P04776 (GLYG1_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycinin G1

Cleaved into the following 2 chains:

1. Glycinin A1a subunit
2. Glycinin Bx subunit

Gene names

Name:

GY1

Organism

Glycine max (Soybean) (Glycine hispida)

Taxonomic identifier

3847 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glycinin is the major seed storage protein of soybean.
Subunit structure	Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ref.6 Ref.7
Post-translational modification	The precursor is post-translationally processed to form a covalently linked A1a-Bx subunit complex.
Sequence similarities	Belongs to the 11S seed storage protein (globulins) family.

Ontologies

Keywords
Domain	Signal
Molecular function	Seed storage protein Storage protein
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Molecular function	nutrient reservoir activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Chain

20 – 306

287

Glycinin A1a subunit

PRO_0000032009

Propeptide

307 – 310

4

PRO_0000032010

Chain

311 – 490

180

Glycinin Bx subunit

PRO_0000032011

Propeptide

491 – 495

5

PRO_0000032012

Amino acid modifications

Disulfide bond

31 ↔ 64

Ref.6 Ref.7

Disulfide bond

107 ↔ 317

Interchain (between A1a and Bx chains) Ref.6 Ref.7

Experimental info

Sequence conflict

42

1

D → G in CAA26723. Ref.3

Sequence conflict

108

1

P → S in CAA26723. Ref.3

Sequence conflict

136

1

F → S in CAA26723. Ref.3

Sequence conflict

360

1

E → G in CAA26723. Ref.3

Secondary structure

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495

Helix Strand Turn

Details...

Beta strand

44 – 47

4

Beta strand

50 – 54

5

Helix

60 – 65

6

Beta strand

68 – 74

7

Beta strand

78 – 87

10

Beta strand

89 – 95

7

Beta strand

98 – 103

6

Beta strand

133 – 136

4

Beta strand

140 – 144

5

Beta strand

149 – 154

6

Beta strand

156 – 158

3

Beta strand

160 – 166

7

Beta strand

181 – 187

7

Helix

193 – 196

4

Helix

220 – 223

4

Helix

226 – 233

8

Helix

237 – 243

7

Beta strand

254 – 257

4

Beta strand

322 – 324

3

Beta strand

326 – 329

4

Beta strand

332 – 335

4

Turn

336 – 338

3

Beta strand

339 – 344

6

Turn

346 – 348

3

Helix

350 – 352

3

Turn

353 – 356

4

Beta strand

359 – 364

6

Beta strand

369 – 375

7

Beta strand

380 – 394

15

Beta strand

400 – 407

8

Beta strand

411 – 414

4

Beta strand

419 – 424

6

Beta strand

429 – 439

11

Beta strand

442 – 447

6

Helix

452 – 454

3

Helix

457 – 464

8

Helix

468 – 476

9

Beta strand

481 – 484

4

Sequences

	Sequence		Length	Mass (Da)
	P04776 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: 329CB0545B24D894	FASTA	495	55,706
	10 20 30 40 50 60 MAKLVFSLCF LLFSGCCFAF SSREQPQQNE CQIQKLNALK PDNRIESEGG LIETWNPNNK 70 80 90 100 110 120 PFQCAGVALS RCTLNRNALR RPSYTNGPQE IYIQQGKGIF GMIYPGCPST FEEPQQPQQR 130 140 150 160 170 180 GQSSRPQDRH QKIYNFREGD LIAVPTGVAW WMYNNEDTPV VAVSIIDTNS LENQLDQMPR 190 200 210 220 230 240 RFYLAGNQEQ EFLKYQQEQG GHQSQKGKHQ QEEENEGGSI LSGFTLEFLE HAFSVDKQIA 250 260 270 280 290 300 KNLQGENEGE DKGAIVTVKG GLSVIKPPTD EQQQRPQEEE EEEEDEKPQC KGKDKHCQRP 310 320 330 340 350 360 RGSQSKSRRN GIDETICTMR LRHNIGQTSS PDIYNPQAGS VTTATSLDFP ALSWLRLSAE 370 380 390 400 410 420 FGSLRKNAMF VPHYNLNANS IIYALNGRAL IQVVNCNGER VFDGELQEGR VLIVPQNFVV 430 440 450 460 470 480 AARSQSDNFE YVSFKTNDTP MIGTLAGANS LLNALPEEVI QHTFNLKSQQ ARQIKNNNPF 490 KFLVPPQESQ KRAVA

References

[1]	"Characterization of the glycinin gene family in soybean." Nielsen N.C., Dickinson C.D., Cho T.-J., Thanh V.H., Scallon B.J., Fischer R.L., Sims T.L., Drews G.N., Goldberg R.B. Plant Cell 1:313-328(1989) [PubMed: 2485233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Dare. Tissue: Leaf.
[2]	"The glycinin Gy1 gene from soybean." Sims T.L., Goldberg R.B. Nucleic Acids Res. 17:4386-4386(1989) [PubMed: 2740229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Dare. Tissue: Leaf.
[3]	"A cDNA clone encoding a glycinin A1a subunit precursor of soybean." Negoro T., Momma T., Fukazawa C. Nucleic Acids Res. 13:6719-6731(1985) [PubMed: 2997720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Bonminori.
[4]	"An alternate cDNA encoding glycinin A1a Bx subunit." Utsumi S., Kohno M., Mori T., Kito M. J. Agric. Food Chem. 35:210-214(1987) Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"mRNA of soybean proglycinin A1aB1b subunit." Urade R., Nakatani H., Nakano C. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Crystal structure of soybean proglycinin A1aB1b homotrimer." Adachi M., Takenaka Y., Gidamis A.B., Mikami B., Utsumi S. J. Mol. Biol. 305:291-305(2001) [PubMed: 11124907] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-495, SUBUNIT, DISULFIDE BONDS.
[7]	"Crystal structures and structural stabilities of the disulfide bond-deficient soybean proglycinin mutants C12G and C88S." Adachi M., Okuda E., Kaneda Y., Hashimoto A., Shutov A.D., Becker C., Muntz K., Utsumi S. J. Agric. Food Chem. 51:4633-4639(2003) [PubMed: 14705889] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 20-495, SUBUNIT, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M36686 mRNA. Translation: AAA33966.1.
X15121 Genomic DNA. Translation: CAA33215.1.
X02985 mRNA. Translation: CAA26723.1.
AB113349 mRNA. Translation: BAC78522.1.

PIR

FWSYG2. A23497.
S10851.

RefSeq

XP_003521292.1. XM_003521244.1.

UniGene

Gma.1897.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FXZ	X-ray	2.80	A/B/C	20-495	[»]
1UCX	X-ray	3.20	A/B/C	20-495	[»]
1UD1	X-ray	3.10	A/B/C	20-495	[»]

ProteinModelPortal

P04776.

SMR

P04776. Positions 29-489.

ModBase

Search...

Protein family/group databases

Allergome

1142. Gly m 6.0101.
5821. Gly m 6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

GLYMA03G32030.1; GLYMA03G32030.1; GLYMA03G32030.
Gmax_FGT19686; Gmax_FGP19686; Gmax_FG19686.

GeneID

547901.

Phylogenomic databases

PhylomeDB

P04776.

Gene expression databases

Genevestigator

P04776.

Family and domain databases

InterPro

IPR022379. 11S_seedstore_CS.
IPR006044. 11S_seedstore_pln.
IPR006045. Cupin_1.
IPR011051. Cupin_RmlC_type.
IPR014710. RmlC-like_jellyroll.
[Graphical view]

Gene3D

G3DSA:2.60.120.10. RmlC-like_jellyroll. 3 hits.

Pfam

PF00190. Cupin_1. 2 hits.
[Graphical view]

PRINTS

PR00439. 11SGLOBULIN.

SMART

SM00835. Cupin_1. 2 hits.
[Graphical view]

SUPFAM

SSF51182. RmlC_like_cupin. 2 hits.

PROSITE

PS00305. 11S_SEED_STORAGE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLYG1_SOYBN

Accession

Primary (citable) accession number: P04776

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	October 1, 1989
Last modified:	January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program