LEGJ_PEA
ID LEGJ_PEA Reviewed; 503 AA.
AC P05692;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Legumin J;
DE Contains:
DE RecName: Full=Legumin J alpha chain;
DE AltName: Full=Legumin J acidic chain;
DE Contains:
DE RecName: Full=Legumin J beta chain;
DE AltName: Full=Legumin J basic chain;
DE Flags: Precursor;
GN Name=LEGJ;
OS Pisum sativum (Garden pea).
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; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Feltham First;
RX PubMed=3355508; DOI=10.1042/bj2500015;
RA Gatehouse J.A., Bown D., Gilroy J., Levasseur M., Castleton J.,
RA Ellis T.H.N.;
RT "Two genes encoding 'minor' legumin polypeptides in pea (Pisum sativum L.).
RT Characterization and complete sequence of the LegJ gene.";
RL Biochem. J. 250:15-24(1988).
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; X07014; CAA30067.1; -; Genomic_DNA.
DR PIR; S00336; S00336.
DR AlphaFoldDB; P05692; -.
DR SMR; P05692; -.
DR PRIDE; P05692; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Seed storage protein; Signal;
KW Storage protein.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..322
FT /note="Legumin J alpha chain"
FT /id="PRO_0000032072"
FT CHAIN 323..503
FT /note="Legumin J beta chain"
FT /id="PRO_0000032073"
FT DOMAIN 38..257
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 335..482
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..66
FT /evidence="ECO:0000250"
FT DISULFID 109..329
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 503 AA; 56895 MW; 3F90F4DE85046DAA CRC64;
MSKPFLSLLS LSLLLFASAC LATSSEFDRL NQCQLDSINA LEPDHRVESE AGLTETWNPN
HPELKCAGVS LIRRTIDPNG LHLPSFSPSP QLIFIIQGKG VLGLSFPGCP ETYEEPRSSQ
SRQESRQQQG DSHQKVRRFR KGDIIAIPSG IPYWTYNHGD EPLVAISLLD TSNIANQLDS
TPRVFYLGGN PETEFPETQE EQQGRHRQKH SYPVGRRSGH HQQEEESEEQ NEGNSVLSGF
SSEFLAQTFN TEEDTAKRLR SPRDERSQIV RVEGGLRIIK PKGKEEEEKE QSHSHSHREE
KEEEEEEEED EEEKQRSEER KNGLEETICS AKIRENIADA ARADLYNPRA GRISTANSLT
LPVLRYLRLS AEYVRLYRNG IYAPHWNINA NSLLYVIRGE GRVRIVNCQG NTVFDNKVRK
GQLVVVPQNF VVAEQAGEEE GLEYVVFKTN DRAAVSHVQQ VFRATPSEVL ANAFGLRQRQ
VTELKLSGNR GPLVHPRSQS QSH