SOQ1_ARATH
ID SOQ1_ARATH Reviewed; 1055 AA.
AC Q8VZ10; A0A1P8APV3; A0A1P8APY8; C0Z278; Q0WQ65; Q8GX08; Q8L9X3; Q9C7X1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein SUPPRESSOR OF QUENCHING 1, chloroplastic {ECO:0000303|PubMed:23818601};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:P95649};
DE Flags: Precursor;
GN Name=SOQ1 {ECO:0000303|PubMed:23818601};
GN OrderedLocusNames=At1g56500 {ECO:0000312|Araport:AT1G56500};
GN ORFNames=F13N6.21 {ECO:0000312|EMBL:AAG51506.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] (ISOFORM 5).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-57, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-56, AND IDENTIFICATION BY MASS
RP 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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-80; 431-CYS--CYS-434 AND
RP GLU-859, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23818601; DOI=10.1073/pnas.1305443110;
RA Brooks M.D., Sylak-Glassman E.J., Fleming G.R., Niyogi K.K.;
RT "A thioredoxin-like/beta-propeller protein maintains the efficiency of
RT light harvesting in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E2733-E2740(2013).
CC -!- FUNCTION: Required to maintain light harvesting efficiency, especially
CC during nonphotochemical quenching (NPQ) recovery, via the regulation of
CC chlorophyll excited-state lifetime probably by preventing the formation
CC of a slowly reversible form of antenna quenching.
CC {ECO:0000269|PubMed:23818601}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P95649};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:23818601}; Single-pass membrane protein
CC {ECO:0000255}. Note=Mostly localized in thylakoid grana margins, and,
CC to a lower extent, in grana and stroma lamellae.
CC {ECO:0000269|PubMed:23818601}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8VZ10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZ10-2; Sequence=VSP_059050;
CC Name=3;
CC IsoId=Q8VZ10-3; Sequence=VSP_059046;
CC Name=4;
CC IsoId=Q8VZ10-4; Sequence=VSP_059048, VSP_059049;
CC Name=5;
CC IsoId=Q8VZ10-5; Sequence=VSP_059047;
CC Name=6;
CC IsoId=Q8VZ10-6; Sequence=VSP_059046, VSP_059048, VSP_059049;
CC -!- DISRUPTION PHENOTYPE: High light intensity-dependent and irreversible
CC nonphotochemical quenching (NPQ) due to a decrease in chlorophyll
CC excited-state lifetime. {ECO:0000269|PubMed:23818601}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HAD-like
CC hydrolase superfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the thioredoxin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AC058785; AAG51506.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33400.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58700.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58701.1; -; Genomic_DNA.
DR EMBL; AK118507; BAC43111.1; -; mRNA.
DR EMBL; AY065399; AAL38840.1; -; mRNA.
DR EMBL; AK318692; BAH56807.1; -; mRNA.
DR EMBL; AK228839; BAF00734.1; -; mRNA.
DR EMBL; AY088165; AAM65709.1; -; mRNA.
DR PIR; F96606; F96606.
DR RefSeq; NP_001321116.1; NM_001333783.1. [Q8VZ10-2]
DR RefSeq; NP_001321117.1; NM_001333784.1. [Q8VZ10-3]
DR RefSeq; NP_564718.2; NM_104525.3. [Q8VZ10-1]
DR AlphaFoldDB; Q8VZ10; -.
DR SMR; Q8VZ10; -.
DR STRING; 3702.AT1G56500.1; -.
DR iPTMnet; Q8VZ10; -.
DR PaxDb; Q8VZ10; -.
DR PRIDE; Q8VZ10; -.
DR ProteomicsDB; 245325; -. [Q8VZ10-1]
DR EnsemblPlants; AT1G56500.1; AT1G56500.1; AT1G56500. [Q8VZ10-1]
DR EnsemblPlants; AT1G56500.2; AT1G56500.2; AT1G56500. [Q8VZ10-2]
DR EnsemblPlants; AT1G56500.3; AT1G56500.3; AT1G56500. [Q8VZ10-3]
DR GeneID; 842103; -.
DR Gramene; AT1G56500.1; AT1G56500.1; AT1G56500. [Q8VZ10-1]
DR Gramene; AT1G56500.2; AT1G56500.2; AT1G56500. [Q8VZ10-2]
DR Gramene; AT1G56500.3; AT1G56500.3; AT1G56500. [Q8VZ10-3]
DR KEGG; ath:AT1G56500; -.
DR Araport; AT1G56500; -.
DR TAIR; locus:2010728; AT1G56500.
DR eggNOG; KOG2177; Eukaryota.
DR eggNOG; KOG2914; Eukaryota.
DR HOGENOM; CLU_312014_0_0_1; -.
DR InParanoid; Q8VZ10; -.
DR OMA; GGDPMIP; -.
DR OrthoDB; 1145834at2759; -.
DR PhylomeDB; Q8VZ10; -.
DR PRO; PR:Q8VZ10; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VZ10; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010196; P:nonphotochemical quenching; IMP:TAIR.
DR CDD; cd14951; NHL-2_like; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR045302; NHL2_NHL_rpt_dom.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF13419; HAD_2; 1.
DR Pfam; PF01436; NHL; 2.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SMART; SM00135; LY; 2.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Disulfide bond; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Plastid; Reference proteome; Repeat;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 57..1055
FT /note="Protein SUPPRESSOR OF QUENCHING 1, chloroplastic"
FT /id="PRO_0000441235"
FT TOPO_DOM 59..327
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:23818601"
FT TRANSMEM 328..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..1055
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:23818601"
FT DOMAIN 359..536
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REPEAT 565..597
FT /note="NHL 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 611..647
FT /note="NHL 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 673..712
FT /note="NHL 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 802..832
FT /note="NHL 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT REPEAT 854..887
FT /note="NHL 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00504"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 118..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 141..144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 183..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
FT MOD_RES 57
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 431..434
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..202
FT /note="Missing (in isoform 3 and isoform 6)"
FT /id="VSP_059046"
FT VAR_SEQ 237..1055
FT /note="Missing (in isoform 5)"
FT /id="VSP_059047"
FT VAR_SEQ 298..299
FT /note="RN -> SM (in isoform 4 and isoform 6)"
FT /id="VSP_059048"
FT VAR_SEQ 300..1055
FT /note="Missing (in isoform 4 and isoform 6)"
FT /id="VSP_059049"
FT VAR_SEQ 870..1055
FT /note="RLFVADTNNSLIRYIDLNKGEDSEILTLELKGVQPPTPKAKSLKRLRKRASA
FT DTKIVKVDSVTSREGDLNLKISLPDGYHFSKEARSKFVVDVEPENAVAIDPTEGTLSPE
FT GSTMLHFIQSSTSASVGKISCKVYYCKEDEVCLYQSVQFEVPFKVESELSASPTITFTV
FT TPRAPDAGGLQLQGTR -> NFLVLFNSY (in isoform 2)"
FT /id="VSP_059050"
FT MUTAGEN 80
FT /note="D->N: Complete rescue in complementation test of the
FT nonphotochemical quenching (NPQ) phenotype observed in
FT disrupted plants."
FT /evidence="ECO:0000269|PubMed:23818601"
FT MUTAGEN 431..434
FT /note="CINC->SINS: No rescue in complementation test of the
FT nonphotochemical quenching (NPQ) phenotype observed in
FT disrupted plants."
FT /evidence="ECO:0000269|PubMed:23818601"
FT MUTAGEN 859
FT /note="E->K: In soq1-2; high light intensity-dependent and
FT irreversible nonphotochemical quenching (NPQ) due to a
FT decrease in chlorophyll excited-state lifetime."
FT /evidence="ECO:0000269|PubMed:23818601"
FT CONFLICT 143
FT /note="E -> K (in Ref. 7; AAM65709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1055 AA; 114402 MW; CC3603CD905E80AA CRC64;
MALKLTSPPS VFSQSRRLSS SSLIPIRSKS TFTGFRSRTG VYLSKTTALQ SSTKLSVAAE
SPAATIATDD WGKVSAVLFD MDGVLCNSED LSRRAAVDVF TEMGVEVTVD DFVPFMGTGE
AKFLGGVASV KEVKGFDPDA AKERFFEIYL DKYAKPESGI GFPGALELVT ECKNKGLKVA
VASSADRIKV DANLKAAGLS LTMFDAIVSA DAFENLKPAP DIFLAAAKIL GVPTSECVVI
EDALAGVQAA QAANMRCIAV KTTLSEAILK DAGPSMIRDD IGNISINDIL TGGSDSTRNS
TAMLEENTVS DKTSANGFQG SRRDILRYGS LGIALSCVYF AATNWKAMQY ASPKALWNAL
VGAKSPSFTQ NQGEGRVQQF VDYIADLESK QTATTVPEFP SKLDWLNTAP LQFRRDLKGK
VVILDFWTYC CINCMHVLPD LEFLEKKYKD MPFTVVGVHS AKFDNEKDLD AIRNAVLRYD
ISHPVVNDGD MYMWRELGIN SWPTFAVVSP NGKVIAQIAG EGHRKDLDDV VAAALTYYGG
KNVLDSTPLP TRLEKDNDPR LATSPLKFPG KLAIDTLNNR LFISDSNHNR IIVTDLEGNF
IVQIGSSGEE GFQDGSFEDA AFNRPQGLAY NAKKNLLYVA DTENHALREI DFVNERVQTL
AGNGTKGSDY QGGRKGTKQL LNSPWDVCFE PVNEKVYIAM AGQHQIWEYS VLDGITRVFS
GNGYERNLNG STPQTTSFAQ PSGISLGPDL KEAYIADSES SSIRALDLQT GGSRLLAGGD
PYFSENLFKF GDNDGVGAEV LLQHPLGVLC ANDGQIYLTD SYNHKIKKLD PVTKRVVTLA
GTGKAGFKDG KVKGAQLSEP AGLAITENGR LFVADTNNSL IRYIDLNKGE DSEILTLELK
GVQPPTPKAK SLKRLRKRAS ADTKIVKVDS VTSREGDLNL KISLPDGYHF SKEARSKFVV
DVEPENAVAI DPTEGTLSPE GSTMLHFIQS STSASVGKIS CKVYYCKEDE VCLYQSVQFE
VPFKVESELS ASPTITFTVT PRAPDAGGLQ LQGTR
