CRU3_BRANA
ID CRU3_BRANA Reviewed; 509 AA.
AC P33525;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cruciferin CRU1;
DE AltName: Full=11S globulin;
DE AltName: Full=12S storage protein;
DE Contains:
DE RecName: Full=Cruciferin CRU1 alpha chain;
DE Contains:
DE RecName: Full=Cruciferin CRU1 beta chain;
DE Flags: Precursor;
GN Name=CRU1;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1421158; DOI=10.1007/bf00040615;
RA Roedin J., Sjoedahl S., Josefsson L.-G., Rask L.;
RT "Characterization of a Brassica napus gene encoding a cruciferin subunit:
RT estimation of sizes of cruciferin gene families.";
RL Plant Mol. Biol. 20:559-563(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; X62120; CAA44042.1; -; Genomic_DNA.
DR AlphaFoldDB; P33525; -.
DR SMR; P33525; -.
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; -; 3.
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; Seed storage protein; Signal;
KW Storage protein.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..319
FT /note="Cruciferin CRU1 alpha chain"
FT /id="PRO_0000032036"
FT CHAIN 320..509
FT /note="Cruciferin CRU1 beta chain"
FT /id="PRO_0000032037"
FT DOMAIN 42..271
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 332..481
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 119..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96318"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96318"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96318"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96318"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96318"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96318"
FT DISULFID 37..70
FT /evidence="ECO:0000250"
FT DISULFID 113..326
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 509 AA; 56503 MW; 5939845DF2A08695 CRC64;
MVKVPHLLVA TFGVLLVLNG CLARQSLGVP PQLGNACNLD NLDVLQPTET IKSEAGRVEY
WDHNNPQIRC AGVSVSRVII EQGGLYLPTF FSSPKISYVV QGMGISGRVV PGCAETFMDS
QPMQGQQQGQ PWQGQQGQQG QQGQQGQQGQ QGQQGQQGQQ GQQGQQGQQQ QGFRDMHQKV
EHVRHGDIIA ITAGSSHWIY NTGDQPLVII CLLDIANYQN QLDRNPRTFR LAGNNPQGGS
QQQQQQQQNM LSGFDPQVLA QALKIDVRLA QELQNQQDSR GNIVRVKGPF QVVRPPLRQP
YESEQWRHPR GPPQSPQDNG LEETICSMRT HENIDDPARA DVYKPNLGRV TSVNSYTLPI
LQYIRLSATR GILQGNAMVL PKYNMNANEI LYCTQGQARI QVVNDNGQNV LDQQVQKGQL
VVIPQGFAYV VQSHQNNFEW ISFKTNANAM VSTLAGRTSA LRALPLEVIT NAFQISLEEA
RRIKFNTLET TLTRARGGQP QLIEEIVEA