CRU3_ARATH
ID CRU3_ARATH Reviewed; 524 AA.
AC Q96318; A8MRV6; C0Z2B9; Q41905; Q41913; Q42181; Q56YY3; Q8RX74;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=12S seed storage protein CRC;
DE AltName: Full=Cruciferin 3;
DE Short=AtCRU3;
DE AltName: Full=Cruciferin C;
DE AltName: Full=Legumin-type globulin Cruciferin1;
DE AltName: Full=Legumin-type globulin storage protein CRU1;
DE Contains:
DE RecName: Full=12S seed storage protein CRC alpha chain;
DE AltName: Full=12S seed storage protein CRC acidic chain;
DE Contains:
DE RecName: Full=12S seed storage protein CRC beta chain;
DE AltName: Full=12S seed storage protein CRC basic chain;
DE Flags: Precursor;
GN Name=CRC; Synonyms=CRU1, CRU3; OrderedLocusNames=At4g28520;
GN ORFNames=F20O9.210;
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP VARIANTS 141-GLN--GLY-153 DEL AND GLN-170.
RC STRAIN=cv. Columbia, and cv. Mr-0;
RX PubMed=15912356; DOI=10.1007/s00425-005-1555-z;
RA Hou A., Liu K., Catawatcharakul N., Tang X., Nguyen V., Keller W.A.,
RA Tsang E.W., Cui Y.;
RT "Two naturally occurring deletion mutants of 12S seed storage proteins in
RT Arabidopsis thaliana.";
RL Planta 222:512-520(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA McCourt P., Ferraioli G., Riggs C.D.;
RT "Characterization of a cruciferin-deficient mutant of Arabidopsis.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154; 227-341 AND 431-524
RP (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Seed, and Silique;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-221 (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
RP PROTEIN SEQUENCE OF 24-33 AND 323-331, PROTEIN SEQUENCE OF N-TERMINUS, AND
RP 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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 385-524 (ISOFORM 1).
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 [10]
RP DEVELOPMENTAL STAGE.
RX DOI=10.1007/BF00019521;
RA Pang P.P., Pruitt R.E., Meyerowitz E.M.;
RT "Molecular cloning, genomic organization, expression and evolution of 12S
RT seed storage protein.";
RL Plant Mol. Biol. 11:805-820(1988).
RN [11]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=7827492; DOI=10.2307/3869944;
RA Parcy F., Valon C., Raynal M., Gaubier-Comella P., Delseny M., Giraudat J.;
RT "Regulation of gene expression programs during Arabidopsis seed
RT development: roles of the ABI3 locus and of endogenous abscisic acid.";
RL Plant Cell 6:1567-1582(1994).
RN [12]
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 [13]
RP INDUCTION BY ABSCISIC ACID.
RX PubMed=15695463; DOI=10.1093/pcp/pci031;
RA Kagaya Y., Okuda R., Ban A., Toyoshima R., Tsutsumida K., Usui H.,
RA Yamamoto A., Hattori T.;
RT "Indirect ABA-dependent regulation of seed storage protein genes by FUSCA3
RT transcription factor in Arabidopsis.";
RL Plant Cell Physiol. 46:300-311(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-53; TYR-78;
RP SER-97; THR-116; SER-259; SER-366; THR-459; SER-484 AND THR-501, 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 [15]
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 [16]
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 [17]
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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Protein storage vacuole {ECO:0000305}.
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 Name=3;
CC IsoId=Q96318-3; Sequence=VSP_039936, VSP_039938;
CC Name=4;
CC IsoId=Q96318-4; Sequence=VSP_039935, VSP_039937;
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|PubMed:7827492, ECO:0000269|Ref.10}.
CC -!- INDUCTION: By abscisic acid (ABA) in an ABI3- and FUS3-dependent
CC manner. {ECO:0000269|PubMed:15695463, ECO:0000269|PubMed:7827492}.
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=BAD95275.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH56848.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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 PIR; T04623; T04623.
DR RefSeq; NP_001078459.1; NM_001084990.1. [Q96318-3]
DR RefSeq; NP_194581.1; NM_118994.4. [Q96318-1]
DR RefSeq; NP_849464.1; NM_179133.2. [Q96318-4]
DR AlphaFoldDB; Q96318; -.
DR SMR; Q96318; -.
DR BioGRID; 14257; 4.
DR STRING; 3702.AT4G28520.1; -.
DR iPTMnet; Q96318; -.
DR PaxDb; Q96318; -.
DR PRIDE; Q96318; -.
DR EnsemblPlants; AT4G28520.1; AT4G28520.1; AT4G28520. [Q96318-1]
DR EnsemblPlants; AT4G28520.2; AT4G28520.2; AT4G28520. [Q96318-4]
DR EnsemblPlants; AT4G28520.4; AT4G28520.4; AT4G28520. [Q96318-3]
DR GeneID; 828970; -.
DR Gramene; AT4G28520.1; AT4G28520.1; AT4G28520. [Q96318-1]
DR Gramene; AT4G28520.2; AT4G28520.2; AT4G28520. [Q96318-4]
DR Gramene; AT4G28520.4; AT4G28520.4; AT4G28520. [Q96318-3]
DR KEGG; ath:AT4G28520; -.
DR Araport; AT4G28520; -.
DR TAIR; locus:2121308; AT4G28520.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR InParanoid; Q96318; -.
DR OMA; KFGRGQE; -.
DR OrthoDB; 603461at2759; -.
DR PhylomeDB; Q96318; -.
DR PRO; PR:Q96318; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q96318; baseline and differential.
DR Genevisible; Q96318; 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; -; 3.
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 Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Phosphoprotein; Reference proteome; Seed storage protein; Signal;
KW Storage protein; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:14688293"
FT CHAIN 24..333
FT /note="12S seed storage protein CRC alpha chain"
FT /id="PRO_0000399923"
FT CHAIN 334..524
FT /note="12S seed storage protein CRC beta chain"
FT /id="PRO_0000399924"
FT DOMAIN 42..289
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 346..495
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 119..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 78
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17313365"
FT DISULFID 37..70
FT /evidence="ECO:0000250"
FT DISULFID 113..340
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
FT VAR_SEQ 204..221
FT /note="VFANTPGSAHWIYNSGEQ -> GIAIGGHIKWFPDLSRGS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039933"
FT VAR_SEQ 222..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039934"
FT VAR_SEQ 389..394
FT /note="GNAMVL -> ECDGAS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_039935"
FT VAR_SEQ 390..396
FT /note="NAMVLPK -> VKCDGAS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039936"
FT VAR_SEQ 395..524
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_039937"
FT VAR_SEQ 397..524
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039938"
FT VARIANT 141..153
FT /note="Missing (in strain: cv. Mr-0)"
FT /evidence="ECO:0000269|PubMed:15912356"
FT VARIANT 170
FT /note="R -> Q (in strain: cv. Mr-0)"
FT /evidence="ECO:0000269|PubMed:15912356"
FT CONFLICT 21
FT /note="C -> S (in Ref. 6; CAA79027)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="Q -> H (in Ref. 5; AAL91248/AAN72284)"
FT /evidence="ECO:0000305"
FT CONFLICT Q96318-2:204
FT /note="G -> V (in Ref. 7; BAH56848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 58235 MW; 6C5C2DFB28B143E3 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
