ID   CRUA_BRANA              Reviewed;         488 AA.
AC   P11090; Q9SAP6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Cruciferin;
DE   AltName: Full=11S globulin;
DE   AltName: Full=12S storage protein;
DE   Contains:
DE     RecName: Full=Cruciferin subunit alpha;
DE   Contains:
DE     RecName: Full=Cruciferin subunit beta;
DE   Flags: Precursor;
GN   Name=CRUA; Synonyms=CRU2/3;
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].
RC   STRAIN=cv. Jet neuf; TISSUE=Seed;
RX   PubMed=2726488; DOI=10.1093/nar/17.9.3584;
RA   Shaw C.H., Ryan A.J.;
RT   "Genomic sequence of a 12S seed storage protein from oilseed rape (Brassica
RT   napus cv. jet neuf).";
RL   Nucleic Acids Res. 17:3584-3584(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   AGRICOLA=IND85080144; DOI=10.1007/BF00015683;
RA   Simon A.E., Tenbarge K.M., Scofield S.R., Finkelstein R.R., Crouch M.L.;
RT   "Nucleotide sequence of a cDNA clone of Brassica napus 12S storage protein
RT   shows homology with legumin from Pisum sativum.";
RL   Plant Mol. Biol. 5:191-201(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 379-488.
RC   STRAIN=cv. Svalofs Karat 20516-K;
RX   PubMed=2013284; DOI=10.1111/j.1432-1033.1991.tb15857.x;
RA   Sjoedahl S., Roedin J., Rask L.;
RT   "Characterization of the 12S globulin complex of Brassica napus.
RT   Evolutionary relationship to other 11-12S storage globulins.";
RL   Eur. J. Biochem. 196:617-621(1991).
RN   [4]
RP   PROTEIN SEQUENCE OF 48-74; 108-126; 299-336 AND 358-382.
RX   PubMed=2303422; DOI=10.1016/s0021-9258(19)39861-8;
RA   Roedin J., Ericson M.L., Josefsson L.-G., Rask L.;
RT   "Characterization of a cDNA clone encoding a Brassica napus 12 S protein
RT   (cruciferin) subunit. Relationship between precursors and mature chains.";
RL   J. Biol. Chem. 265:2720-2723(1990).
RN   [5]
RP   PROTEIN SEQUENCE OF 299-310, AND DISULFIDE BOND.
RX   PubMed=8223645; DOI=10.1111/j.1432-1033.1993.tb18318.x;
RA   Inquello V., Raymond J., Azanza J.L.;
RT   "Disulfide interchange reactions in 11S globulin subunits of Cruciferae
RT   seeds. Relationships to gene families.";
RL   Eur. J. Biochem. 217:891-895(1993).
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   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000305}.
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DR   EMBL; X14555; CAA32692.1; -; Genomic_DNA.
DR   EMBL; M16860; AAA32988.1; -; mRNA.
DR   EMBL; X57849; CAA40979.1; -; mRNA.
DR   PIR; S04095; B35540.
DR   AlphaFoldDB; P11090; -.
DR   SMR; P11090; -.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..23
FT   CHAIN           24..298
FT                   /note="Cruciferin subunit alpha"
FT                   /id="PRO_0000032030"
FT   CHAIN           299..488
FT                   /note="Cruciferin subunit beta"
FT                   /id="PRO_0000032031"
FT   DOMAIN          35..262
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          311..460
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          116..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        30..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..305
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000269|PubMed:8223645"
FT   CONFLICT        16
FT                   /note="T -> I (in Ref. 2; AAA32988)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="R -> K (in Ref. 2; AAA32988)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   488 AA;  53758 MW;  1268DD1CBF49B486 CRC64;
     MARLSSLLSF SLALLTFLHG STAQQFPNEC QLDQLNALEP SHVLKAEAGR IEVWDHHAPQ
     LRCSGVSFVR YIIESKGLYL PSFFSTARLS FVAKGEGLMG RVVLCAETFQ DSSVFQPSGG
     SPFGEGQGQG QQGQGQGHQG QGQGQQGQQG QQGQQSQGQG FRDMHQKVEH IRTGDTIATH
     PGVAQWFYND GNQPLVIVSV LDLASHQNQL DRNPRPFYLA GNNPQGQVWI EGREQQPQKN
     ILNGFTPEVL AKAFKIDVRT AQQLQNQQDN RGNIIRVQGP FSVIRPPLRS QRPQEEVNGL
     EETICSARCT DNLDDPSNAD VYKPQLGYIS TLNSYDLPIL RFLRLSALRG SIRQNAMVLP
     QWNANANAVL YVTDGEAHVQ VVNDNGDRVF DGQVSQGQLL SIPQGFSVVK RATSEQFRWI
     EFKTNANAQI NTLAGRTSVL RGLPLEVISN GYQISLEEAR RVKFNTIETT LTHSSGPASY
     GGPRKADA