GLCAP_SOYBN
ID GLCAP_SOYBN Reviewed; 621 AA.
AC P11827; Q4LER6; Q7XXT2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Beta-conglycinin alpha' subunit {ECO:0000303|PubMed:3013879};
DE Short=CG-alpha'-1 {ECO:0000303|PubMed:22193750};
DE AltName: Full=Beta-conglycinin alpha prime subunit {ECO:0000303|PubMed:17181539};
DE AltName: Allergen=Gly m 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=CG-1 {ECO:0000305}; Synonyms=CGY-1 {ECO:0000303|Ref.3};
GN ORFNames=GLYMA_10G246300 {ECO:0000312|EMBL:KRH35498.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3013879; DOI=10.1016/s0021-9258(18)67644-6;
RA Doyle J.J., Schuler M.A., Godette W.D., Zenger V., Beachy R.N.,
RA Slightom J.L.;
RT "The glycosylated seed storage proteins of Glycine max and Phaseolus
RT vulgaris. Structural homologies of genes and proteins.";
RL J. Biol. Chem. 261:9228-9238(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=17181539; DOI=10.1111/j.1742-4658.2006.05613.x;
RA Wadahama H., Kamauchi S., Ishimoto M., Kawada T., Urade R.;
RT "Protein disulfide isomerase family proteins involved in soybean protein
RT biogenesis.";
RL FEBS J. 274:687-703(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND44467547; DOI=10.1007/s10681-010-0251-7;
RA Kim S.-I., Kim M.Y., Van K., Lee Y.-H., Kim H.S., Cai C.M., Park B.-S.,
RA Seo H.-S., Lee S.-H.;
RT "The development of a co-dominant marker for the beta-conglycinin alpha'
RT subunit in soybeans.";
RL Euphytica 177:355-363(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=22193750; DOI=10.1007/s11103-011-9865-y;
RA Tsubokura Y., Hajika M., Kanamori H., Xia Z., Watanabe S., Kaga A.,
RA Katayose Y., Ishimoto M., Harada K.;
RT "The beta-conglycinin deficiency in wild soybean is associated with the
RT tail-to-tail inverted repeat of the alpha-subunit genes.";
RL Plant Mol. Biol. 78:301-309(2012).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [6]
RP PROTEIN SEQUENCE OF 63-75.
RC STRAIN=cv. Raiden;
RX DOI=10.1016/S0031-9422(00)81477-6;
RA Hirano H., Kagawa H., Kamata Y., Yamauchi F.;
RT "Structural homology among the major 7s globulin subunits of soybean seed
RT storage proteins.";
RL Phytochemistry 26:41-45(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 321-621.
RX PubMed=6897678; DOI=10.1093/nar/10.24.8245;
RA Schuler M.A., Ladin B.F., Pollaco J.C., Freyer G., Beachy R.N.;
RT "Structural sequences are conserved in the genes coding for the alpha,
RT alpha' and beta-subunits of the soybean 7S seed storage protein.";
RL Nucleic Acids Res. 10:8245-8261(1982).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-621.
RX PubMed=6298713; DOI=10.1093/nar/10.24.8225;
RA Schuler M.A., Schmitt E.S., Beachy R.N.;
RT "Closely related families of genes code for the alpha and alpha' subunits
RT of the soybean 7S storage protein complex.";
RL Nucleic Acids Res. 10:8225-8244(1982).
RN [9]
RP FUNCTION.
RX PubMed=12681509; DOI=10.1016/s0014-5793(03)00265-5;
RA Tsuruki T., Kishi K., Takahashi M., Tanaka M., Matsukawa T., Yoshikawa M.;
RT "Soymetide, an immunostimulating peptide derived from soybean beta-
RT conglycinin, is an fMLP agonist.";
RL FEBS Lett. 540:206-210(2003).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12787246; DOI=10.1046/j.1365-313x.2003.01754.x;
RA Nishizawa K., Maruyama N., Satoh R., Fuchikami Y., Higasa T., Utsumi S.;
RT "A C-terminal sequence of soybean beta-conglycinin alpha' subunit acts as a
RT vacuolar sorting determinant in seed cells.";
RL Plant J. 34:647-659(2003).
RN [11]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15447650; DOI=10.1111/j.1365-313x.2004.02204.x;
RA Mori T., Maruyama N., Nishizawa K., Higasa T., Yagasaki K., Ishimoto M.,
RA Utsumi S.;
RT "The composition of newly synthesized proteins in the endoplasmic reticulum
RT determines the transport pathways of soybean seed storage proteins.";
RL Plant J. 40:238-249(2004).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16900322; DOI=10.1007/s11103-006-9007-0;
RA Nishizawa K., Maruyama N., Utsumi S.;
RT "The C-terminal region of alpha' subunit of soybean beta-conglycinin
RT contains two types of vacuolar sorting determinants.";
RL Plant Mol. Biol. 62:111-125(2006).
RN [13]
RP ALLERGEN.
RX PubMed=17823539; DOI=10.1159/000108135;
RA Guo P., Piao X., Cao Y., Ou D., Li D.;
RT "Recombinant soybean protein beta-conglycinin alpha'-subunit expression and
RT induced hypersensitivity reaction in rats.";
RL Int. Arch. Allergy Immunol. 145:102-110(2008).
RN [14]
RP ALLERGEN.
RX PubMed=18996574; DOI=10.1016/j.jaci.2008.09.034;
RA Holzhauser T., Wackermann O., Ballmer-Weber B.K., Bindslev-Jensen C.,
RA Scibilia J., Perono-Garoffo L., Utsumi S., Poulsen L.K., Vieths S.;
RT "Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and
RT Gly m 6 (glycinin) are potential diagnostic markers for severe allergic
RT reactions to soy.";
RL J. Allergy Clin. Immunol. 123:452-458(2009).
RN [15]
RP DISULFIDE BOND.
RX PubMed=22218927; DOI=10.1104/pp.111.189621;
RA Wadahama H., Iwasaki K., Matsusaki M., Nishizawa K., Ishimoto M.,
RA Arisaka F., Takagi K., Urade R.;
RT "Accumulation of beta-conglycinin in soybean cotyledon through the
RT formation of disulfide bonds between alpha'- and alpha-subunits.";
RL Plant Physiol. 158:1395-1405(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 204-621.
RX PubMed=14747705; DOI=10.1107/s0907444903027367;
RA Maruyama Y., Maruyama N., Mikami B., Utsumi S.;
RT "Structure of the core region of the soybean beta-conglycinin alpha'
RT subunit.";
RL Acta Crystallogr. D 60:289-297(2004).
CC -!- FUNCTION: Seed storage protein. Accumulates during seed development and
CC is hydrolyzed after germination to provide a carbon and nitrogen source
CC for the developing seedling. {ECO:0000305}.
CC -!- SUBUNIT: The alpha-, alpha'-, and beta-subunits associate in various
CC combinations to form trimeric proteins. {ECO:0000305|PubMed:15447650}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain {ECO:0000305}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:15447650}. Protein storage
CC vacuole {ECO:0000269|PubMed:12787246, ECO:0000269|PubMed:15447650,
CC ECO:0000269|PubMed:16900322, ECO:0000269|PubMed:17181539}.
CC Note=Localizes in protein storage vacuoles in cotyledons of developing
CC and mature beans (PubMed:17181539, PubMed:15447650, PubMed:12787246,
CC PubMed:16900322). Synthesized and assembled into trimers in the
CC endoplasmic reticulum, and transported to the protein storage vacuoles
CC by the dense vesicles (PubMed:15447650). {ECO:0000269|PubMed:12787246,
CC ECO:0000269|PubMed:15447650, ECO:0000269|PubMed:16900322,
CC ECO:0000269|PubMed:17181539}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:18996574). Binds
CC to IgE of patients with severe allergic reactions (anaphylaxis) to
CC soybean (PubMed:18996574). Causes an allergic reaction in rat
CC (PubMed:17823539). Induces IgE-mediated passive cutaneous anaphylactic
CC reactions coupled to mast cell degranulation and histamine release
CC after intragastric absorption (PubMed:17823539).
CC {ECO:0000269|PubMed:17823539, ECO:0000269|PubMed:18996574}.
CC -!- MISCELLANEOUS: A tridecapeptide (MITLAIPVNKPGR), called soymetide and
CC derived from a trypsin digest of CG-1, stimulates phagocytosis of human
CC neutrophils (PubMed:12681509). The N-terminal methionine residue is
CC essential for its activity, and the N-terminal soymetide-4 (MITL) is
CC the minimal structure required for phagocytosis stimulation
CC (PubMed:12681509). Although not formylated at their N-termini,
CC soymetides have a weak affinity for the N-formyl-methionyl-leucyl-
CC phenylalanine (fMLP) receptor (PubMed:12681509).
CC {ECO:0000269|PubMed:12681509}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB01374.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; M13759; AAB01374.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB113351; BAC78524.1; -; mRNA.
DR EMBL; GU723691; ADD38965.1; -; Genomic_DNA.
DR EMBL; AB197784; BAE02726.1; -; mRNA.
DR EMBL; AB234094; BAE44298.1; -; mRNA.
DR EMBL; AB610665; BAK53445.1; -; Genomic_DNA.
DR EMBL; CM000843; KRH35498.1; -; Genomic_DNA.
DR EMBL; ACUP02006681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01290; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; J01293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B24810; B24810.
DR RefSeq; NP_001237316.1; NM_001250387.1.
DR PDB; 1UIK; X-ray; 2.30 A; A/B/C=204-621.
DR PDBsum; 1UIK; -.
DR AlphaFoldDB; P11827; -.
DR SMR; P11827; -.
DR STRING; 3847.GLYMA10G39150.1; -.
DR Allergome; 5816; Gly m 5.
DR TCDB; 1.C.121.1.1; the soybean glycinin-derived pore-forming peptide (sgpp) family.
DR PRIDE; P11827; -.
DR EnsemblPlants; KRH35498; KRH35498; GLYMA_10G246300.
DR GeneID; 548007; -.
DR Gramene; KRH35498; KRH35498; GLYMA_10G246300.
DR KEGG; gmx:548007; -.
DR eggNOG; ENOG502QQEP; Eukaryota.
DR HOGENOM; CLU_018703_0_1_1; -.
DR OMA; YEACPRE; -.
DR OrthoDB; 1072107at2759; -.
DR Proteomes; UP000008827; Chromosome 10.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0000326; C:protein storage vacuole; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
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; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW Seed storage protein; Signal; Storage protein; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..62
FT /evidence="ECO:0000305|Ref.6"
FT /id="PRO_0000032188"
FT CHAIN 63..621
FT /note="Beta-conglycinin alpha' subunit"
FT /id="PRO_0000032189"
FT DOMAIN 212..370
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 422..583
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 64..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..621
FT /note="Necessary for sorting to protein storage vacuole"
FT /evidence="ECO:0000269|PubMed:12787246,
FT ECO:0000269|PubMed:16900322"
FT COMPBIAS 64..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 69
FT /note="Interchain (with C-68 in alpha subunit)"
FT /evidence="ECO:0000305|PubMed:22218927"
FT CONFLICT 112
FT /note="H -> R (in Ref. 2; BAC78524)"
FT /evidence="ECO:0000305"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 258..285
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 320..331
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:1UIK"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 412..416
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 430..441
FT /evidence="ECO:0007829|PDB:1UIK"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 447..452
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 465..474
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 510..516
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 530..545
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 552..561
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 568..574
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:1UIK"
FT HELIX 579..588
FT /evidence="ECO:0007829|PDB:1UIK"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:1UIK"
SQ SEQUENCE 621 AA; 72228 MW; 0DF4B6E33737E0A5 CRC64;
MMRARFPLLL LGVVFLASVS VSFGIAYWEK QNPSHNKCLR SCNSEKDSYR NQACHARCNL
LKVEEEEECE EGQIPRPRPQ HPERERQQHG EKEEDEGEQP RPFPFPRPRQ PHQEEEHEQK
EEHEWHRKEE KHGGKGSEEE QDEREHPRPH QPHQKEEEKH EWQHKQEKHQ GKESEEEEED
QDEDEEQDKE SQESEGSESQ REPRRHKNKN PFHFNSKRFQ TLFKNQYGHV RVLQRFNKRS
QQLQNLRDYR ILEFNSKPNT LLLPHHADAD YLIVILNGTA ILTLVNNDDR DSYNLQSGDA
LRVPAGTTYY VVNPDNDENL RMITLAIPVN KPGRFESFFL SSTQAQQSYL QGFSKNILEA
SYDTKFEEIN KVLFGREEGQ QQGEERLQES VIVEISKKQI RELSKHAKSS SRKTISSEDK
PFNLRSRDPI YSNKLGKLFE ITPEKNPQLR DLDVFLSVVD MNEGALFLPH FNSKAIVVLV
INEGEANIEL VGIKEQQQRQ QQEEQPLEVR KYRAELSEQD IFVIPAGYPV VVNATSDLNF
FAFGINAENN QRNFLAGSKD NVISQIPSQV QELAFPGSAK DIENLIKSQS ESYFVDAQPQ
QKEEGNKGRK GPLSSILRAF Y
