(data stored in ACNUC5340 zone)

HOGENOM: ARATH_4_PE3686

ID   ARATH_4_PE3686                       STANDARD;      PRT;   524 AA.
AC   ARATH_4_PE3686;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=12S seed storage protein CRU1;AltName: Full=Cruciferin 1;
DE   Short=AtCRU1;AltName: Full=Cruciferin C;AltName: Full=Legumin-type
DE   globulin storage protein CRU1;Contains: RecName: Full=Cruciferin CRU1
DE   alpha chain;Contains: RecName: Full=Cruciferin CRU1 beta chain;Flags:
DE   Precursor; (ARATH_4.PE3686).
GN   Name=CRU1; Synonyms=CRC, CRU3; OrderedLocusNames=At4g28520;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_4.PE3686.
CC       Arabidopsis thaliana chromosome 4 TAIR10 full sequence 1..18585056
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:CRU1_ARATH
CC   -!- FUNCTION: Seed storage protein.
CC   -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a
CC       basic chain derived from a single precursor and linked by a
CC       disulfide bond (By similarity).
CC   -!- SUBCELLULAR LOCATION: Protein storage vacuole (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q96318-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96318-2; Sequence=VSP_039933, VSP_039934;
CC         Note=Ref.7 (BAH56848) sequence is in conflict in position:
CC         204:G->V. No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q96318-3; Sequence=VSP_039936, VSP_039938;
CC         Note=Derived from EST data. No experimental confirmation
CC         available;
CC       Name=4;
CC         IsoId=Q96318-4; Sequence=VSP_039935, VSP_039937;
CC         Note=Derived from EST data. No experimental confirmation
CC         available;
CC   -!- TISSUE SPECIFICITY: Accumulates in seeds 8 days after anthesis.
CC   -!- DEVELOPMENTAL STAGE: Detected in siliques at nucleotide level from
CC       6 days post anthesis (dpa) to 17 dpa. First observed in siliques
CC       at protein level 12 dpa and accumulates progressively as native
CC       isoforms or proteolytic fragments during the last week of seed
CC       maturation/desiccation. Present in dry seeds, but disapears during
CC       their germination (at protein level).
CC   -!- INDUCTION: By abscisic acid (ABA) in an ABI3- and FUS3-dependent
CC       manner.
CC   -!- PTM: Ubiquitinated.
CC   -!- PTM: Proteolytically processed during seed maturation at a
CC       conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to
CC       produce two mature polypeptides referred to as alpha and beta
CC       subunits that are joined together by a disulfide bond.
CC   -!- PTM: Phosphorylated in seeds on some Tyr residues in response to
CC       abscisic acid (ABA).
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins)
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD95275.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAH56848.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -!- GENE_FAMILY: HOG000217279 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT4G28520;AT4G28520.1;AT4G28520.1.
DR   EMBL; AK221187; - ;
DR   EMBL; AK318733; - ;
DR   EMBL; AL021749; - ;
DR   EMBL; AL161573; - ;
DR   EMBL; AY090342; - ;
DR   EMBL; BT002273; - ;
DR   EMBL; U66916; - ;
DR   EMBL; Z17616; - ;
DR   EMBL; Z17659; - ;
DR   EMBL; Z27261; - ;
DR   UniProtKB/Swiss-Prot; Q96318; A8MRV6; C0Z2B9; Q41905; Q41913; Q42181; Q56YY3; Q8RX74; -.
DR   EMBL; U66916; AAB17379.1; -; Genomic_DNA.
DR   EMBL; AL021749; CAA16892.1; -; Genomic_DNA.
DR   EMBL; AL161573; CAB81440.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85497.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85498.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85500.1; -; Genomic_DNA.
DR   EMBL; AY090342; AAL91248.1; -; mRNA.
DR   EMBL; BT002273; AAN72284.1; -; mRNA.
DR   EMBL; Z17659; CAA79027.1; -; mRNA.
DR   EMBL; Z17616; CAA79014.1; -; mRNA.
DR   EMBL; Z27261; CAA81772.1; -; mRNA.
DR   EMBL; AK318733; BAH56848.1; ALT_INIT; mRNA.
DR   EMBL; AK221187; BAD95275.1; ALT_INIT; mRNA.
DR   IPI; IPI00521539; -.
DR   IPI; IPI00543385; -.
DR   IPI; IPI00846782; -.
DR   IPI; IPI00971326; -.
DR   PIR; T04623; T04623.
DR   RefSeq; NP_001078459.1; NM_001084990.1.
DR   RefSeq; NP_194581.1; NM_118994.4.
DR   RefSeq; NP_849464.1; NM_179133.1.
DR   UniGene; At.21702; -.
DR   UniGene; At.74816; -.
DR   HSSP; P04776; 1FXZ.
DR   ProteinModelPortal; Q96318; -.
DR   SMR; Q96318; 32-510.
DR   STRING; Q96318; -.
DR   PRIDE; Q96318; -.
DR   ProMEX; Q96318; -.
DR   EnsemblPlants; AT4G28520.1; AT4G28520.1; AT4G28520.
DR   GeneID; 828970; -.
DR   GenomeReviews; CT486007_GR; AT4G28520.
DR   KEGG; ath:AT4G28520; -.
DR   NMPDR; fig|3702.1.peg.20810; -.
DR   TAIR; At4g28520; -.
DR   GeneTree; EPGT00050000006653; -.
DR   InParanoid; Q96318; -.
DR   OMA; GQPWEGQ; -.
DR   ProtClustDB; CLSN2680133; -.
DR   ArrayExpress; Q96318; -.
DR   Genevestigator; Q96318; -.
DR   GO; GO:0000326; C:protein storage vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0045735; F:nutrient reservoir activity; IDA:UniProtKB.
DR   GO; GO:0071215; P:cellular response to abscisic acid stimulus; IDA:UniProtKB.
DR   GO; GO:0010431; P:seed maturation; IDA:UniProtKB.
DR   InterPro; IPR022379; 11S_seedstore_CS.
DR   InterPro; IPR006044; 11S_seedstore_pln.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR011051; Cupin_RmlC_type.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 3.
DR   Pfam; PF00190; Cupin_1; 2.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; RmlC_like_cupin; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
DR   HOGENOMDNA; ARATH_4.PE3686; -.
KW   AT4G28520pg.C_scaffold_1320000031; AT4G28520.1.C_scaffold_1320000031;
KW   AK221187; AK318733; AL021749; AL161573; AY090342; BT002273; U66916;
KW   Z17659; Z27261;
KW   Alternative splicing; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Phosphoprotein; Reference proteome;
KW   Seed storage protein; Signal; Storage protein; Ubl conjugation;
KW   Vacuole.
SQ   SEQUENCE   524 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVKLSNLLVA TFGVLLVLNG CLARQSLGVP PQLQNECNLD NLDVLQATET IKSEAGQIEY
     WDHNHPQLRC VGVSVARYVI EQGGLYLPTF FTSPKISYVV QGTGISGRVV PGCAETFMDS
     QPMQGQQQGQ PWQGRQGQQG QPWEGQGQQG QQGRQGQPWE GQGQQGQQGR QGQQGQPWEG
     QGQQGQQGFR DMHQKVEHVR RGDVFANTPG SAHWIYNSGE QPLVIIALLD IANYQNQLDR
     NPRVFHLAGN NQQGGFGGSQ QQQEQKNLWS GFDAQVIAQA LKIDVQLAQQ LQNQQDSRGN
     IVRVKGPFQV VRPPLRQPYE SEEWRHPRSP QGNGLEETIC SMRSHENIDD PARADVYKPS
     LGRVTSVNSY TLPILEYVRL SATRGVLQGN AMVLPKYNMN ANEILYCTGG QGRIQVVNDN
     GQNVLDQQVQ KGQLVVIPQG FAYVVQSHGN KFEWISFKTN ENAMISTLAG RTSLLRALPL
     EVISNGFQIS PEEARKIKFN TLETTLTRAA GRQQQQLIEE IVEA
//

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