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Conglutin-7 (2S protein 1) (Seed storage protein SSP1) (Seed storage protein SSP2) (allergen Ara h 2)

 CONG7_ARAHY             Reviewed;         172 AA.
Q6PSU2; A1DZE8; A5Z1R1; C0LJJ1; Q647H0; Q6PSU1; Q7Y1C0; Q84TU1;
Q8GV20; Q941R0;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 2.
25-OCT-2017, entry version 54.
RecName: Full=Conglutin-7 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
AltName: Full=2S protein 1 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
AltName: Full=Seed storage protein SSP1 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
AltName: Full=Seed storage protein SSP2 {ECO:0000303|PubMed:16372900, ECO:0000312|EMBL:AAT00598.1};
AltName: Allergen=Ara h 2;
Flags: Precursor;
Arachis hypogaea (Peanut).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Dalbergieae; Arachis.
NCBI_TaxID=3818;
[1] {ECO:0000305, ECO:0000312|EMBL:AAN77576.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
22-31, AND MASS SPECTROMETRY.
PubMed=12759484; DOI=10.1159/000070429;
Chatel J.-M., Bernard H., Orson F.M.;
"Isolation and characterization of two complete Ara h 2 isoforms
cDNA.";
Int. Arch. Allergy Immunol. 131:14-18(2003).
[2] {ECO:0000312|EMBL:AAT00598.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.2};
TISSUE=Cotyledon {ECO:0000269|Ref.2};
AGRICOLA=IND43739496; DOI=10.1016/j.plantsci.2005.04.010;
Yan Y.-S., Lin X.-D., Zhang Y.-S., Wang L., Wu K., Huang S.-Z.;
"Isolation of peanut genes encoding arachins and conglutins by
expressed sequence tags.";
Plant Sci. 169:439-445(2005).
[3] {ECO:0000312|EMBL:ABQ96215.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. F78-1339 {ECO:0000269|PubMed:16614814};
PubMed=16614814; DOI=10.1007/s00438-006-0114-z;
Ramos M.L., Fleming G., Chu Y., Akiyama Y., Gallo M., Ozias-Akins P.;
"Chromosomal and phylogenetic context for conglutin genes in Arachis
based on genomic sequence.";
Mol. Genet. Genomics 275:578-592(2006).
[4] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.4};
Yan Y.-S., Wang L., Liao B., Li H., Lin X.-D., Huang S.-Z.;
"cDNA cloning of peanut seed storage protein.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.5};
Fu G., Yan Y.-S., Wang L., Zhong Y., Huang S.-Z.;
"Isolation of peanut genes encoding seed storage proteins and stress
proteins from developing cotyledons by expressed sequence tags.";
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.6};
Li C., Fu G., Zhong Y., Yan Y., Wang L., Huang S.;
"Cloning and characterization of four genes encoding peanut seed
oleosins.";
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Radosavljevic J., Dobrijevic D., Blanusa M., Jadranin M.,
Cirkovic Velickovic T.;
"Proteolytical processing of Ara h 2 into mature form.";
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000312|EMBL:AAK96887.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
STRAIN=cv. F78-1339 {ECO:0000269|PubMed:11295663};
TISSUE=Seed {ECO:0000269|PubMed:11295663};
PubMed=11295663; DOI=10.1067/mai.2001.113522;
Viquez O.M., Summer C.G., Dodo H.W.;
"Isolation and molecular characterization of the first genomic clone
of a major peanut allergen, Ara h 2.";
J. Allergy Clin. Immunol. 107:713-717(2001).
[9] {ECO:0000305, ECO:0000312|EMBL:AAO61750.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 3-168 (ISOFORMS 1 AND 3), TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=cv. FL435 {ECO:0000269|PubMed:12582692};
TISSUE=Seed {ECO:0000312|EMBL:AAO61750.1};
PubMed=12582692; DOI=10.1007/s001220100763;
Paik-Ro O.G., Seib J.C., Smith R.L.;
"Seed-specific, developmentally regulated genes of peanut.";
Theor. Appl. Genet. 104:236-240(2002).
[10] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 4-172 (ISOFORM 1).
Becker W.-M., Suhr M., Lindner B., Wicklein D., Lepp U.;
"Re-investigation of the major peanut allergen Arah2 on the molecular
level.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 22-172 (ISOFORMS 1; 2; 3 AND 4), HYDROXYLATION AT
PRO-67; PRO-74 AND PRO-86, DISULFIDE BONDS, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=19937656; DOI=10.1002/pro.295;
Li J., Shefcheck K., Callahan J., Fenselau C.;
"Primary sequence and site-selective hydroxylation of prolines in
isoforms of a major peanut allergen protein Ara h 2.";
Protein Sci. 19:174-182(2010).
[12] {ECO:0000305, ECO:0000312|EMBL:AAT00599.1}
PROTEIN SEQUENCE OF 22-33; 117-131; 147-155 AND 160-169, AND
REPRESSION BY WATER STRESS.
STRAIN=cv. M13 {ECO:0000269|Ref.12}; TISSUE=Seed {ECO:0000269|Ref.12};
Katam R., Vasanthaiah H.K.N., Basha S.M., McClung S.;
"Suppression of seed storage proteins upon water stress in Arachis
hypogea var. M-13 seeds.";
Submitted (MAR-2007) to UniProtKB.
[13] {ECO:0000305}
PROTEIN SEQUENCE OF 26-31 AND 93-99, ALLERGEN, AND RESISTANCE TO HEAT
AND PROTEOLYSIS.
PubMed=16372900; DOI=10.1042/BJ20051728;
Lehmann K., Schweimer K., Reese G., Randow S., Suhr M., Becker W.-M.,
Vieths S., Roesch P.;
"Structure and stability of 2S albumin-type peanut allergens:
implications for the severity of peanut allergic reactions.";
Biochem. J. 395:463-472(2006).
[14] {ECO:0000305}
FUNCTION.
PubMed=12847498; DOI=10.1067/mai.2003.1551;
Maleki S.J., Viquez O.M., Jacks T., Dodo H.W., Champagne E.T.,
Chung S.-Y., Landry S.J.;
"The major peanut allergen, Ara h 2, functions as a trypsin inhibitor,
and roasting enhances this function.";
J. Allergy Clin. Immunol. 112:190-195(2003).
-!- FUNCTION: Weak inhibitor of trypsin.
{ECO:0000269|PubMed:12847498}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Thermostable. {ECO:0000269|PubMed:16372900};
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=P1;
IsoId=Q6PSU2-1; Sequence=Displayed;
Name=2; Synonyms=P2;
IsoId=Q6PSU2-2; Sequence=VSP_038916;
Name=3; Synonyms=P3;
IsoId=Q6PSU2-3; Sequence=VSP_038917;
Name=4; Synonyms=P4;
IsoId=Q6PSU2-4; Sequence=VSP_038916, VSP_038917;
-!- TISSUE SPECIFICITY: Expressed in seeds, not expressed in leaves,
roots and pegs. {ECO:0000269|PubMed:12582692}.
-!- DEVELOPMENTAL STAGE: Expressed at very low levels in immature
seeds and at high levels from 40-75 days after pollination.
Expression decreases after 75 days after pollination.
{ECO:0000269|PubMed:12582692}.
-!- INDUCTION: Repressed by water stress. {ECO:0000269|Ref.12}.
-!- PTM: The hydroxyproline modifications determined by mass
spectrometry are probably 4-hydroxyproline as determined for other
extracellular plant proteins. {ECO:0000269|PubMed:19937656}.
-!- MASS SPECTROMETRY: Mass=18050; Method=MALDI; Range=22-172;
Note=Isoform 1.; Evidence={ECO:0000269|PubMed:12759484};
-!- MASS SPECTROMETRY: Mass=16670; Method=MALDI; Range=22-172;
Note=Isoform 3.; Evidence={ECO:0000269|PubMed:12759484};
-!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
{ECO:0000269|PubMed:16372900}.
-!- MISCELLANEOUS: Resistant to proteolysis.
{ECO:0000269|PubMed:16372900}.
-!- SIMILARITY: Belongs to the 2S seed storage albumins family.
{ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAT00598.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAT00599.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAU21494.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY158467; AAN77576.1; -; mRNA.
EMBL; AY581853; AAT00598.1; ALT_INIT; mRNA.
EMBL; AY722689; AAU21494.1; ALT_INIT; mRNA.
EMBL; EF609644; ABQ96215.1; -; Genomic_DNA.
EMBL; AY581854; AAT00599.1; ALT_INIT; mRNA.
EMBL; EF080817; ABL14268.1; -; mRNA.
EMBL; EF695402; ABS28872.1; -; Genomic_DNA.
EMBL; FJ713110; ACN62248.1; -; Genomic_DNA.
EMBL; AY007229; AAK96887.1; -; Genomic_DNA.
EMBL; AF366560; AAO61750.1; -; mRNA.
EMBL; AY117434; AAM78596.1; -; mRNA.
ProteinModelPortal; Q6PSU2; -.
SMR; Q6PSU2; -.
Allergome; 1081; Ara h 2.0101.
Allergome; 1082; Ara h 2.0201.
Allergome; 51; Ara h 2.
GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
Pfam; PF00234; Tryp_alpha_amyl; 1.
SMART; SM00499; AAI; 1.
SUPFAM; SSF47699; SSF47699; 1.
1: Evidence at protein level;
Allergen; Alternative splicing; Direct protein sequencing;
Disulfide bond; Hydroxylation; IgE-binding protein;
Protease inhibitor; Seed storage protein; Serine protease inhibitor;
Signal; Storage protein.
SIGNAL 1 21 {ECO:0000269|PubMed:12759484,
ECO:0000269|Ref.12}.
CHAIN 22 172 Conglutin-7.
{ECO:0000269|PubMed:12759484,
ECO:0000269|Ref.12}.
/FTId=PRO_0000370687.
MOD_RES 67 67 4-hydroxyproline.
{ECO:0000269|PubMed:19937656}.
MOD_RES 74 74 4-hydroxyproline.
{ECO:0000269|PubMed:19937656}.
MOD_RES 86 86 4-hydroxyproline.
{ECO:0000269|PubMed:19937656}.
DISULFID 33 116 {ECO:0000269|PubMed:19937656}.
DISULFID 45 103 Or C-45 with C-104.
{ECO:0000269|PubMed:19937656}.
DISULFID 104 152 Or C-103 with C-152.
{ECO:0000269|PubMed:19937656}.
DISULFID 118 160 {ECO:0000269|PubMed:19937656}.
VAR_SEQ 76 87 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:12759484,
ECO:0000303|Ref.2, ECO:0000303|Ref.4}.
/FTId=VSP_038916.
VAR_SEQ 170 172 DRY -> D (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:12582692}.
/FTId=VSP_038917.
CONFLICT 2 3 Missing (in Ref. 7; ACN62248).
{ECO:0000305}.
CONFLICT 10 10 L -> P (in Ref. 10; AAM78596).
{ECO:0000305}.
CONFLICT 27 27 L -> F (in Ref. 4; AAT00599).
{ECO:0000305}.
CONFLICT 61 61 G -> E (in Ref. 2; AAU21494, 4; AAT00599,
7; ACN62248 and 8; AAK96887).
{ECO:0000305}.
CONFLICT 65 78 Missing (in Ref. 5; ABL14268).
{ECO:0000305}.
CONFLICT 163 163 E -> D (in Ref. 2; AAU21494, 4; AAT00599,
7; ACN62248 and 8; AAK96887).
{ECO:0000305}.
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


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