CRU2_ARATH
ID CRU2_ARATH Reviewed; 455 AA.
AC P15456; Q56WH8; Q9SAW0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=12S seed storage protein CRB;
DE AltName: Full=Cruciferin 2;
DE Short=AtCRU2;
DE AltName: Full=Cruciferin B;
DE AltName: Full=Legumin-type globulin storage protein CRU2;
DE Contains:
DE RecName: Full=12S seed storage protein CRB alpha chain;
DE AltName: Full=12S seed storage protein CRB acidic chain;
DE Contains:
DE RecName: Full=12S seed storage protein CRB beta chain;
DE AltName: Full=12S seed storage protein CRB basic chain;
DE Flags: Precursor;
GN Name=CRB; Synonyms=CRU2, CRU3; OrderedLocusNames=At1g03880;
GN ORFNames=F21M11.19;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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] OF 240-360.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 269-455.
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-109; TYR-299;
RP SER-367; THR-395; THR-420 AND SER-436, 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 [9]
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 [10]
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).
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 -!- 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 12 dpa and accumulates progressively as native isoforms
CC or proteolytic fragments during the last week of seed
CC maturation/desiccation. Present in dry seeds, but disappears during
CC their germination (at protein level). {ECO:0000269|PubMed:17562289,
CC ECO:0000269|Ref.1}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94859.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M37248; AAA32778.1; -; Genomic_DNA.
DR EMBL; X14313; CAA32494.1; -; Genomic_DNA.
DR EMBL; AC003027; AAD10680.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27628.1; -; Genomic_DNA.
DR EMBL; AY093005; AAM13004.1; -; mRNA.
DR EMBL; BT009682; AAP81800.1; -; mRNA.
DR EMBL; Z17654; CAA79024.1; -; mRNA.
DR EMBL; AK222062; BAD94859.1; ALT_INIT; mRNA.
DR PIR; E86169; E86169.
DR PIR; S08510; S08510.
DR RefSeq; NP_171884.1; NM_100268.5.
DR AlphaFoldDB; P15456; -.
DR SMR; P15456; -.
DR STRING; 3702.AT1G03880.1; -.
DR iPTMnet; P15456; -.
DR PaxDb; P15456; -.
DR PRIDE; P15456; -.
DR ProteomicsDB; 222679; -.
DR EnsemblPlants; AT1G03880.1; AT1G03880.1; AT1G03880.
DR GeneID; 839383; -.
DR Gramene; AT1G03880.1; AT1G03880.1; AT1G03880.
DR KEGG; ath:AT1G03880; -.
DR Araport; AT1G03880; -.
DR TAIR; locus:2024234; AT1G03880.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR HOGENOM; CLU_026341_2_0_1; -.
DR InParanoid; P15456; -.
DR OMA; CTIKARI; -.
DR OrthoDB; 603461at2759; -.
DR PhylomeDB; P15456; -.
DR PRO; PR:P15456; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P15456; baseline and differential.
DR Genevisible; P15456; 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 Disulfide bond; Phosphoprotein; Reference proteome; Seed storage protein;
KW Signal; Storage protein; Ubl conjugation; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..269
FT /note="12S seed storage protein CRB alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000032001"
FT CHAIN 270..455
FT /note="12S seed storage protein CRB beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000032002"
FT DOMAIN 35..229
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 282..431
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 299
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 420
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT DISULFID 30..63
FT /evidence="ECO:0000250"
FT DISULFID 106..276
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
FT CONFLICT 383
FT /note="A -> R (in Ref. 1; AAA32778/CAA32494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 50558 MW; BE24BCBD2F69B538 CRC64;
MGRVSSIISF SLTLLILFNG YTAQQWPNEC QLDQLNALEP SQIIKSEGGR IEVWDHHAPQ
LRCSGFAFER FVIEPQGLFL PTFLNAGKLT FVVHGRGLMG RVIPGCAETF MESPVFGEGQ
GQGQSQGFRD MHQKVEHLRC GDTIATPSGV AQWFYNNGNE PLILVAAADL ASNQNQLDRN
LRPFLIAGNN PQGQEWLQGR KQQKQNNIFN GFAPEILAQA FKINVETAQQ LQNQQDNRGN
IVKVNGPFGV IRPPLRRGEG GQQPHEIANG LEETLCTMRC TENLDDPSDA DVYKPSLGYI
STLNSYNLPI LRLLRLSALR GSIRKNAMVL PQWNVNANAA LYVTNGKAHI QMVNDNGERV
FDQEISSGQL LVVPQGFSVM KHAIGEQFEW IEFKTNENAQ VNTLAGRTSV MRGLPLEVIT
NGYQISPEEA KRVKFSTIET TLTHSSPMSY GRPRA
