ALL12_ARAHY
ID ALL12_ARAHY Reviewed; 626 AA.
AC P43238; Q547W5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Allergen Ara h 1, clone P41B;
DE AltName: Full=Allergen Ara h I;
DE AltName: Allergen=Ara h 1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC STRAIN=cv. Florunner;
RX PubMed=7560062; DOI=10.1172/jci118216;
RA Burks A.W., Cockrell G., Stanley J.S., Helm R.M., Bannon G.A.;
RT "Recombinant peanut allergen Ara h I expression and IgE binding in patients
RT with peanut hypersensitivity.";
RL J. Clin. Invest. 96:1715-1721(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. F78-1339;
RX PubMed=14597159; DOI=10.1016/j.molimm.2003.09.002;
RA Viquez O.M., Konan K.N., Dodo H.W.;
RT "Structure and organization of the genomic clone of a major peanut allergen
RT gene, Ara h 1.";
RL Mol. Immunol. 40:565-571(2003).
RN [3]
RP PROTEIN SEQUENCE OF 96-108; 153-165; 171-181; 203-277; 288-351; 357-367;
RP 387-471; 478-498 AND 541-572, AND REPRESSION BY WATER STRESS.
RC STRAIN=cv. M13; TISSUE=Seed;
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 [4]
RP GLYCOSYLATION AT ASN-521.
RX PubMed=10998264; DOI=10.1006/abio.2000.4737;
RA Kolarich D., Altmann F.;
RT "N-glycan analysis by matrix-assisted laser desorption/ionization mass
RT spectrometry of electrophoretically separated nonmammalian proteins:
RT application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1.";
RL Anal. Biochem. 285:64-75(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 170-586.
RX PubMed=21917921; DOI=10.1074/jbc.m111.270132;
RA Chruszcz M., Maleki S.J., Majorek K.A., Demas M., Bublin M., Solberg R.,
RA Hurlburt B.K., Ruan S., Mattison C.P., Breiteneder H., Minor W.;
RT "Structural and immunologic characterization of Ara h 1, a major peanut
RT allergen.";
RL J. Biol. Chem. 286:39318-39327(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 170-587.
RX PubMed=21903274; DOI=10.1016/j.molimm.2011.08.004;
RA Cabanos C., Urabe H., Tandang-Silvas M.R., Utsumi S., Mikami B.,
RA Maruyama N.;
RT "Crystal structure of the major peanut allergen Ara h 1.";
RL Mol. Immunol. 49:115-123(2011).
CC -!- INDUCTION: Repressed by water stress. {ECO:0000269|Ref.3}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:7560062}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; L34402; AAB00861.1; -; mRNA.
DR EMBL; AF432231; AAL27476.1; -; Genomic_DNA.
DR PDB; 3S7E; X-ray; 2.71 A; A/B=170-586.
DR PDB; 3S7I; X-ray; 2.35 A; A/B=170-586.
DR PDB; 3SMH; X-ray; 2.43 A; A/B/C/D/E/F=170-587.
DR PDB; 7LXK; NMR; -; A=25-83.
DR PDBsum; 3S7E; -.
DR PDBsum; 3S7I; -.
DR PDBsum; 3SMH; -.
DR PDBsum; 7LXK; -.
DR AlphaFoldDB; P43238; -.
DR SMR; P43238; -.
DR Allergome; 3094; Ara h 1.0101.
DR Allergome; 50; Ara h 1.
DR iPTMnet; P43238; -.
DR PRIDE; P43238; -.
DR EvolutionaryTrace; P43238; -.
DR GO; GO:0019863; F:IgE binding; IDA: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; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Glycoprotein; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..626
FT /note="Allergen Ara h 1, clone P41B"
FT /id="PRO_0000032197"
FT DOMAIN 175..333
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 398..571
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 70..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10998264"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3S7E"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 223..248
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3SMH"
FT STRAND 283..294
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:3SMH"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3S7E"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 329..335
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:3S7E"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 463..472
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 495..504
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 526..534
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 556..562
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:3S7I"
FT HELIX 567..575
FT /evidence="ECO:0007829|PDB:3S7I"
FT STRAND 581..584
FT /evidence="ECO:0007829|PDB:3S7I"
SQ SEQUENCE 626 AA; 71345 MW; 1A6BBBE41490D0E3 CRC64;
MRGRVSPLML LLGILVLASV SATHAKSSPY QKKTENPCAQ RCLQSCQQEP DDLKQKACES
RCTKLEYDPR CVYDPRGHTG TTNQRSPPGE RTRGRQPGDY DDDRRQPRRE EGGRWGPAGP
REREREEDWR QPREDWRRPS HQQPRKIRPE GREGEQEWGT PGSHVREETS RNNPFYFPSR
RFSTRYGNQN GRIRVLQRFD QRSRQFQNLQ NHRIVQIEAK PNTLVLPKHA DADNILVIQQ
GQATVTVANG NNRKSFNLDE GHALRIPSGF ISYILNRHDN QNLRVAKISM PVNTPGQFED
FFPASSRDQS SYLQGFSRNT LEAAFNAEFN EIRRVLLEEN AGGEQEERGQ RRWSTRSSEN
NEGVIVKVSK EHVEELTKHA KSVSKKGSEE EGDITNPINL REGEPDLSNN FGKLFEVKPD
KKNPQLQDLD MMLTCVEIKE GALMLPHFNS KAMVIVVVNK GTGNLELVAV RKEQQQRGRR
EEEEDEDEEE EGSNREVRRY TARLKEGDVF IMPAAHPVAI NASSELHLLG FGINAENNHR
IFLAGDKDNV IDQIEKQAKD LAFPGSGEQV EKLIKNQKES HFVSARPQSQ SQSPSSPEKE
SPEKEDQEEE NQGGKGPLLS ILKAFN
