ID A5Z1Q8_ARADU Unreviewed; 160 AA. AC A5Z1Q8; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 84. DE SubName: Full=Ara d 2.01 {ECO:0000313|EMBL:ABQ96212.1}; DE SubName: Full=Ara h 2 allergen {ECO:0000313|EMBL:QGA89289.1}; DE SubName: Full=Conglutin {ECO:0000313|EMBL:ABW36071.1, ECO:0000313|RefSeq:NP_001391917.1}; GN Name=Ara d 2.01 {ECO:0000313|EMBL:ABQ96212.1}; GN Synonyms=ara d 2 {ECO:0000313|EMBL:ABW36071.1}, Ara h 2 GN {ECO:0000313|EMBL:QGA89289.1}, conglutin GN {ECO:0000313|RefSeq:NP_001391917.1}, LOC107462439 GN {ECO:0000313|RefSeq:NP_001391917.1}; OS Arachis duranensis (Wild 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=130453 {ECO:0000313|EMBL:ABQ96212.1}; RN [1] {ECO:0000313|EMBL:ABQ96212.1, ECO:0000313|RefSeq:NP_001391917.1} RP NUCLEOTIDE SEQUENCE. 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 [2] {ECO:0000313|EMBL:ABQ96212.1} RP NUCLEOTIDE SEQUENCE. RA Kang B., Hong J., Kim J., Kim A., Lee S., Cheon D., Jee Y.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ABW36071.1} RP NUCLEOTIDE SEQUENCE. RA Ramos M.L., Huntley J.J., Maleki S.J., Ozias-Akins P.; RT "Identification of a hypoallergenic Ara d 2.01 isoform in Arachis RT duranensis."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0007829|PDB:3OB4} RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 31-160, AND DISULFIDE BONDS. RX PubMed=21255036; DOI=10.1111/j.1398-9995.2010.02532.x; RA Mueller G.A., Gosavi R.A., Pomes A., Wunschmann S., Moon A.F., London R.E., RA Pedersen L.C.; RT "Ara h 2: crystal structure and IgE binding distinguish two subpopulations RT of peanut allergic patients by epitope diversity."; RL Allergy 66:878-885(2011). RN [5] {ECO:0000313|RefSeq:NP_001391917.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22967170; RA Nagy E.D., Guo Y., Tang S., Bowers J.E., Okashah R.A., Taylor C.A., RA Zhang D., Khanal S., Heesacker A.F., Khalilian N., Farmer A.D., RA Carrasquilla-Garcia N., Penmetsa R.V., Cook D., Stalker H.T., Nielsen N., RA Ozias-Akins P., Knapp S.J.; RT "A high-density genetic map of Arachis duranensis, a diploid ancestor of RT cultivated peanut."; RL BMC Genomics 13:469-469(2012). RN [6] {ECO:0000313|RefSeq:NP_001391917.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25551607; RA Chopra R., Burow G., Farmer A., Mudge J., Simpson C.E., Burow M.D.; RT "Comparisons of De Novo Transcriptome Assemblers in Diploid and Polyploid RT Species Using Peanut (Arachis spp.) RNA-Seq Data."; RL PLoS ONE 9:E115055-E115055(2014). RN [7] {ECO:0000313|EMBL:QGA89289.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PI219823 {ECO:0000313|EMBL:QGA89289.1}; RX PubMed=31675366; RA Hilu K.W., Friend S.A., Vallanadu V., Brown A.M., Hollingsworth L.R.IV., RA Bevan D.R.; RT "Molecular evolution of genes encoding allergen proteins in the peanuts RT genus Arachis: Structural and functional implications."; RL PLoS ONE 14:0-e0222440(2019). RN [8] {ECO:0000313|RefSeq:NP_001391917.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family. CC {ECO:0000256|ARBA:ARBA00008262}. 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; EF609641; ABQ96212.1; -; mRNA. DR EMBL; EU183225; ABW36071.1; -; Genomic_DNA. DR EMBL; MN027223; QGA89289.1; -; Genomic_DNA. DR RefSeq; NP_001391917.1; NM_001404988.1. DR RefSeq; XP_015936509.1; XM_016081023.1. DR PDB; 3OB4; X-ray; 2.71 A; A=31-160. DR PDBsum; 3OB4; -. DR KEGG; adu:107462439; -. DR OrthoDB; 945792at2759; -. DR Proteomes; UP000515211; Chromosome 8. 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. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3OB4}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Reference proteome {ECO:0000313|Proteomes:UP000515211}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..160 FT /evidence="ECO:0000256|SAM:SignalP, FT ECO:0000313|RefSeq:NP_001391917.1" FT /id="PRO_5036531203" FT DOMAIN 33..148 FT /note="Bifunctional inhibitor/plant lipid transfer FT protein/seed storage helical" FT /evidence="ECO:0000259|SMART:SM00499" FT REGION 52..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 33..104 FT /evidence="ECO:0007829|PDB:3OB4" FT DISULFID 45..91 FT /evidence="ECO:0007829|PDB:3OB4" FT DISULFID 92..140 FT /evidence="ECO:0007829|PDB:3OB4" FT DISULFID 106..148 FT /evidence="ECO:0007829|PDB:3OB4" SQ SEQUENCE 160 AA; 18758 MW; EE66B2BAB64D6832 CRC64; MAKLTILVAL ALFLLAAHAS ARQQWELQGD RRCQSQLERA NLRPCEQHLM QKIQRDEDSY ERDPYSPSQD PYSPSPYDRR GAGSSQHQER CCNELNEFEN NQRCMCEALQ QIMENQSDRL QGRQQEQQFK RELRNLPQQC GLRAPQRCDL DVESGGRDRY //