BSD2_CHLRE
ID BSD2_CHLRE Reviewed; 156 AA.
AC A0A2K3DZC4; A8IXN3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic {ECO:0000303|PubMed:25124725};
DE Short=CrBSD2 {ECO:0000305};
DE Flags: Precursor;
GN Name=BSD2 {ECO:0000303|PubMed:25124725};
GN Synonyms=ZNJ2 {ECO:0000312|EMBL:EDP03249.1};
GN ORFNames=CHLRE_03g201050v5 {ECO:0000312|EMBL:PNW85892.1},
GN CHLREDRAFT_183954 {ECO:0000312|EMBL:EDP03249.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-42; CYS-78; CYS-81;
RP CYS-89; CYS-92; CYS-133; CYS-136; CYS-144 AND CYS-147.
RX PubMed=25124725; DOI=10.1111/tpj.12638;
RA Doron L., Segal N., Gibori H., Shapira M.;
RT "The BSD2 ortholog in Chlamydomonas reinhardtii is a polysome-associated
RT chaperone that co-migrates on sucrose gradients with the rbcL transcript
RT encoding the Rubisco large subunit.";
RL Plant J. 80:345-355(2014).
CC -!- FUNCTION: Chloroplast chaperone required for RuBisCo biogenesis and
CC translational regulation of the RuBisCo large subunit (RbcL)
CC (PubMed:25124725). Stabilizes an end-state assembly intermediate of
CC eight RbcL subunits until the small subunits (RBCSs) become available
CC to produce a complete stable RuBisCo complex containing eight small and
CC eight large subunits (By similarity). {ECO:0000250|UniProtKB:Q9SN73,
CC ECO:0000269|PubMed:25124725}.
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:25124725}. Note=Associates with chloroplastic
CC polysomes. {ECO:0000269|PubMed:25124725}.
CC -!- SIMILARITY: Belongs to the BSD2 chaperone family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP03249.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM008964; PNW85892.1; -; Genomic_DNA.
DR EMBL; DS496126; EDP03249.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A0A2K3DZC4; -.
DR STRING; 3055.EDP03249; -.
DR EnsemblPlants; PNW85892; PNW85892; CHLRE_03g201050v5.
DR Gramene; PNW85892; PNW85892; CHLRE_03g201050v5.
DR eggNOG; ENOG502S1HB; Eukaryota.
DR HOGENOM; CLU_1909641_0_0_1; -.
DR OMA; QACHACK; -.
DR OrthoDB; 1627756at2759; -.
DR Proteomes; UP000006906; Chromosome 3.
DR ExpressionAtlas; A0A2K3DZC4; baseline and differential.
DR GO; GO:0101031; C:chaperone complex; IDA: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; IDA:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Chaperone; Chloroplast; Metal-binding; Plastid; Reference proteome; Repeat;
KW Transit peptide; Zinc.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..156
FT /note="Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic"
FT /id="PRO_0000447231"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT MUTAGEN 42
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-78, S-81, S-89, S-92, S-133, S-136, S-144 and S-
FT 147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 78
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-81, S-89, S-92, S-133, S-136, S-144 and S-
FT 147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 81
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-78, S-89, S-92, S-133, S-136, S-144 and S-
FT 147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 89
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-78, S-81, S-92, S-133, S-136, S-144 and S-
FT 147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 92
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-78, S-81, S-89, S-133, S-136, S-144 and S-
FT 147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 133
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-78, S-81, S-89, S-92, S-136, S-144 and S-147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 136
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-78, S-81, S-89, S-92, S-133, S-144 and S-147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 144
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-78, S-81, S-89, S-92, S-133, S-136 and S-147."
FT /evidence="ECO:0000269|PubMed:25124725"
FT MUTAGEN 147
FT /note="C->S: Impaired chaperone properties; when associated
FT with S-42, S-78, S-81, S-89, S-92, S-133, S-136 and S-144."
FT /evidence="ECO:0000269|PubMed:25124725"
SQ SEQUENCE 156 AA; 16059 MW; 2CD8A4C841C4DB5C CRC64;
MNSAALNART ASVAPQPQAC HACKCRQLLS RRVPPAQRQV ECSAIAPETL QDIIVGGAVV
GAVSVALYAG LKKDPVPCSL CQGTGGIRCF ACGGDGRNAT VSRDDLYDSK ALGGGVAPPK
RDPLGRTINP RDCKVCRGAG LVLCSQCKGT GFQSAF
