BSD2_MAIZE
ID BSD2_MAIZE Reviewed; 129 AA.
AC Q9XF14; A0A1D6KEF8; A0A317YH68; B6SUD2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic {ECO:0000303|PubMed:10330470};
DE Short=ZmBSD2 {ECO:0000305};
DE Flags: Precursor;
GN Name=BSD2 {ECO:0000312|EMBL:AAD28599.1};
GN ORFNames=ZEAMMB73_Zm00001d030786 {ECO:0000312|EMBL:ONM01538.1},
GN Zm00014a_034282 {ECO:0000312|EMBL:PWZ57870.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. B73;
RX PubMed=10330470; DOI=10.2307/3870819;
RA Brutnell T.P., Sawers R.J., Mant A., Langdale J.A.;
RT "BUNDLE SHEATH DEFECTIVE2, a novel protein required for post-translational
RT regulation of the rbcL gene of maize.";
RL Plant Cell 11:849-864(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Missouri 17; TISSUE=Seedling;
RX PubMed=30061735; DOI=10.1038/s41588-018-0182-0;
RA Sun S., Zhou Y., Chen J., Shi J., Zhao H., Zhao H., Song W., Zhang M.,
RA Cui Y., Dong X., Liu H., Ma X., Jiao Y., Wang B., Wei X., Stein J.C.,
RA Glaubitz J.C., Lu F., Yu G., Liang C., Fengler K., Li B., Rafalski A.,
RA Schnable P.S., Ware D.H., Buckler E.S., Lai J.;
RT "Extensive intraspecific gene order and gene structural variations between
RT Mo17 and other maize genomes.";
RL Nat. Genet. 50:1289-1295(2018).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12239405; DOI=10.2307/3870292;
RA Roth R., Hall L.N., Brutnell T.P., Langdale J.A.;
RT "bundle sheath defective2, a Mutation That Disrupts the Coordinated
RT Development of Bundle Sheath and Mesophyll Cells in the Maize Leaf.";
RL Plant Cell 8:915-927(1996).
CC -!- FUNCTION: Chloroplast chaperone required for RuBisCo complex biogenesis
CC and translational regulation of the RuBisCo large subunit (RbcL)
CC (PubMed:10330470, PubMed:12239405). Stabilizes an end-state assembly
CC intermediate of eight RbcL subunits until the small subunits (RBCSs)
CC become available to produce a complete stable RuBisCo complex
CC containing eight small and eight large subunits (By similarity).
CC Involved in the differentiation of bundle sheath cells, especially
CC chloroplast structure (PubMed:12239405). {ECO:0000250|UniProtKB:Q9SN73,
CC ECO:0000269|PubMed:10330470, ECO:0000269|PubMed:12239405}.
CC -!- SUBUNIT: Interacts with the RuBisCo large subunit (RbcL) assembled as
CC an intermediate complex made of eight RbcL and eight BSD2 subunits.
CC {ECO:0000250|UniProtKB:Q9SN73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:10330470}. Note=Associates with chloroplastic
CC polysomes. {ECO:0000269|PubMed:10330470}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot tissues, in both bundle sheath
CC and mesophyll cells. {ECO:0000269|PubMed:10330470}.
CC -!- DEVELOPMENTAL STAGE: Relatively abundant in etiolated, light-shifted,
CC and young (plastochron 1 to 5) leaves. {ECO:0000269|PubMed:10330470}.
CC -!- DISRUPTION PHENOTYPE: Mu-active bsd2-m1 mutants are specifically
CC disrupted C4 differentiation in bundle sheath cells with reduced levels
CC of bundle sheath cell-specific photosynthetic enzymes and aberrant
CC bundle sheath chloroplast structure and altered RuBisCo complex
CC formation (PubMed:12239405). Ectopic accumulation of RuBisCo large
CC subunit (RbcL) in mesophyll cells (PubMed:12239405). Reduced
CC accumulation in Mu-inactivated bsd2-m1 mutants exhibiting slightly pale
CC green and grainy leaves (due to the random presence of altered bundle
CC sheath cell chloroplasts) associated with the loss of RuBisCo complex
CC formation, but accumulation of chloroplast-encoded RbcL transcripts
CC associated with polysomes in both bundle sheath and mesophyll cells
CC (PubMed:10330470). RbcL transcription is abnormally similar in both
CC dark-grown and light-shifted seedlings (PubMed:10330470).
CC {ECO:0000269|PubMed:10330470, ECO:0000269|PubMed:12239405}.
CC -!- SIMILARITY: Belongs to the BSD2 chaperone family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ONM01539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=PWZ57870.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF126742; AAD28599.1; -; mRNA.
DR EMBL; CM007647; ONM01538.1; -; Genomic_DNA.
DR EMBL; CM007647; ONM01539.1; ALT_SEQ; Genomic_DNA.
DR EMBL; NCVQ01000001; PWZ57870.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EU956347; ACG28465.1; -; mRNA.
DR RefSeq; NP_001105880.1; NM_001112410.1.
DR AlphaFoldDB; Q9XF14; -.
DR SMR; Q9XF14; -.
DR STRING; 4577.GRMZM2G062788_P01; -.
DR PaxDb; Q9XF14; -.
DR EnsemblPlants; Zm00001eb029690_T002; Zm00001eb029690_P002; Zm00001eb029690.
DR GeneID; 732793; -.
DR Gramene; Zm00001eb029690_T002; Zm00001eb029690_P002; Zm00001eb029690.
DR KEGG; zma:732793; -.
DR MaizeGDB; 716010; -.
DR eggNOG; ENOG502S25V; Eukaryota.
DR HOGENOM; CLU_152807_1_0_1; -.
DR OMA; ANFQSWE; -.
DR OrthoDB; 1528729at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR Proteomes; UP000251960; Chromosome 1.
DR ExpressionAtlas; Q9XF14; baseline and differential.
DR GO; GO:0101031; C:chaperone complex; IMP:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1905538; F:polysome binding; IDA:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IMP:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:UniProtKB.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IMP:UniProtKB.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR SUPFAM; SSF57938; SSF57938; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Chloroplast; Metal-binding; Plastid; Reference proteome; Repeat;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..129
FT /note="Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic"
FT /id="PRO_0000447232"
FT ZN_FING 49..123
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT CONFLICT 72
FT /note="V -> T (in Ref. 4; ACG28465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 13719 MW; B58FCA2F6390E9DB CRC64;
MAATASLTTT APSPPALLKA SAPLLISFRP VSRHCKNLCI KTKATENDQS AKKHQKVKSI
LCQDCEGNGA IVCTKCEGNG VNSVDYFEGR FKAGSLCWLC RGKREILCGN CNGAGFLGGF
LSTFDETAQ
