CRU1_BRANA
ID CRU1_BRANA Reviewed; 490 AA.
AC P33523;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cruciferin BnC1;
DE AltName: Full=11S globulin;
DE AltName: Full=12S storage protein;
DE Contains:
DE RecName: Full=Cruciferin BnC1 subunit alpha;
DE Contains:
DE RecName: Full=Cruciferin BnC1 subunit beta;
DE Flags: Precursor;
GN Name=BnC1;
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}.
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DR EMBL; X59294; CAA41984.1; -; Genomic_DNA.
DR AlphaFoldDB; P33523; -.
DR SMR; P33523; -.
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..300
FT /note="Cruciferin BnC1 subunit alpha"
FT /id="PRO_0000032032"
FT CHAIN 301..490
FT /note="Cruciferin BnC1 subunit beta"
FT /id="PRO_0000032033"
FT DOMAIN 35..263
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 313..462
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 113..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 330
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT DISULFID 30..63
FT /evidence="ECO:0000250"
FT DISULFID 106..307
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 53824 MW; 63BEE04AD8FE7080 CRC64;
MARLSSLLSF SLALLIFLHG STAQQFPNEC QLDQLNALEP SHVLKAEAGR IEVWDHHAPQ
LRCSGVSFVR YIIESKGLYL PSFFSTAKLS FVAKGEGLMG RVVPGCAETF QDSSVFQPSG
GSPSGEGQGQ GQQGQGQGHQ GQGQGQQGQQ GQQGQQSQGQ GFRDMHQKVE HIRTGDTIAT
HPGVAQWFYN DGNQPLVIVS VLDLASHQNQ LDRNPRPFYL AGNNPQGQVW IEGREQQPQK
NILNGFTPEV LAKAFKIDVR TAQQLQNQQD NRGNIIRVQG PFSVIRPPLR SQRPQETEVN
GLEETICSAR CTDNLDDPSN ADVYKPQLGY ISTLNSYDLP ILRFLRLSAL RGSIRQNAMV
LPQWNANANA VLYVTDGEAH VQVVNDNGDR VFDGQVSQGQ LLSIPQGFSV VKRATSEQFR
WIEFKTNANA QINTLAGRTS VLRGLPLEVI SNGYQISLEE ARRVKFNTIE TTLTHSSGPA
SYGGPRKADA
