CRU4_BRANA
ID CRU4_BRANA Reviewed; 465 AA.
AC P33522;
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 CRU4;
DE AltName: Full=11S globulin;
DE AltName: Full=12S storage protein;
DE Contains:
DE RecName: Full=Cruciferin CRU4 alpha chain;
DE Contains:
DE RecName: Full=Cruciferin CRU4 beta chain;
DE Flags: Precursor;
GN Name=CRU4;
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 [MRNA].
RC STRAIN=cv. Svalofs Karat 20516-K; TISSUE=Seed;
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 [2]
RP PROTEIN SEQUENCE OF 108-119; 139-153; 277-308; 336-360 AND 372-395.
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).
CC -!- FUNCTION: This is a seed storage protein.
CC -!- SUBUNIT: Heterohexamer; each subunit is composed of an acidic and a
CC basic chain derived from a single precursor and linked by a disulfide
CC 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; X57848; CAA40978.1; -; mRNA.
DR EMBL; X57850; CAA40980.1; -; mRNA.
DR EMBL; X57851; CAA40981.1; -; mRNA.
DR PIR; S14762; S14762.
DR AlphaFoldDB; P33522; -.
DR SMR; P33522; -.
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 Phosphoprotein; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..276
FT /note="Cruciferin CRU4 alpha chain"
FT /id="PRO_0000032038"
FT CHAIN 277..465
FT /note="Cruciferin CRU4 beta chain"
FT /id="PRO_0000032039"
FT DOMAIN 34..236
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 289..438
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 112..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 306
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT DISULFID 29..62
FT /evidence="ECO:0000250"
FT DISULFID 105..283
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
FT VARIANT 110
FT /note="N -> M"
FT VARIANT 147
FT /note="S -> H"
FT VARIANT 359
FT /note="N -> M"
FT VARIANT 374
FT /note="K -> Q"
SQ SEQUENCE 465 AA; 51377 MW; ECC51AFEB30CC8D2 CRC64;
MGPTSLLSFF FTFLTLFHGF TAQQWPNECQ LDQLNALEPS QIIKSEGGRI EVWDHHAPQL
RCSGFAFERF VIEPQGLYLP TFLNAGKLTF VVHGHALMGK VTPGCAETFN DSPVFGQGQG
QEQGQGQGQG QGQGFRDMHQ KVEHLRSGDT IATPPGVAQW FYNNGNEPLI LVAAADIANN
LNQLDRNLRP FLLAGNNPQG QQWLQGRQQQ KQNNIFNGFA PQILAQAFKI SVETAQKLQN
QQVNRGNIVK VQGQFGVIRP PLRQGQGGQQ PQEEGNGLEE TLCTMRCTEN LDDPSSADVY
KPSLGYISTL NSYNLPILRF LRLSALRGSI HNNAMVLPQW NVNANAALYV TKGKAHIQNV
NDNGQRVFDQ EISKGQLLVV PQGFAVVKRA TSQQFQWIEF KSNDNAQINT LAGRTSVMRG
LPLEVISNGY QISPQEARSV KFSTLETTLT QSSGPMGYGM PRVEA
