., Jadranin M.,
RA   Cirkovic Velickovic T.;
RT   "Proteolytical processing of Ara h 2 into mature form.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000312|EMBL:AAK96887.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RC   STRAIN=cv. F78-1339 {ECO:0000269|PubMed:11295663};
RC   TISSUE=Seed {ECO:0000269|PubMed:11295663};
RX   PubMed=11295663; DOI=10.1067/mai.2001.113522;
RA   Viquez O.M., Summer C.G., Dodo H.W.;
RT   "Isolation and molecular characterization of the first genomic clone of a
RT   major peanut allergen, Ara h 2.";
RL   J. Allergy Clin. Immunol. 107:713-717(2001).
RN   [9] {ECO:0000305, ECO:0000312|EMBL:AAO61750.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-168 (ISOFORMS 1 AND 3), TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. FL435 {ECO:0000269|PubMed:12582692};
RC   TISSUE=Seed {ECO:0000312|EMBL:AAO61750.1};
RX   PubMed=12582692; DOI=10.1007/s001220100763;
RA   Paik-Ro O.G., Seib J.C., Smith R.L.;
RT   "Seed-specific, developmentally regulated genes of peanut.";
RL   Theor. Appl. Genet. 104:236-240(2002).
RN   [10] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-172 (ISOFORM 1).
RA   Becker W.-M., Suhr M., Lindner B., Wicklein D., Lepp U.;
RT   "Re-investigation of the major peanut allergen Arah2 on the molecular
RT   level.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   PROTEIN SEQUENCE OF 22-172 (ISOFORMS 1; 2; 3 AND 4), HYDROXYLATION AT
RP   PRO-67; PRO-74 AND PRO-86, DISULFIDE BONDS, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19937656; DOI=10.1002/pro.295;
RA   Li J., Shefcheck K., Callahan J., Fenselau C.;
RT   "Primary sequence and site-selective hydroxylation of prolines in isoforms
RT   of a major peanut allergen protein Ara h 2.";
RL   Protein Sci. 19:174-182(2010).
RN   [12] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
RP   PROTEIN SEQUENCE OF 22-33; 117-131; 147-155 AND 160-169, AND REPRESSION BY
RP   WATER STRESS.
RC   STRAIN=cv. M13 {ECO:0000269|Ref.12}; TISSUE=Seed {ECO:0000269|Ref.12};
RA   Katam R., Vasanthaiah H.K.N., Basha S.M., McClung S.;
RT   "Suppression of seed storage proteins upon water stress in Arachis hypogea
RT   var. M-13 seeds.";
RL   Submitted (MAR-2007) to UniProtKB.
RN   [13] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 26-31 AND 93-99, ALLERGEN, AND RESISTANCE TO HEAT AND
RP   PROTEOLYSIS.
RX   PubMed=16372900; DOI=10.1042/bj20051728;
RA   Lehmann K., Schweimer K., Reese G., Randow S., Suhr M., Becker W.-M.,
RA   Vieths S., Roesch P.;
RT   "Structure and stability of 2S albumin-type peanut allergens: implications
RT   for the severity of peanut allergic reactions.";
RL   Biochem. J. 395:463-472(2006).
RN   [14] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=12847498; DOI=10.1067/mai.2003.1551;
RA   Maleki S.J., Viquez O.M., Jacks T., Dodo H.W., Champagne E.T., Chung S.-Y.,
RA   Landry S.J.;
RT   "The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and
RT   roasting enhances this function.";
RL   J. Allergy Clin. Immunol. 112:190-195(2003).
CC   -!- FUNCTION: Weak inhibitor of trypsin. {ECO:0000269|PubMed:12847498}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. {ECO:0000269|PubMed:16372900};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=P1;
CC         IsoId=Q6PSU2-1; Sequence=Displayed;
CC       Name=2; Synonyms=P2;
CC         IsoId=Q6PSU2-2; Sequence=VSP_038916;
CC       Name=3; Synonyms=P3;
CC         IsoId=Q6PSU2-3; Sequence=VSP_038917;
CC       Name=4; Synonyms=P4;
CC         IsoId=Q6PSU2-4; Sequence=VSP_038916, VSP_038917;
CC   -!- TISSUE SPECIFICITY: Expressed in seeds, not expressed in leaves, roots
CC       and pegs. {ECO:0000269|PubMed:12582692}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at very low levels in immature seeds and
CC       at high levels from 40-75 days after pollination. Expression decreases
CC       after 75 days after pollination. {ECO:0000269|PubMed:12582692}.
CC   -!- INDUCTION: Repressed by water stress. {ECO:0000269|Ref.12}.
CC   -!- PTM: The hydroxyproline modifications determined by mass spectrometry
CC       are probably 4-hydroxyproline as determined for other extracellular
CC       plant proteins. {ECO:0000269|PubMed:19937656}.
CC   -!- MASS SPECTROMETRY: Mass=18050; Method=MALDI; Note=Isoform 1.;
CC       Evidence={ECO:0000269|PubMed:12759484};
CC   -!- MASS SPECTROMETRY: Mass=16670; Method=MALDI; Note=Isoform 3.;
CC       Evidence={ECO:0000269|PubMed:12759484};
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:16372900}.
CC   -!- MISCELLANEOUS: Resistant to proteolysis. {ECO:0000269|PubMed:16372900}.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT00598.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAT00599.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAU21494.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AY158467; AAN77576.1; -; mRNA.
DR   EMBL; AY581853; AAT00598.1; ALT_INIT; mRNA.
DR   EMBL; AY722689; AAU21494.1; ALT_INIT; mRNA.
DR   EMBL; EF609644; ABQ96215.1; -; Genomic_DNA.
DR   EMBL; AY581854; AAT00599.1; ALT_INIT; mRNA.
DR   EMBL; EF080817; ABL14268.1; -; mRNA.
DR   EMBL; EF695402; ABS28872.1; -; Genomic_DNA.
DR   EMBL; FJ713110; ACN62248.1; -; Genomic_DNA.
DR   EMBL; AY007229; AAK96887.1; -; Genomic_DNA.
DR   EMBL; AF366560; AAO61750.1; -; mRNA.
DR   EMBL; AY117434; AAM78596.1; -; mRNA.
DR   RefSeq; NP_001392340.1; NM_001405411.1. [Q6PSU2-1]
DR   PDB; 8SHW; X-ray; 1.95 A; B/Q=57-70.
DR   PDB; 8SJ6; X-ray; 3.97 A; Q=26-172.
DR   PDB; 9CMC; X-ray; 2.95 A; E/J/O/T=26-172.
DR   AlphaFoldDB; Q6PSU2; -.
DR   SMR; Q6PSU2; -.
DR   Allergome; 1081; Ara h 2.0101.
DR   Allergome; 1082; Ara h 2.0201.
DR   Allergome; 51; Ara h 2.
DR   ABCD; Q6PSU2; 8 sequenced antibodies.
DR   EnsemblPlants; arahy.Tifrunner.gnm2.ann2.Ah18g135300.1; arahy.Tifrunner.gnm2.ann2.Ah18g135300.1-CDS-1; arahy.Tifrunner.gnm2.ann2.Ah18g135300.
DR   GeneID; 112771110; -.
DR   Gramene; arahy.Tifrunner.gnm2.ann2.Ah18g135300.1; arahy.Tifrunner.gnm2.ann2.Ah18g135300.1-CDS-1; arahy.Tifrunner.gnm2.ann2.Ah18g135300.
DR   KEGG; ahf:112771110; -.
DR   OrthoDB; 1424936at2759; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:InterPro.
DR   Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 1.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR000617; Napin/2SS/CON.
DR   PANTHER; PTHR35496; 2S SEED STORAGE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR35496:SF20; 2S SEED STORAGE PROTEIN 1-RELATED; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
DR   PDBsum; 8SHW; -.
DR   PDBsum; 8SJ6; -.
DR   PDBsum; 9CMC; -.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; IgE-binding protein; Protease inhibitor;
KW   Seed storage protein; Serine protease inhibitor; Signal; Storage protein.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:12759484, ECO:0000269|Ref.12"
FT   CHAIN           22..172
FT                   /note="Conglutin-7"
FT                   /evidence="ECO:0000269|PubMed:12759484, ECO:0000269|Ref.12"
FT                   /id="PRO_0000370687"
FT   REGION          54..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..76
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         67
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:19937656"
FT   MOD_RES         74
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:19937656"
FT   MOD_RES         86
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:19937656"
FT   DISULFID        33..116
FT                   /evidence="ECO:0000269|PubMed:19937656"
FT   DISULFID        45..103
FT                   /note="Or C-45 with C-104"
FT                   /evidence="ECO:0000269|PubMed:19937656"
FT   DISULFID        104..152
FT                   /note="Or C-103 with C-152"
FT                   /evidence="ECO:0000269|PubMed:19937656"
FT   DISULFID        118..160
FT                   /evidence="ECO:0000269|PubMed:19937656"
FT   VAR_SEQ         76..87
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12759484, ECO:0000303|Ref.2,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_038916"
FT   VAR_SEQ         170..172
FT                   /note="DRY -> D (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12582692"
FT                   /id="VSP_038917"
FT   CONFLICT        2..3
FT                   /note="Missing (in Ref. 7; ACN62248)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="L -> P (in Ref. 10; AAM78596)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27
FT                   /note="L -> F (in Ref. 4; AAT00599)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="G -> E (in Ref. 2; AAU21494, 4; AAT00599, 7;
FT                   ACN62248 and 8; AAK96887)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65..78
FT                   /note="Missing (in Ref. 5; ABL14268)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="E -> D (in Ref. 2; AAU21494, 4; AAT00599, 7;
FT                   ACN62248 and 8; AAK96887)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..35
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           43..54
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           98..107
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           114..128
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           135..146
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           148..151
FT                   /evidence="ECO:0007829|PDB:9CMC"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:9CMC"
SQ   SEQUENCE   172 AA;  20114 MW;  B8BB91C8D8C143AB CRC64;
     MAKLTILVAL ALFLLAAHAS ARQQWELQGD RRCQSQLERA NLRPCEQHLM QKIQRDEDSY
     GRDPYSPSQD PYSPSQDPDR RDPYSPSPYD RRGAGSSQHQ ERCCNELNEF ENNQRCMCEA
     LQQIMENQSD RLQGRQQEQQ FKRELRNLPQ QCGLRAPQRC DLEVESGGRD RY
//