ID   CRU2_BRANA              Reviewed;         496 AA.
AC   P33524;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cruciferin BnC2;
DE   AltName: Full=11S globulin;
DE   AltName: Full=12S storage protein;
DE   Contains:
DE     RecName: Full=Cruciferin BnC2 subunit alpha;
DE   Contains:
DE     RecName: Full=Cruciferin BnC2 subunit beta;
DE   Flags: Precursor;
GN   Name=BnC2;
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. Tower;
RX   PubMed=1511129; DOI=10.1007/bf00040536;
RA   Breen J.P., Crouch M.L.;
RT   "Molecular analysis of a cruciferin storage protein gene family of Brassica
RT   napus.";
RL   Plant Mol. Biol. 19:1049-1055(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X59295; CAA41985.1; -; Genomic_DNA.
DR   PIR; S25091; S25091.
DR   AlphaFoldDB; P33524; -.
DR   SMR; P33524; -.
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; Seed storage protein; Signal;
KW   Storage protein.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..306
FT                   /note="Cruciferin BnC2 subunit alpha"
FT                   /id="PRO_0000032034"
FT   CHAIN           307..496
FT                   /note="Cruciferin BnC2 subunit beta"
FT                   /id="PRO_0000032035"
FT   DOMAIN          35..269
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          319..468
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          114..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15456"
FT   MOD_RES         336
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P15456"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15455"
FT   MOD_RES         432
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15456"
FT   DISULFID        30..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        106..313
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   496 AA;  54291 MW;  0E2A5292E7EDE85F CRC64;
     MARLSSLLYF SITVLIFLHG STAQQFPNEC QLDQLNALEP SHVLKAEAGR IEVWDHHAPQ
     LRCSGVSFVR YIIESQGLYL PSFLNTANVS FVAKGQGLMG RVVPGCAETF QDSSVFQPGS
     GSPFGEGQGQ GQQGQGQGQG QGQGKGQQGQ GKGQQGQSQG QQGQGQGFRD MHQKVEHIRS
     GDTIATHPGV AQWFYNNGNQ PLVIVAVMDL ASHQNQLDRN PSQFYLAGKN PQGQSWLHGR
     GQQPQNNILN GFSPEVLAQA FKIDVRTAQQ LQNQQDNRGN IVRVQGPFGV IRPPLKSQRP
     QETEANGLEE TICSARCTDN LDDPSNADVY KPQLGYISIL NSYDLPILRV LRLSALRGSI
     RQNAMVLPQW KSKSNAVLYV TDGEAQIQVV NDNGDRVFDG QVSQGQLLSI PQGFSVVKRA
     TSDQFRWIEF KTNANAQINT LAGRTSVMRG LPLEVIANGY QISLEEARRV KFNTIETTLT
     HSSGPASYGR PRKADA