CONG_ARAHY
ID CONG_ARAHY Reviewed; 145 AA.
AC Q647G9; Q5I1E9; Q5I6T1; Q8W251; Q9SQG5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Conglutin;
DE AltName: Allergen=Ara h 6;
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:0000312|EMBL:AAU21495.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.1};
RC TISSUE=Cotyledon {ECO:0000269|Ref.1};
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAL37561.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-145, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. FL435 {ECO:0000269|PubMed:12582692};
RC TISSUE=Seed {ECO:0000269|PubMed:12582692};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAD56337.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-145, AND ALLERGEN.
RC STRAIN=cv. Virginia {ECO:0000269|PubMed:10474031};
RC TISSUE=Seed {ECO:0000312|EMBL:AAD56337.1};
RX PubMed=10474031; DOI=10.1159/000024203;
RA Kleber-Janke T., Crameri R., Appenzeller U., Schlaak M., Becker W.-M.;
RT "Selective cloning of peanut allergens, including profilin and 2S albumins,
RT by phage display technology.";
RL Int. Arch. Allergy Immunol. 119:265-274(1999).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAW34231.1}
RP PROTEIN SEQUENCE OF 22-145, REPRESSION BY WATER STRESS, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. M13 {ECO:0000269|Ref.4}; TISSUE=Seed {ECO:0000269|Ref.4};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAW34231.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-145.
RA Schocker F., Suhr M., Becker W.-M.;
RT "Epitope mapping of Ara h 6.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP STRUCTURE BY NMR OF 22-145, PARTIAL PROTEIN SEQUENCE, ALLERGEN, AND
RP DISULFIDE BONDS.
RC TISSUE=Seed;
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).
CC -!- TISSUE SPECIFICITY: Expressed in seeds. Not expressed in roots, pegs
CC (budding ovaries) or leaves. {ECO:0000269|PubMed:12582692}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the later, cell expansion, stages of
CC seed development. {ECO:0000269|PubMed:12582692}.
CC -!- INDUCTION: Repressed by water stress. {ECO:0000269|Ref.4}.
CC -!- MASS SPECTROMETRY: Mass=17479; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.4};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:10474031, ECO:0000269|PubMed:16372900}.
CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC {ECO:0000255}.
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DR EMBL; AY722690; AAU21495.1; -; mRNA.
DR EMBL; AY848699; AAW56068.1; -; mRNA.
DR EMBL; AY849314; AAW32558.1; -; mRNA.
DR EMBL; AF366561; AAL37561.1; -; mRNA.
DR EMBL; AF092846; AAD56337.1; -; mRNA.
DR EMBL; AY871100; AAW34231.1; -; Genomic_DNA.
DR PDB; 1W2Q; NMR; -; A=22-145.
DR PDBsum; 1W2Q; -.
DR AlphaFoldDB; Q647G9; -.
DR SMR; Q647G9; -.
DR Allergome; 3098; Ara h 6.0101.
DR Allergome; 55; Ara h 6.
DR ABCD; Q647G9; 3 sequenced antibodies.
DR EvolutionaryTrace; Q647G9; -.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR DisProt; DP00942; -.
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 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW IgE-binding protein; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..145
FT /note="Conglutin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272966"
FT DISULFID 35..92
FT /evidence="ECO:0000269|PubMed:16372900"
FT DISULFID 47..79
FT /evidence="ECO:0000269|PubMed:16372900"
FT DISULFID 80..128
FT /evidence="ECO:0000269|PubMed:16372900"
FT DISULFID 94..136
FT /evidence="ECO:0000269|PubMed:16372900"
FT DISULFID 105..145
FT /evidence="ECO:0000269|PubMed:16372900"
FT CONFLICT 41
FT /note="R -> G (in Ref. 3; AAD56337)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..68
FT /note="DIR -> NFG (in Ref. 3; AAD56337)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..85
FT /note="NE -> DQ (in Ref. 1; AAW56068 and 2; AAL37561)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="Q -> E (in Ref. 1; AAW56068 and 2; AAL37561)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="R -> G (in Ref. 5; AAW34231)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="R -> G (in Ref. 3; AAD56337)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="Q -> H (in Ref. 3; AAD56337)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="N -> S (in Ref. 5; AAW34231)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="R -> G (in Ref. 3; AAD56337)"
FT /evidence="ECO:0000305"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:1W2Q"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1W2Q"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1W2Q"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1W2Q"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:1W2Q"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:1W2Q"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:1W2Q"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:1W2Q"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1W2Q"
SQ SEQUENCE 145 AA; 16920 MW; FA3D6FC41CB6267D CRC64;
MAKSTILVAL LALVLVAHAS AMRRERGRQG DSSSCERQVD RVNLKPCEQH IMQRIMGEQE
QYDSYDIRST RSSDQQQRCC DELNEMENTQ RCMCEALQQI MENQCDRLQD RQMVQQFKRE
LMNLPQQCNF RAPQRCDLDV SGGRC
