LEGB4_VICFA
ID LEGB4_VICFA Reviewed; 484 AA.
AC P05190;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Legumin type B;
DE Contains:
DE RecName: Full=Legumin type B alpha chain;
DE AltName: Full=Legumin type B acidic chain;
DE Contains:
DE RecName: Full=Legumin type B beta chain;
DE AltName: Full=Legumin type B basic chain;
DE Flags: Precursor;
GN Name=LEB4;
OS Vicia faba (Broad bean) (Faba vulgaris).
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; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3960730; DOI=10.1093/nar/14.6.2707;
RA Baeumlein H., Wobus U., Pustell J., Kafatos F.C.;
RT "The legumin gene family: structure of a B type gene of Vicia faba and a
RT possible legumin gene specific regulatory element.";
RL Nucleic Acids Res. 14:2707-2720(1986).
CC -!- FUNCTION: This protein found in the seeds of many leguminous and non-
CC leguminous plants is the source of sulfur-containing amino acids in
CC seed meals.
CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic
CC chain derived from a single precursor and linked by a disulfide bond.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
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DR EMBL; X03677; CAA27313.1; -; Genomic_DNA.
DR PIR; A24942; A24942.
DR AlphaFoldDB; P05190; -.
DR SMR; P05190; -.
DR PRIDE; P05190; -.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR022379; 11S_seedstore_CS.
DR InterPro; IPR006044; 11S_seedstore_pln.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR PRINTS; PR00439; 11SGLOBULIN.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..303
FT /note="Legumin type B alpha chain"
FT /id="PRO_0000032078"
FT CHAIN 304..484
FT /note="Legumin type B beta chain"
FT /id="PRO_0000032079"
FT DOMAIN 38..257
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 316..463
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 109..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..66
FT /evidence="ECO:0000250"
FT DISULFID 109..310
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 484 AA; 54448 MW; 3A40F53F43F3D737 CRC64;
MSKPFLSLLS LSLLLFTSTC LATSSEFDRL NQCRLDNINA LEPDHRVESE AGLTETWNPN
HPELRCAGVS LIRRTIDPNG LHLPSYSPSP QLIYIIQGKG VIGLTLPGCP QTYQEPRSSQ
SRQGSRQQQP DSHQKIRRFR KGDIIAIPSG IPYWTYNNGD EPLVAISLLD TSNIANQLDS
TPRVFYLVGN PEVEFPETQE EQQERHQQKH SLPVGRRGGQ HQQEEESEEQ KDGNSVLSGF
SSEFLAHTFN TEEDTAKRLR SPRDKRNQIV RVEGGLRIIN PEGQQEEEEE EEEEKQRSEQ
GRNGLEETIC SLKIRENIAQ PARADLYNPR AGSISTANSL TLPILRYLRL SAEYVRLYRN
GIYAPHWNIN ANSLLYVIRG EGRVRIVNSQ GNAVFDNKVT KGQLVVVPQN FVVAEQAGEE
EGLEYLVFKT NDRAAVSHVQ QVFRATPADV LANAFGLRQR QVTELKLSGN RGPLVHPQSQ
SQSN