CRU1_ARATH
ID CRU1_ARATH Reviewed; 472 AA.
AC P15455; Q3E711; Q56Z11; Q9FFH7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=12S seed storage protein CRA1;
DE AltName: Full=Cruciferin 1;
DE Short=AtCRU1;
DE AltName: Full=Cruciferin A1;
DE AltName: Full=Legumin-type globulin storage protein CRA1;
DE Contains:
DE RecName: Full=12S seed storage protein CRA1 alpha chain;
DE AltName: Full=12S seed storage protein CRA1 acidic chain;
DE Contains:
DE RecName: Full=12S seed storage protein CRA1 beta chain;
DE AltName: Full=12S seed storage protein CRA1 basic chain;
DE Flags: Precursor;
GN Name=CRA1; Synonyms=CRU1, CRU4; OrderedLocusNames=At5g44120;
GN ORFNames=MLN1.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX AGRICOLA=IND91035197; DOI=10.1007/BF00019521;
RA Pang P.P., Pruitt R.E., Meyerowitz E.M.;
RT "Molecular cloning, genome organization, expression and evolution of 12S
RT seed storage protein genes of Arabidopsis thaliana.";
RL Plant Mol. Biol. 11:805-820(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 126-134, AND PROTEOLYSIS.
RX PubMed=14688293; DOI=10.1105/tpc.016378;
RA Gruis D., Schulze J., Jung R.;
RT "Storage protein accumulation in the absence of the vacuolar processing
RT enzyme family of cysteine proteases.";
RL Plant Cell 16:270-290(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-472 (ISOFORM 1/2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-472 (ISOFORM 1/2).
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=12417707; DOI=10.1105/tpc.005009;
RA Gruis D.F., Selinger D.A., Curran J.M., Jung R.;
RT "Redundant proteolytic mechanisms process seed storage proteins in the
RT absence of seed-type members of the vacuolar processing enzyme family of
RT cysteine proteases.";
RL Plant Cell 14:2863-2882(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-115; TYR-312
RP AND SER-314, AND NOMENCLATURE.
RX PubMed=17313365; DOI=10.1042/bj20061569;
RA Wan L., Ross A.R., Yang J., Hegedus D.D., Kermode A.R.;
RT "Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1
RT mutant Arabidopsis thaliana (thale cress) seeds.";
RL Biochem. J. 404:247-256(2007).
RN [11]
RP PROTEOLYSIS, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=17562289; DOI=10.5483/bmbrep.2007.40.3.373;
RA Li Q., Wang B.-C., Xu Y., Zhu Y.-X.;
RT "Systematic studies of 12S seed storage protein accumulation and
RT degradation patterns during Arabidopsis seed maturation and early seedling
RT germination stages.";
RL J. Biochem. Mol. Biol. 40:373-381(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION.
RX PubMed=18768909; DOI=10.1104/pp.108.124594;
RA Ghelis T., Bolbach G., Clodic G., Habricot Y., Miginiac E., Sotta B.,
RA Jeannette E.;
RT "Protein tyrosine kinases and protein tyrosine phosphatases are involved in
RT abscisic acid-dependent processes in Arabidopsis seeds and suspension
RT cells.";
RL Plant Physiol. 148:1668-1680(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: 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 -!- SUBCELLULAR LOCATION: Protein storage vacuole {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15455-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15455-2; Sequence=VSP_026066;
CC -!- TISSUE SPECIFICITY: Accumulates in seeds 8 days after anthesis.
CC {ECO:0000269|PubMed:12417707, ECO:0000269|PubMed:17562289}.
CC -!- DEVELOPMENTAL STAGE: Detected in siliques at nucleotide level from 6
CC days post anthesis (dpa) to 17 dpa. First observed in siliques at
CC protein level 15 dpa and accumulates progressively as native isoforms
CC or proteolytic fragments during the last week of seed
CC maturation/desiccation. Present in dry seeds, essentially in cotyledons
CC and hypocotyls, but disappears during their germination (at protein
CC level). {ECO:0000269|PubMed:17562289, ECO:0000269|Ref.1}.
CC -!- PTM: Phosphorylated in seeds on some Tyr residues in response to
CC abscisic acid (ABA). {ECO:0000269|PubMed:17313365,
CC ECO:0000269|PubMed:18768909}.
CC -!- PTM: Proteolytically processed during seed maturation at a conserved
CC Asn-Gly peptide bond by an asparaginyl endopeptidase to produce two
CC mature polypeptides referred to as alpha and beta subunits that are
CC joined together 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; M37247; AAA32777.1; -; Genomic_DNA.
DR EMBL; X14312; CAA32493.1; -; Genomic_DNA.
DR EMBL; AB005239; BAB10979.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95062.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95064.1; -; Genomic_DNA.
DR EMBL; AY070730; AAL50071.1; -; mRNA.
DR EMBL; BT029491; ABL66748.1; -; mRNA.
DR EMBL; AK221158; BAD95189.1; -; mRNA.
DR EMBL; Z17590; CAA79005.1; -; mRNA.
DR PIR; S08509; S08509.
DR RefSeq; NP_199225.1; NM_123779.5. [P15455-1]
DR RefSeq; NP_851128.1; NM_180797.1. [P15455-2]
DR PDB; 7F2D; X-ray; 2.45 A; B=468-472.
DR PDB; 7F2I; X-ray; 2.35 A; B=468-472.
DR PDBsum; 7F2D; -.
DR PDBsum; 7F2I; -.
DR AlphaFoldDB; P15455; -.
DR SMR; P15455; -.
DR BioGRID; 19685; 3.
DR STRING; 3702.AT5G44120.3; -.
DR iPTMnet; P15455; -.
DR PaxDb; P15455; -.
DR PRIDE; P15455; -.
DR ProteomicsDB; 220492; -. [P15455-1]
DR EnsemblPlants; AT5G44120.2; AT5G44120.2; AT5G44120. [P15455-2]
DR EnsemblPlants; AT5G44120.3; AT5G44120.3; AT5G44120. [P15455-1]
DR GeneID; 834435; -.
DR Gramene; AT5G44120.2; AT5G44120.2; AT5G44120. [P15455-2]
DR Gramene; AT5G44120.3; AT5G44120.3; AT5G44120. [P15455-1]
DR KEGG; ath:AT5G44120; -.
DR Araport; AT5G44120; -.
DR TAIR; locus:2167654; AT5G44120.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR InParanoid; P15455; -.
DR OMA; NINTHGI; -.
DR OrthoDB; 603461at2759; -.
DR PhylomeDB; P15455; -.
DR PRO; PR:P15455; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P15455; baseline and differential.
DR Genevisible; P15455; AT.
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:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0010431; P:seed maturation; IDA:UniProtKB.
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 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Phosphoprotein; Reference proteome; Seed storage protein;
KW Signal; Storage protein; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..282
FT /note="12S seed storage protein CRA1 alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000031999"
FT CHAIN 283..472
FT /note="12S seed storage protein CRA1 beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000032000"
FT DOMAIN 41..236
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 295..444
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 259..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 312
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT DISULFID 36..69
FT /evidence="ECO:0000250"
FT DISULFID 112..289
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_026066"
FT CONFLICT 167
FT /note="E -> Q (in Ref. 1; AAA32777/CAA32493)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="V -> E (in Ref. 1; AAA32777/CAA32493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52595 MW; 700B468E4D251994 CRC64;
MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW
DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS
EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQEPLV IVSVFDLASH
QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN
QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP
SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYVTDGE
AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR
TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA
