RBS1A_ARATH
ID RBS1A_ARATH Reviewed; 180 AA.
AC P10795; Q0WVH4; Q94JW2; Q9FPI6; Q9SAV4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit 1A, chloroplastic;
DE Short=RuBisCO small subunit 1A;
DE Flags: Precursor;
GN Name=RBCS-1A; Synonyms=ATS1A; OrderedLocusNames=At1g67090;
GN ORFNames=F1O19.14, F5A8.1;
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.
RC STRAIN=cv. Columbia K85;
RX AGRICOLA=IND91035191; DOI=10.1007/BF00019515;
RA Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P.;
RT "Four genes in two diverged subfamilies encode the ribulose-1,5-
RT bisphosphate carboxylase small subunit polypeptides of Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 11:745-759(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-79.
RX PubMed=1515613; DOI=10.1007/bf00029151;
RA Wong E.Y., Hironaka C.M., Fishhoff D.A.;
RT "Arabidopsis thaliana small subunit leader and transit peptide enhance the
RT expression of Bacillus thuringiensis proteins in transgenic plants.";
RL Plant Mol. Biol. 20:81-93(1992).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=28839179; DOI=10.1038/s41598-017-09473-x;
RA Razzak M.A., Lee D.W., Yoo Y.J., Hwang I.;
RT "Evolution of rubisco complex small subunit transit peptides from algae to
RT plants.";
RL Sci. Rep. 7:9279-9279(2017).
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. {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- INTERACTION:
CC P10795; O23160: MYB73; NbExp=3; IntAct=EBI-1541681, EBI-25506855;
CC P10795; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1541681, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:12766230}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12766230}. Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:28839179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P10795-1; Sequence=Displayed;
CC -!- MISCELLANEOUS: There are four genes coding for RBS in Arabidopsis
CC thaliana.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAK49590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA31948.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X13611; CAA31948.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004146; AAD10655.1; -; Genomic_DNA.
DR EMBL; AC007152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE34594.1; -; Genomic_DNA.
DR EMBL; AF325011; AAG40363.1; -; mRNA.
DR EMBL; AF325004; AAG40356.1; -; mRNA.
DR EMBL; AF372874; AAK49590.1; ALT_INIT; mRNA.
DR EMBL; AF410291; AAK95277.1; -; mRNA.
DR EMBL; AY054188; AAL06849.1; -; mRNA.
DR EMBL; AY054581; AAK96772.1; -; mRNA.
DR EMBL; AY058831; AAL24219.1; -; mRNA.
DR EMBL; AY059940; AAL24422.1; -; mRNA.
DR EMBL; AY062612; AAL32690.1; -; mRNA.
DR EMBL; AY062711; AAL32789.1; -; mRNA.
DR EMBL; AY065101; AAL38277.1; -; mRNA.
DR EMBL; AY093380; AAM13379.1; -; mRNA.
DR EMBL; AY093388; AAM13387.1; -; mRNA.
DR EMBL; AY097366; AAM19882.1; -; mRNA.
DR EMBL; BT000362; AAN15681.1; -; mRNA.
DR EMBL; BT002076; AAN72087.1; -; mRNA.
DR EMBL; AK226468; BAE98610.1; -; mRNA.
DR EMBL; AK226776; BAE98874.1; -; mRNA.
DR EMBL; AK226546; BAE98685.1; -; mRNA.
DR EMBL; AK226565; BAE98695.1; -; mRNA.
DR EMBL; X68342; CAA48415.1; ALT_TERM; Other_DNA.
DR PIR; G96694; G96694.
DR PIR; S03720; RKMUA1.
DR RefSeq; NP_176880.1; NM_105379.4. [P10795-1]
DR AlphaFoldDB; P10795; -.
DR SMR; P10795; -.
DR BioGRID; 28250; 16.
DR IntAct; P10795; 8.
DR MINT; P10795; -.
DR STRING; 3702.AT1G67090.1; -.
DR iPTMnet; P10795; -.
DR World-2DPAGE; 0003:P10795; -.
DR PaxDb; P10795; -.
DR PRIDE; P10795; -.
DR ProteomicsDB; 236530; -. [P10795-1]
DR EnsemblPlants; AT1G67090.1; AT1G67090.1; AT1G67090. [P10795-1]
DR GeneID; 843029; -.
DR Gramene; AT1G67090.1; AT1G67090.1; AT1G67090. [P10795-1]
DR KEGG; ath:AT1G67090; -.
DR Araport; AT1G67090; -.
DR TAIR; locus:2033686; AT1G67090.
DR eggNOG; ENOG502QT0M; Eukaryota.
DR HOGENOM; CLU_098114_1_0_1; -.
DR InParanoid; P10795; -.
DR OMA; YREHGNS; -.
DR PhylomeDB; P10795; -.
DR BioCyc; MetaCyc:AT1G67090-MON; -.
DR PRO; PR:P10795; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P10795; baseline and differential.
DR Genevisible; P10795; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IMP:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Membrane; Phosphoprotein; Photorespiration; Photosynthesis; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT CHAIN 55..180
FT /note="Ribulose bisphosphate carboxylase small subunit 1A,
FT chloroplastic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00860"
FT /id="PRO_0000031463"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 115
FT /note="G -> R (in Ref. 4; AAG40356)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="I -> V (in Ref. 1; CAA31948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20216 MW; 5DE768676D61F8F7 CRC64;
MASSMLSSAT MVASPAQATM VAPFNGLKSS AAFPATRKAN NDITSITSNG GRVNCMQVWP
PIGKKKFETL SYLPDLTDSE LAKEVDYLIR NKWIPCVEFE LEHGFVYREH GNSPGYYDGR
YWTMWKLPLF GCTDSAQVLK EVEECKKEYP NAFIRIIGFD NTRQVQCISF IAYKPPSFTG
