CONG7_ARAHY
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 25-MAY-2022, entry version 66.
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};
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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 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 GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.110.10; -; 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; PTHR35496; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Allergen; Alternative splicing; Direct protein sequencing; Disulfide bond;
KW 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 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"
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
