CRU1_RAPSA
ID CRU1_RAPSA Reviewed; 479 AA.
AC Q02498;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cruciferin PGCRURSE5;
DE AltName: Full=11S globulin;
DE AltName: Full=12S storage protein;
DE Contains:
DE RecName: Full=Cruciferin PGCRURSE5 alpha chain;
DE Contains:
DE RecName: Full=Cruciferin PGCRURSE5 beta chain;
DE Flags: Precursor;
GN Name=CRURS;
OS Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus.
OX NCBI_TaxID=3726;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Saxa Knacker;
RX PubMed=1421150; DOI=10.1007/bf00040606;
RA Depigny-This D., Raynal M., Aspart L., Delseny M., Grellet F.;
RT "The cruciferin gene family in radish.";
RL Plant Mol. Biol. 20:467-479(1992).
CC -!- FUNCTION: This is a seed storage protein.
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; X59808; CAA42478.1; -; Genomic_DNA.
DR PIR; S26223; S26223.
DR AlphaFoldDB; Q02498; -.
DR SMR; Q02498; -.
DR Proteomes; UP000504610; Unplaced.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0010431; P:seed maturation; IEA:UniProt.
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; Phosphoprotein; Reference proteome; Seed storage protein;
KW Signal; Storage protein.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..289
FT /note="Cruciferin PGCRURSE5 alpha chain"
FT /id="PRO_0000032040"
FT CHAIN 290..479
FT /note="Cruciferin PGCRURSE5 beta chain"
FT /id="PRO_0000032041"
FT DOMAIN 42..241
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 302..451
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 117..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 415
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT DISULFID 37..70
FT /evidence="ECO:0000250"
FT DISULFID 113..296
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 53256 MW; 4E06960C0974E710 CRC64;
MVKLAHLLVA TFGVLLVLNG CLARQSLGVP PQLGNACNLD NLDVLQPTET IKSEAGRLEY
WDHNHPQLRC AGVSVSRLII EQGGLYLPTF FSSPKIAYVV QGMGISGRVV PGCAETFMDS
QPMQGQGQQG QQGQQGQQQQ GFRDMHQKVE HVRHGDVIAI TAGSAHWIYN TGDQPLVIVC
LLDIANYQNQ LDRNPRTFRL AGNNPQGGSH QQQQQQQQNM LSGFDPQVLA QALKMQLRLA
QELQNQQDNR GNIVRVKGPF QVVRPPLRQQ YESEQWRHPR GPPQSPQDNG LEETICSMRT
HENIDDPARA DVYKPNLGRV TSVNSYTLPI LQYIRLSATR GILQGNAMVL PKYNMNANEI
LYCTQGQARI QVVNDNGQNV LDQQVQKGQL VVIPQGFAYV VQSHGNNFEW ISFKTNANAM
VSTLAGRTSA LRALPLEVIT NAFQISLEEA RRIKFNTPET TLTHARGGQP QLIEEIVEA