CONG1_PRUDU
ID CONG1_PRUDU Reviewed; 431 AA.
AC P82952; A0A5E4EAH6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Gamma conglutin 1 {ECO:0000305};
DE AltName: Full=Conglutin gamma {ECO:0000303|PubMed:31529539};
DE AltName: Full=Seed allergenic protein 2 {ECO:0000303|PubMed:22260748};
DE AltName: Allergen=Pru du gamma-conglutin {ECO:0000303|PubMed:22260748};
DE Contains:
DE RecName: Full=Gamma conglutin 1 beta subunit {ECO:0000305};
DE Contains:
DE RecName: Full=Gamma conglutin 1 alpha subunit {ECO:0000305};
DE Flags: Precursor;
GN Name=Cgamma1 {ECO:0000303|PubMed:31529539};
GN ORFNames=ALMOND_2B001639 {ECO:0000312|EMBL:VVA12735.1};
OS Prunus dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Texas;
RX PubMed=31529539; DOI=10.1111/tpj.14538;
RA Alioto T., Alexiou K.G., Bardil A., Barteri F., Castanera R., Cruz F.,
RA Dhingra A., Duval H., Fernandez I Marti A., Frias L., Galan B.,
RA Garcia J.L., Howad W., Gomez-Garrido J., Gut M., Julca I., Morata J.,
RA Puigdomenech P., Ribeca P., Rubio Cabetas M.J., Vlasova A., Wirthensohn M.,
RA Garcia-Mas J., Gabaldon T., Casacuberta J.M., Arus P.;
RT "Transposons played a major role in the diversification between the closely
RT related almond and peach genomes: results from the almond genome
RT sequence.";
RL Plant J. 101:455-472(2020).
RN [2]
RP PROTEIN SEQUENCE OF 25-49, AND ALLERGEN.
RC STRAIN=cv. Tuono; TISSUE=Seed;
RX PubMed=12065909; DOI=10.1159/000059399;
RA Poltronieri P., Cappello M.S., Dohmae N., Conti A., Fortunato D.,
RA Pastorello E.A., Ortolani C., Zacheo G.;
RT "Identification and characterisation of the IgE-binding proteins 2S albumin
RT and conglutin gamma in almond (Prunus dulcis) seeds.";
RL Int. Arch. Allergy Immunol. 128:97-104(2002).
RN [3]
RP REVIEW.
RX PubMed=22260748; DOI=10.1021/jf2044923;
RA Costa J., Mafra I., Carrapatoso I., Oliveira M.B.P.P.;
RT "Almond allergens: molecular characterization, detection, and clinical
RT relevance.";
RL J. Agric. Food Chem. 60:1337-1349(2012).
RN [4]
RP REVIEW.
RX PubMed=32270879; DOI=10.1002/jsfa.10417;
RA Zhang Y., Jin T.;
RT "Almond allergens: update and perspective on identification and
RT characterization.";
RL J. Sci. Food Agric. 100:4657-4663(2020).
CC -!- FUNCTION: Sulfur-rich seed storage protein that remains undegraded at
CC germination. {ECO:0000250|UniProtKB:Q9FSH9}.
CC -!- SUBUNIT: Two-subunit monomeric unit made of alpha and beta subunits
CC coupled by disulfide bonds (at pH 4.5 and under non-reducing
CC conditions) (By similarity). Monomeric alpha and beta subunits in
CC reducing conditions (By similarity). Can also form oligomers including
CC dimer, tetramer and cyclic hexamer (trimer of dimers) (at pH > 5.5) (By
CC similarity). Component of globulins complexes which accumulate in seeds
CC (By similarity). Interacts with flavonoids (e.g. apigenin glucosides)
CC present in globulins complexes (By similarity).
CC {ECO:0000250|UniProtKB:Q42369, ECO:0000250|UniProtKB:Q9FSH9}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9FSH9}. Note=Present in the extracellular
CC spaces of germinating seedlings. {ECO:0000250|UniProtKB:Q9FSH9}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:12065909). Binds
CC to IgE (PubMed:12065909). {ECO:0000269|PubMed:12065909}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; CABIKO010000006; VVA12735.1; -; Genomic_DNA.
DR AlphaFoldDB; P82952; -.
DR SMR; P82952; -.
DR Allergome; 911; Pru du AP.
DR EnsemblPlants; VVA12735; VVA12735; Prudul26B001639.
DR Gramene; VVA12735; VVA12735; Prudul26B001639.
DR OMA; PNNVQGV; -.
DR Proteomes; UP000327085; Chromosome: 6.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR PANTHER; PTHR47965; PTHR47965; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; IgE-binding protein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..431
FT /note="Gamma conglutin 1"
FT /id="PRO_0000262967"
FT CHAIN 25..275
FT /note="Gamma conglutin 1 alpha subunit"
FT /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT /id="PRO_0000451770"
FT CHAIN 276..431
FT /note="Gamma conglutin 1 beta subunit"
FT /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT /id="PRO_0000451771"
FT DOMAIN 51..407
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT SITE 271..272
FT /note="Cleavage; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT SITE 273..274
FT /note="Cleavage; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT SITE 275..276
FT /note="Cleavage; partial"
FT /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT DISULFID 79..168
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 93..106
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 98..123
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 109..118
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 212
FT /note="Interchain (between alpha and beta chains, with C-
FT 417 in beta chain)"
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 322..369
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 417
FT /note="Interchain (between alpha and beta chains, with C-
FT 212 in alpha chain)"
FT /evidence="ECO:0000250|UniProtKB:Q42369"
SQ SEQUENCE 431 AA; 46945 MW; EE059981E5648909 CRC64;
MASFLHNFLL FFCSLSLIIL TSSATKSQTH VPIRPNKLVL KVQKDRATNL HVVQIHKRTP
LVQFPFVIDL TGRFLSVNCE NQYTSSTYKA PVCHSSQCAR ANSHTCRTCS SSKTRPGCHT
NACGLLTTNP VTQQSAQGEL AEDVLKIPST QGSSPGPMVT YPHFLFACAP SNILQKGLPK
NVQGVAGLGH SPISLPYQLA SHFGFPPKFA VCLTSSPGKN GAVFFGEGPY FMKPGIDVSR
QLTYAPFTIG QQGEYYINVQ SFKINNAMLP SIPKGGFGGA MISTTTPYTT LQTPIFRALN
QLFMNQLRGV PHVKPVAPFG ACFDANRIPT SKMGPTVPSI DLVLDNKKNI MWRIFGANAM
IQPRPGVMCL AFVDGGMRPK APIVIGTQQL EDNLLQFDLM NSRLGFSSSL LFRRTNCANF
NFGTSSTNTD P
