RBS3_SOLLC
ID RBS3_SOLLC Reviewed; 180 AA.
AC P07180;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit 3 {ECO:0000255|HAMAP-Rule:MF_00860};
DE AltName: Full=Ribulose bisphosphate carboxylase small chain 3A/3C, chloroplastic {ECO:0000303|PubMed:3478552};
DE Short=RuBisCO small subunit 3A/3C {ECO:0000303|PubMed:3478552};
DE Flags: Precursor;
GN Name=RBCS3 {ECO:0000255|HAMAP-Rule:MF_00860};
GN Synonyms=RBCS-3A/3C {ECO:0000303|PubMed:3478552};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3012537; DOI=10.1073/pnas.83.11.3880;
RA Pichersky E., Bernatzky R., Tanksley S.D., Cashmore A.R.;
RT "Evidence for selection as a mechanism in the concerted evolution of
RT Lycopersicon esculentum (tomato) genes encoding the small subunit of
RT ribulose-1,5-bisphosphate carboxylase/oxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3880-3884(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. VFNT Cherry LA1221;
RX PubMed=3478552; DOI=10.1007/bf00329650;
RA Sugita M., Manzara T., Pichersky E., Cashmore A., Gruissem W.;
RT "Genomic organization, sequence analysis and expression of all five genes
RT encoding the small subunit of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase from tomato.";
RL Mol. Gen. Genet. 209:247-256(1987).
RN [3]
RP SEQUENCE REVISION.
RA Manzara T.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=cv. VFNT Cherry LA1221; TISSUE=Root;
RX PubMed=8425051; DOI=10.1007/bf00039619;
RA Manzara T., Carrasco P., Gruissem W.;
RT "Developmental and organ-specific changes in DNA-protein interactions in
RT the tomato rbcS1, rbcS2 and rbcS3A promoter regions.";
RL Plant Mol. Biol. 21:69-88(1993).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate. Both reactions occur simultaneously and in competition at
CC the same active site. Although the small subunit is not catalytic it is
CC essential for maximal activity. Involved in antiviral defenses (By
CC similarity). {ECO:0000250|UniProtKB:A0A0S4IJL0, ECO:0000255|HAMAP-
CC Rule:MF_00860}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SUBUNIT: (Microbial infection) Binds to tobamovirus movement protein;
CC this interaction seems required for viral systemic movement.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_00860}.
CC -!- SUBCELLULAR LOCATION: Cell junction, plasmodesma
CC {ECO:0000250|UniProtKB:A0A0S4IJL0}. Note=(Microbial infection) May be
CC present in virus replication complexes (VRCs) of tobamovirus infected
CC cells. {ECO:0000250|UniProtKB:A0A0S4IJL0}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X05984; CAA29402.1; -; Genomic_DNA.
DR EMBL; M13544; AAA34190.1; -; Genomic_DNA.
DR EMBL; X05986; CAA29404.1; -; Genomic_DNA.
DR EMBL; X66070; CAA46870.1; -; Genomic_DNA.
DR EMBL; X66072; CAA46872.1; -; Genomic_DNA.
DR PIR; S01109; RKTO3C.
DR RefSeq; NP_001334840.1; NM_001347911.1.
DR AlphaFoldDB; P07180; -.
DR SMR; P07180; -.
DR PRIDE; P07180; -.
DR GeneID; 108449891; -.
DR InParanoid; P07180; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P07180; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 1.
DR Gene3D; 3.30.190.10; -; 1.
DR HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR InterPro; IPR024681; RuBisCO_ssu.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR024680; RuBisCO_ssu_N.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 1.
DR Pfam; PF12338; RbcS; 1.
DR Pfam; PF00101; RuBisCO_small; 1.
DR PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 1.
DR SUPFAM; SSF55239; SSF55239; 1.
PE 3: Inferred from homology;
KW Antiviral defense; Calvin cycle; Carbon dioxide fixation; Cell junction;
KW Chloroplast; Host-virus interaction; Photorespiration; Photosynthesis;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 57..180
FT /note="Ribulose bisphosphate carboxylase small subunit,
FT chloroplastic 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031520"
SQ SEQUENCE 180 AA; 20231 MW; 8D091B21167B821C CRC64;
MASSVMSSAA VATRGNGAQA SMVAPFTGLK STASFPVSRK QNLDITSIAS NGGRVSCMQV
WPPINMKKYE TLSYLPDLSD EQLLSEIEYL LKNGWVPCLE FETEHGFVYR ENHKSPGYYD
GRYWTMWKLP MFGCTDATQV LAEVQEAKKA YPQAWVRIIG FDNVRQVQCI SFIAYKPEGY
