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Protein

12S seed storage protein CRC

Gene

CRC

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seed storage protein.

GO - Molecular functioni

  • nutrient reservoir activity Source: UniProtKB

GO - Biological processi

  • cellular response to abscisic acid stimulus Source: UniProtKB
  • response to abscisic acid Source: TAIR
  • response to cytokinin Source: TAIR
  • seed maturation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Seed storage protein, Storage protein

Names & Taxonomyi

Protein namesi
Recommended name:
12S seed storage protein CRC
Alternative name(s):
Cruciferin 3
Short name:
AtCRU3
Cruciferin C
Legumin-type globulin Cruciferin1
Legumin-type globulin storage protein CRU1
Cleaved into the following 2 chains:
Alternative name(s):
12S seed storage protein CRC acidic chain
Alternative name(s):
12S seed storage protein CRC basic chain
Gene namesi
Name:CRC
Synonyms:CRU1, CRU3
Ordered Locus Names:At4g28520
ORF Names:F20O9.210
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G28520.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 33331012S seed storage protein CRC alpha chainPRO_0000399923Add
BLAST
Chaini334 – 52419112S seed storage protein CRC beta chainPRO_0000399924Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 70By similarity
Modified residuei53 – 531Phosphoserine1 Publication
Modified residuei78 – 781Phosphotyrosine1 Publication
Modified residuei97 – 971Phosphoserine1 Publication
Disulfide bondi113 ↔ 340Interchain (between alpha and beta chains)Sequence analysis
Modified residuei116 – 1161Phosphothreonine1 Publication
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei366 – 3661Phosphoserine1 Publication
Modified residuei459 – 4591Phosphothreonine1 Publication
Modified residuei484 – 4841Phosphoserine1 Publication
Modified residuei501 – 5011Phosphothreonine1 Publication

Post-translational modificationi

Ubiquitinated.1 Publication
Proteolytically processed during seed maturation at a conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to produce two mature polypeptides referred to as alpha and beta subunits that are joined together by a disulfide bond.
Phosphorylated in seeds on some Tyr residues in response to abscisic acid (ABA).2 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ96318.
PRIDEiQ96318.

PTM databases

iPTMnetiQ96318.

Expressioni

Tissue specificityi

Accumulates in seeds 8 days after anthesis.2 Publications

Developmental stagei

Detected in siliques at nucleotide level from 6 days post anthesis (dpa) to 17 dpa. First observed in siliques at protein level 12 dpa and accumulates progressively as native isoforms or proteolytic fragments during the last week of seed maturation/desiccation. Present in dry seeds, but disappears during their germination (at protein level).3 Publications

Inductioni

By abscisic acid (ABA) in an ABI3- and FUS3-dependent manner.2 Publications

Gene expression databases

ExpressionAtlasiQ96318. baseline and differential.
GenevisibleiQ96318. AT.

Interactioni

Subunit structurei

Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond.By similarity

Protein-protein interaction databases

BioGridi14257. 4 interactions.
STRINGi3702.AT4G28520.1.

Structurei

3D structure databases

ProteinModelPortaliQ96318.
SMRiQ96318. Positions 32-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi102 – 18887Gly-richAdd
BLAST
Compositional biasi121 – 295175Gln-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHSE. Eukaryota.
ENOG410YATH. LUCA.
InParanoidiQ96318.
OMAiGQPWEGQ.
PhylomeDBiQ96318.

Family and domain databases

Gene3Di2.60.120.10. 3 hits.
InterProiIPR022379. 11S_seedstore_CS.
IPR006044. 11S_seedstore_pln.
IPR006045. Cupin_1.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 2 hits.
[Graphical view]
PRINTSiPR00439. 11SGLOBULIN.
SMARTiSM00835. Cupin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 2 hits.
PROSITEiPS00305. 11S_SEED_STORAGE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96318-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVKLSNLLVA TFGVLLVLNG CLARQSLGVP PQLQNECNLD NLDVLQATET
60 70 80 90 100
IKSEAGQIEY WDHNHPQLRC VGVSVARYVI EQGGLYLPTF FTSPKISYVV
110 120 130 140 150
QGTGISGRVV PGCAETFMDS QPMQGQQQGQ PWQGRQGQQG QPWEGQGQQG
160 170 180 190 200
QQGRQGQPWE GQGQQGQQGR QGQQGQPWEG QGQQGQQGFR DMHQKVEHVR
210 220 230 240 250
RGDVFANTPG SAHWIYNSGE QPLVIIALLD IANYQNQLDR NPRVFHLAGN
260 270 280 290 300
NQQGGFGGSQ QQQEQKNLWS GFDAQVIAQA LKIDVQLAQQ LQNQQDSRGN
310 320 330 340 350
IVRVKGPFQV VRPPLRQPYE SEEWRHPRSP QGNGLEETIC SMRSHENIDD
360 370 380 390 400
PARADVYKPS LGRVTSVNSY TLPILEYVRL SATRGVLQGN AMVLPKYNMN
410 420 430 440 450
ANEILYCTGG QGRIQVVNDN GQNVLDQQVQ KGQLVVIPQG FAYVVQSHGN
460 470 480 490 500
KFEWISFKTN ENAMISTLAG RTSLLRALPL EVISNGFQIS PEEARKIKFN
510 520
TLETTLTRAA GRQQQQLIEE IVEA
Length:524
Mass (Da):58,235
Last modified:February 1, 1997 - v1
Checksum:i6C5C2DFB28B143E3
GO
Isoform 2 (identifier: Q96318-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     204-221: VFANTPGSAHWIYNSGEQ → GIAIGGHIKWFPDLSRGS
     222-524: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:221
Mass (Da):24,285
Checksum:iB80580294C57A6C6
GO
Isoform 3 (identifier: Q96318-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     390-396: NAMVLPK → VKCDGAS
     397-524: Missing.

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:396
Mass (Da):43,879
Checksum:i5EC58D412627C3A3
GO
Isoform 4 (identifier: Q96318-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     389-394: GNAMVL → ECDGAS
     395-524: Missing.

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:394
Mass (Da):43,724
Checksum:i108650EE4FD054C9
GO

Sequence cautioni

The sequence BAD95275.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAH56848.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211C → S in CAA79027 (Ref. 6) Curated
Sequence conflicti174 – 1741Q → H in AAL91248 (PubMed:14593172).Curated
Sequence conflicti174 – 1741Q → H in AAN72284 (PubMed:14593172).Curated
Isoform 2 (identifier: Q96318-2)
Sequence conflicti204 – 2041G → V in BAH56848 (PubMed:19423640).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 15313Missing in strain: cv. Mr-0. 1 Publication
Add
BLAST
Natural varianti170 – 1701R → Q in strain: cv. Mr-0. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei204 – 22118VFANT…NSGEQ → GIAIGGHIKWFPDLSRGS in isoform 2. 1 PublicationVSP_039933Add
BLAST
Alternative sequencei222 – 524303Missing in isoform 2. 1 PublicationVSP_039934Add
BLAST
Alternative sequencei389 – 3946GNAMVL → ECDGAS in isoform 4. CuratedVSP_039935
Alternative sequencei390 – 3967NAMVLPK → VKCDGAS in isoform 3. CuratedVSP_039936
Alternative sequencei395 – 524130Missing in isoform 4. CuratedVSP_039937Add
BLAST
Alternative sequencei397 – 524128Missing in isoform 3. CuratedVSP_039938Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66916 Genomic DNA. Translation: AAB17379.1.
AL021749 Genomic DNA. Translation: CAA16892.1.
AL161573 Genomic DNA. Translation: CAB81440.1.
CP002687 Genomic DNA. Translation: AEE85497.1.
CP002687 Genomic DNA. Translation: AEE85498.1.
CP002687 Genomic DNA. Translation: AEE85500.1.
AY090342 mRNA. Translation: AAL91248.1.
BT002273 mRNA. Translation: AAN72284.1.
Z17659 mRNA. Translation: CAA79027.1.
Z17616 mRNA. Translation: CAA79014.1.
Z27261 mRNA. Translation: CAA81772.1.
AK318733 mRNA. Translation: BAH56848.1. Different initiation.
AK221187 mRNA. Translation: BAD95275.1. Different initiation.
PIRiT04623.
RefSeqiNP_001078459.1. NM_001084990.1. [Q96318-3]
NP_194581.1. NM_118994.4. [Q96318-1]
NP_849464.1. NM_179133.1. [Q96318-4]
UniGeneiAt.21702.

Genome annotation databases

EnsemblPlantsiAT4G28520.1; AT4G28520.1; AT4G28520. [Q96318-1]
GeneIDi828970.
KEGGiath:AT4G28520.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66916 Genomic DNA. Translation: AAB17379.1.
AL021749 Genomic DNA. Translation: CAA16892.1.
AL161573 Genomic DNA. Translation: CAB81440.1.
CP002687 Genomic DNA. Translation: AEE85497.1.
CP002687 Genomic DNA. Translation: AEE85498.1.
CP002687 Genomic DNA. Translation: AEE85500.1.
AY090342 mRNA. Translation: AAL91248.1.
BT002273 mRNA. Translation: AAN72284.1.
Z17659 mRNA. Translation: CAA79027.1.
Z17616 mRNA. Translation: CAA79014.1.
Z27261 mRNA. Translation: CAA81772.1.
AK318733 mRNA. Translation: BAH56848.1. Different initiation.
AK221187 mRNA. Translation: BAD95275.1. Different initiation.
PIRiT04623.
RefSeqiNP_001078459.1. NM_001084990.1. [Q96318-3]
NP_194581.1. NM_118994.4. [Q96318-1]
NP_849464.1. NM_179133.1. [Q96318-4]
UniGeneiAt.21702.

3D structure databases

ProteinModelPortaliQ96318.
SMRiQ96318. Positions 32-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14257. 4 interactions.
STRINGi3702.AT4G28520.1.

PTM databases

iPTMnetiQ96318.

Proteomic databases

PaxDbiQ96318.
PRIDEiQ96318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G28520.1; AT4G28520.1; AT4G28520. [Q96318-1]
GeneIDi828970.
KEGGiath:AT4G28520.

Organism-specific databases

TAIRiAT4G28520.

Phylogenomic databases

eggNOGiENOG410IHSE. Eukaryota.
ENOG410YATH. LUCA.
InParanoidiQ96318.
OMAiGQPWEGQ.
PhylomeDBiQ96318.

Miscellaneous databases

PROiQ96318.

Gene expression databases

ExpressionAtlasiQ96318. baseline and differential.
GenevisibleiQ96318. AT.

Family and domain databases

Gene3Di2.60.120.10. 3 hits.
InterProiIPR022379. 11S_seedstore_CS.
IPR006044. 11S_seedstore_pln.
IPR006045. Cupin_1.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 2 hits.
[Graphical view]
PRINTSiPR00439. 11SGLOBULIN.
SMARTiSM00835. Cupin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 2 hits.
PROSITEiPS00305. 11S_SEED_STORAGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two naturally occurring deletion mutants of 12S seed storage proteins in Arabidopsis thaliana."
    Hou A., Liu K., Catawatcharakul N., Tang X., Nguyen V., Keller W.A., Tsang E.W., Cui Y.
    Planta 222:512-520(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, VARIANTS 141-GLN--GLY-153 DEL AND GLN-170.
    Strain: cv. Columbia and cv. Mr-0.
  2. "Characterization of a cruciferin-deficient mutant of Arabidopsis."
    McCourt P., Ferraioli G., Riggs C.D.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  6. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
    Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154; 227-341 AND 431-524 (ISOFORM 1).
    Strain: cv. Columbia.
    Tissue: Seed and Silique.
  7. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-221 (ISOFORM 2).
    Strain: cv. Columbia.
    Tissue: Flower and Silique.
  8. "Storage protein accumulation in the absence of the vacuolar processing enzyme family of cysteine proteases."
    Gruis D., Schulze J., Jung R.
    Plant Cell 16:270-290(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-33 AND 323-331, PROTEIN SEQUENCE OF N-TERMINUS, PROTEOLYSIS.
  9. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 385-524 (ISOFORM 1).
    Strain: cv. Columbia.
  10. "Molecular cloning, genomic organization, expression and evolution of 12S seed storage protein."
    Pang P.P., Pruitt R.E., Meyerowitz E.M.
    Plant Mol. Biol. 11:805-820(1988)
    Cited for: DEVELOPMENTAL STAGE.
  11. "Regulation of gene expression programs during Arabidopsis seed development: roles of the ABI3 locus and of endogenous abscisic acid."
    Parcy F., Valon C., Raynal M., Gaubier-Comella P., Delseny M., Giraudat J.
    Plant Cell 6:1567-1582(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, INDUCTION BY ABSCISIC ACID.
  12. "Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases."
    Gruis D.F., Selinger D.A., Curran J.M., Jung R.
    Plant Cell 14:2863-2882(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  13. "Indirect ABA-dependent regulation of seed storage protein genes by FUSCA3 transcription factor in Arabidopsis."
    Kagaya Y., Okuda R., Ban A., Toyoshima R., Tsutsumida K., Usui H., Yamamoto A., Hattori T.
    Plant Cell Physiol. 46:300-311(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY ABSCISIC ACID.
  14. "Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds."
    Wan L., Ross A.R., Yang J., Hegedus D.D., Kermode A.R.
    Biochem. J. 404:247-256(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-53; TYR-78; SER-97; THR-116; SER-259; SER-366; THR-459; SER-484 AND THR-501, NOMENCLATURE.
  15. "Systematic studies of 12S seed storage protein accumulation and degradation patterns during Arabidopsis seed maturation and early seedling germination stages."
    Li Q., Wang B.-C., Xu Y., Zhu Y.-X.
    J. Biochem. Mol. Biol. 40:373-381(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYSIS, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  16. "Protein tyrosine kinases and protein tyrosine phosphatases are involved in abscisic acid-dependent processes in Arabidopsis seeds and suspension cells."
    Ghelis T., Bolbach G., Clodic G., Habricot Y., Miginiac E., Sotta B., Jeannette E.
    Plant Physiol. 148:1668-1680(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION.
  17. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  18. "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
    Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
    Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCRU3_ARATH
AccessioniPrimary (citable) accession number: Q96318
Secondary accession number(s): A8MRV6
, C0Z2B9, Q41905, Q41913, Q42181, Q56YY3, Q8RX74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: February 1, 1997
Last modified: April 13, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.