STR4_ARATH
ID STR4_ARATH Reviewed; 466 AA.
AC Q9M158; O04623; Q0WWP1; Q93VZ2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Rhodanese-like domain-containing protein 4, chloroplastic;
DE AltName: Full=Protein THYLAKOID RHODANESE-LIKE {ECO:0000303|PubMed:19682289};
DE AltName: Full=Sulfurtransferase 4 {ECO:0000303|PubMed:17408957};
DE Short=AtStr4 {ECO:0000303|PubMed:17408957};
DE Flags: Precursor;
GN Name=STR4 {ECO:0000303|PubMed:17408957};
GN Synonyms=TROL {ECO:0000303|PubMed:19682289};
GN OrderedLocusNames=At4g01050 {ECO:0000312|Araport:AT4G01050};
GN ORFNames=F2N1.31 {ECO:0000312|EMBL:CAB80914.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 [4]
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 [5]
RP GENE FAMILY.
RX PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
RA Bartels A., Mock H.P., Papenbrock J.;
RT "Differential expression of Arabidopsis sulfurtransferases under various
RT growth conditions.";
RL Plant Physiol. Biochem. 45:178-187(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19682289; DOI=10.1111/j.1365-313x.2009.03999.x;
RA Juric S., Hazler-Pilepic K., Tomasic A., Lepedus H., Jelicic B.,
RA Puthiyaveetil S., Bionda T., Vojta L., Allen J.F., Schleiff E., Fulgosi H.;
RT "Tethering of ferredoxin:NADP+ oxidoreductase to thylakoid membranes is
RT mediated by novel chloroplast protein TROL.";
RL Plant J. 60:783-794(2009).
RN [8]
RP STRUCTURE BY NMR OF 134-254.
RX PubMed=15014235; DOI=10.1023/b:jnmr.0000019241.66789.c3;
RA Pantoja-Uceda D., Lopez-Mendez B., Koshiba S., Kigawa T., Shirouzu M.,
RA Terada T., Inoue M., Yabuki T., Aoki M., Seki E., Matsuda T., Hirota H.,
RA Yoshida M., Tanaka A., Osanai T., Seki M., Shinozaki K., Yokoyama S.,
RA Guentert P.;
RT "NMR assignment of the hypothetical rhodanese domain At4g01050 from
RT Arabidopsis thaliana.";
RL J. Biomol. NMR 29:207-208(2004).
RN [9]
RP STRUCTURE BY NMR OF 134-254.
RX PubMed=15576557; DOI=10.1110/ps.041138705;
RA Pantoja-Uceda D., Lopez-Mendez B., Koshiba S., Inoue M., Kigawa T.,
RA Terada T., Shirouzu M., Tanaka A., Seki M., Shinozaki K., Yokoyama S.,
RA Guentert P.;
RT "Solution structure of the rhodanese homology domain At4g01050(175-295)
RT from Arabidopsis thaliana.";
RL Protein Sci. 14:224-230(2005).
CC -!- FUNCTION: Rhodanese domain-containing protein required for anchoring
CC ferredoxin--NADP reductase to the thylakoid membranes and sustaining
CC efficient linear electron flow (LEF). {ECO:0000269|PubMed:19682289}.
CC -!- SUBUNIT: Component of high molecular weight thylakoid LFNRs-containing
CC protein complexes containing LIR1, LFNR1, LFNR2, TIC62 and TROL
CC proteins. {ECO:0000250|UniProtKB:Q6ETQ7}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast envelope
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:19682289}. Plastid,
CC chloroplast thylakoid membrane {ECO:0000269|PubMed:19682289}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Mainly localized to the non-
CC appressed regions of the thylakoid membrane.
CC {ECO:0000269|PubMed:19682289}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and stems, and at lower levels
CC in flowers and siliques (at protein level).
CC {ECO:0000269|PubMed:19682289}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in rosette size, yellowish
CC inflorescences and siliques and small chloroplasts with irregular
CC morphology and no starch grains. {ECO:0000269|PubMed:19682289}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61039.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80914.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF007269; AAB61039.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161491; CAB80914.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81973.1; -; Genomic_DNA.
DR EMBL; AY057701; AAL15331.1; -; mRNA.
DR EMBL; AY057565; AAL09804.1; -; mRNA.
DR EMBL; AY124870; AAM70579.1; -; mRNA.
DR EMBL; AK226302; BAE98457.1; -; mRNA.
DR PIR; H85013; H85013.
DR PIR; T01733; T01733.
DR RefSeq; NP_567209.1; NM_116335.2.
DR PDB; 1VEE; NMR; -; A=134-254.
DR PDB; 2DCQ; NMR; -; A=134-254.
DR PDBsum; 1VEE; -.
DR PDBsum; 2DCQ; -.
DR AlphaFoldDB; Q9M158; -.
DR BMRB; Q9M158; -.
DR SMR; Q9M158; -.
DR BioGRID; 13212; 1.
DR STRING; 3702.AT4G01050.1; -.
DR iPTMnet; Q9M158; -.
DR PaxDb; Q9M158; -.
DR PRIDE; Q9M158; -.
DR ProteomicsDB; 228360; -.
DR EnsemblPlants; AT4G01050.1; AT4G01050.1; AT4G01050.
DR GeneID; 827921; -.
DR Gramene; AT4G01050.1; AT4G01050.1; AT4G01050.
DR KEGG; ath:AT4G01050; -.
DR Araport; AT4G01050; -.
DR TAIR; locus:2124998; AT4G01050.
DR eggNOG; ENOG502QTIH; Eukaryota.
DR HOGENOM; CLU_023830_2_1_1; -.
DR InParanoid; Q9M158; -.
DR OMA; KPPKSWG; -.
DR PhylomeDB; Q9M158; -.
DR EvolutionaryTrace; Q9M158; -.
DR PRO; PR:Q9M158; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M158; baseline and differential.
DR Genevisible; Q9M158; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IMP:TAIR.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR044240; STR4-like.
DR PANTHER; PTHR47377; PTHR47377; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Membrane; Plastid; Reference proteome;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..15
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 16..69
FT /note="Thylakoid"
FT /evidence="ECO:0000305|PubMed:19682289"
FT CHAIN 70..466
FT /note="Rhodanese-like domain-containing protein 4,
FT chloroplastic"
FT /id="PRO_0000139432"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 144..250
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1VEE"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1VEE"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:1VEE"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1VEE"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1VEE"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:1VEE"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1VEE"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1VEE"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1VEE"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:1VEE"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1VEE"
FT TURN 232..236
FT /evidence="ECO:0007829|PDB:1VEE"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1VEE"
SQ SEQUENCE 466 AA; 49387 MW; 7155261857464AF4 CRC64;
MEALKTATFS PMSVLSEKRS EPRKPFSLPN LFPPKSQRPI SQESFLKRFN GGLALLTSVL
SSATAPAKSL TYEEALQQSM TTSSSFDSDG LIEGISNFVT DNPLVIAGGV AALAVPFVLS
QVLNKKPKSW GVESAKNAYT KLGTDDNAQL LDIRATADFR QVGSPNIKGL GKKAVSTVYN
GEDKPGFLKK LSLKFKDPEN TTLYILDKFD GNSELVAELV ALNGFKSAYA IKDGAEGPRG
WLNSSLPWIE PKKTLSLDLS SLTDSISGVF GESSDGVSVA LGVAAAAGLS VFAFTEIETI
LQLLGSAALV QLAGKKLLFA EDRKQTLKQV DEFLNTKVAP KELVDELKEI GKALLPQSTS
NKALPAPATV TAEAESATAT TTTVDKPVPE PETVAATTTT VDKPVPEPEP VPEPVPVPAI
EAAVAAQVIT EPTETEAKPK PHSRPLSPYA SYPDLKPPSS PMPSQP
