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RBS2_SOLLC
ID   RBS2_SOLLC              Reviewed;         180 AA.
AC   P07179;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE            Short=RuBisCO small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00860};
DE   AltName: Full=LESS 5 {ECO:0000303|PubMed:3557127};
DE   AltName: Full=Ribulose bisphosphate carboxylase small subunit 2A, chloroplastic {ECO:0000303|PubMed:3012537};
DE            Short=RuBisCO small subunit 2A {ECO:0000303|PubMed:3012537};
DE   Flags: Precursor;
GN   Name=RBCS2 {ECO:0000255|HAMAP-Rule:MF_00860};
GN   Synonyms=RBCS-2A {ECO:0000303|PubMed:3012537};
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 [MRNA] (LESS 5).
RC   STRAIN=cv. VF36;
RX   PubMed=3557127; DOI=10.1016/0378-1119(86)90348-3;
RA   McKnight T.D., Alexander D.C., Babcock M.S., Simpson R.B.;
RT   "Nucleotide sequence and molecular evolution of two tomato genes encoding
RT   the small subunit of ribulose-1,5-bisphosphate carboxylase.";
RL   Gene 48:23-32(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (RBCS-2A).
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   [3]
RP   NUCLEOTIDE SEQUENCE (RBCS-2).
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   [4]
RP   SEQUENCE REVISION.
RA   Manzara T.;
RL   Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 1-9 (RBCS-2).
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}.
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DR   EMBL; M15236; AAA34192.1; -; mRNA.
DR   EMBL; M13543; AAA34189.1; -; mRNA.
DR   EMBL; X05983; CAA29401.2; -; Genomic_DNA.
DR   EMBL; X66069; CAA46869.1; -; Genomic_DNA.
DR   PIR; S02363; RKTOS2.
DR   RefSeq; NP_001295873.1; NM_001308944.1.
DR   AlphaFoldDB; P07179; -.
DR   SMR; P07179; -.
DR   STRING; 4081.Solyc03g034220.2.1; -.
DR   PaxDb; P07179; -.
DR   PRIDE; P07179; -.
DR   EnsemblPlants; Solyc03g034220.3.1; Solyc03g034220.3.1; Solyc03g034220.3.
DR   GeneID; 543974; -.
DR   Gramene; Solyc03g034220.3.1; Solyc03g034220.3.1; Solyc03g034220.3.
DR   KEGG; sly:543974; -.
DR   eggNOG; ENOG502QT0M; Eukaryota.
DR   HOGENOM; CLU_098114_1_0_1; -.
DR   InParanoid; P07179; -.
DR   OMA; GRCWIMW; -.
DR   OrthoDB; 1258997at2759; -.
DR   PhylomeDB; P07179; -.
DR   Proteomes; UP000004994; Chromosome 3.
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   2: Evidence at transcript level;
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 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT                   /id="PRO_0000031519"
FT   VARIANT         87
FT                   /note="I -> V (in strain: cv. VF36)"
SQ   SEQUENCE   180 AA;  20278 MW;  FFB6DD2B1C6D3F3B CRC64;
     MASSVISSAA VATRSNVTQA SMVAPFTGLK SSATFPVTKK QNLDITSIAS NGGRVSCMQV
     WPPINMKKYE TLSYLPDLSD EQLLSEIEYL LKNGWVPCLE FETEHGFVYR ENNKSPGYYD
     GRYWTMWKLP MFGCTDATQV LAEVQEAKKA YPQAWVRIIG FDNVRQVQCI SFIAYKPEGY
 
 
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