CRU4_ARATH
ID CRU4_ARATH Reviewed; 451 AA.
AC Q9ZWA9; Q67ZY3;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=12S seed storage protein CRD;
DE AltName: Full=Cruciferin D;
DE AltName: Full=Legumin-type globulin storage protein CRD;
DE Contains:
DE RecName: Full=12S seed storage protein CRD alpha chain;
DE AltName: Full=12S seed storage protein CRD acidic chain;
DE Contains:
DE RecName: Full=12S seed storage protein CRD beta chain;
DE AltName: Full=12S seed storage protein CRD basic chain;
DE Flags: Precursor;
GN Name=CRD; Synonyms=CRU2; OrderedLocusNames=At1g03890; ORFNames=F21M11.18;
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 [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 [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 26-32, PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION
RP 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 [5]
RP PROTEIN SEQUENCE OF 26-33, PROTEIN SEQUENCE OF N-TERMINUS, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-451.
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-39, AND
RP 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 [8]
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).
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: First observed in siliques 15 days post anthesis
CC and accumulates progressively as native isoforms or proteolytic
CC fragments during the last week of seed maturation/desiccation. Present
CC in dry seeds, but disappears during their germination (at protein
CC level). {ECO:0000269|PubMed:17562289}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
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DR EMBL; AC003027; AAD10679.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27629.1; -; Genomic_DNA.
DR EMBL; AY065432; AAL38873.1; -; mRNA.
DR EMBL; AY117228; AAM51303.1; -; mRNA.
DR EMBL; AK175984; BAD43747.1; -; mRNA.
DR PIR; F86169; F86169.
DR RefSeq; NP_171885.1; NM_100269.4.
DR AlphaFoldDB; Q9ZWA9; -.
DR SMR; Q9ZWA9; -.
DR STRING; 3702.AT1G03890.1; -.
DR iPTMnet; Q9ZWA9; -.
DR PaxDb; Q9ZWA9; -.
DR PRIDE; Q9ZWA9; -.
DR ProteomicsDB; 222727; -.
DR EnsemblPlants; AT1G03890.1; AT1G03890.1; AT1G03890.
DR GeneID; 839379; -.
DR Gramene; AT1G03890.1; AT1G03890.1; AT1G03890.
DR KEGG; ath:AT1G03890; -.
DR Araport; AT1G03890; -.
DR TAIR; locus:2024219; AT1G03890.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR HOGENOM; CLU_026341_2_0_1; -.
DR InParanoid; Q9ZWA9; -.
DR OMA; QRPSWET; -.
DR OrthoDB; 603461at2759; -.
DR PhylomeDB; Q9ZWA9; -.
DR PRO; PR:Q9ZWA9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWA9; baseline and differential.
DR Genevisible; Q9ZWA9; 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:0010431; P:seed maturation; IDA:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Phosphoprotein;
KW Reference proteome; Seed storage protein; Signal; Storage protein;
KW Ubl conjugation; Vacuole.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:12417707,
FT ECO:0000269|PubMed:14688293"
FT CHAIN 27..270
FT /note="12S seed storage protein CRD alpha chain"
FT /id="PRO_0000399925"
FT CHAIN 271..451
FT /note="12S seed storage protein CRD beta chain"
FT /id="PRO_0000399926"
FT DOMAIN 42..234
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 283..432
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15455"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15456"
FT DISULFID 36..69
FT /evidence="ECO:0000250"
FT DISULFID 112..277
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
FT CONFLICT 382
FT /note="K -> R (in Ref. 6; BAD43747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 49675 MW; 456BA2B5BE8BB9B0 CRC64;
MHKLLFSLLS VVSLSFLLFF HGAEARQREA PFPNACHFSQ INSLAPAQAT KFEAGQMEVW
DHMSPELRCA GVTVARITLQ PNSIFLPAFF SPPALAYVVQ GEGVMGTIAS GCPETFAEVE
GSSGRGGGGD PGRRFEDMHQ KLENFRRGDV FASLAGVSQW WYNRGDSDAV IVIVLDVTNR
ENQLDQVPRM FQLAGSRTQE EEQPLTWPSG NNAFSGFDPN IIAEAFKINI ETAKQLQNQK
DNRGNIIRAN GPLHFVIPPP REWQQDGIAN GIEETYCTAK IHENIDDPER SDHFSTRAGR
ISTLNSLNLP VLRLVRLNAL RGYLYSGGMV LPQWTANAHT VLYVTGGQAK IQVVDDNGQS
VFNEQVGQGQ IIVIPQGFAV SKTAGETGFE WISFKTNDNA YINTLSGQTS YLRAVPVDVI
KASYGVNEEE AKRIKFSQQE TMLSMTPSSS S
