TR164_ARATH
ID TR164_ARATH Reviewed; 261 AA.
AC O23166;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Thioredoxin-like protein HCF164, chloroplastic {ECO:0000303|PubMed:11701887};
DE AltName: Full=Protein HIGH CHLOROPHYLL FLUORESCENCE 164 {ECO:0000303|PubMed:11701887};
DE Flags: Precursor;
GN Name=HCF164 {ECO:0000303|PubMed:11701887};
GN OrderedLocusNames=At4g37200 {ECO:0000312|Araport:AT4G37200};
GN ORFNames=C7A10.160 {ECO:0000312|EMBL:CAB16778.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11701887; DOI=10.2307/3871593;
RA Lennartz K., Pluecken H., Seidler A., Westhoff P., Bechtold N.,
RA Meierhoff K.;
RT "HCF164 encodes a thioredoxin-like protein involved in the biogenesis of
RT the cytochrome b(6)f complex in Arabidopsis.";
RL Plant Cell 13:2539-2551(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16997915; DOI=10.1074/jbc.m605938200;
RA Motohashi K., Hisabori T.;
RT "HCF164 receives reducing equivalents from stromal thioredoxin across the
RT thylakoid membrane and mediates reduction of target proteins in the
RT thylakoid lumen.";
RL J. Biol. Chem. 281:35039-35047(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825616; DOI=10.1093/mp/ssn076;
RA Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
RT "Comparative genomic study of the thioredoxin family in photosynthetic
RT organisms with emphasis on Populus trichocarpa.";
RL Mol. Plant 2:308-322(2009).
RN [8]
RP INTERACTION WITH LTO1.
RX PubMed=25412899; DOI=10.2174/0929866521666141121153138;
RA Lu Y., Du J.J., Yu Z.B., Peng J.J., Xu J.N., Wang X.Y.;
RT "Identification of potential targets for thylakoid oxidoreductase
RT AtVKOR/LTO1 in chloroplasts.";
RL Protein Pept. Lett. 22:219-225(2014).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that participates in various
CC redox reactions in the chloroplast. Mediates the reduction of PSI-N in
CC the thylakoid lumen. May interact and probably reduce other target
CC proteins of the thylakoid membrane, such as FTSH2, FTSH8, LHCB5, atpA,
CC atpB, atpE, petA and petC. Involved in the biogenesis of the plastid
CC cytochrome b6f complex. Reducing equivalents are provided by stromal M-
CC type thioredoxins and probably transduced through the thylakoid
CC membrane by CCDA. Possesses low insulin disulfide bonds reducing
CC activity. {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}.
CC -!- SUBUNIT: Interacts in vitro with LTO1. {ECO:0000269|PubMed:25412899}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11701887,
CC ECO:0000269|PubMed:16997915}; Lumenal side
CC {ECO:0000269|PubMed:11701887, ECO:0000269|PubMed:16997915}.
CC -!- DISRUPTION PHENOTYPE: High chlorophyll fluorescence and deficiency in
CC the accumulation of the cytochrome b6f complex subunits.
CC {ECO:0000269|PubMed:11701887}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- CAUTION: The active site contains a CEVC motif wich differs from the
CC conserved CGPC motif. {ECO:0000305}.
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DR EMBL; AJ293262; CAC19858.1; -; mRNA.
DR EMBL; Z99707; CAB16778.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80386.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86766.1; -; Genomic_DNA.
DR EMBL; AY075671; AAL77678.1; -; mRNA.
DR EMBL; AY097426; AAM19942.1; -; mRNA.
DR PIR; E85439; E85439.
DR RefSeq; NP_195437.1; NM_119883.3.
DR AlphaFoldDB; O23166; -.
DR SMR; O23166; -.
DR BioGRID; 15155; 1.
DR STRING; 3702.AT4G37200.1; -.
DR TCDB; 3.D.3.5.2; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR iPTMnet; O23166; -.
DR PaxDb; O23166; -.
DR PRIDE; O23166; -.
DR ProteomicsDB; 228462; -.
DR EnsemblPlants; AT4G37200.1; AT4G37200.1; AT4G37200.
DR GeneID; 829874; -.
DR Gramene; AT4G37200.1; AT4G37200.1; AT4G37200.
DR KEGG; ath:AT4G37200; -.
DR Araport; AT4G37200; -.
DR TAIR; locus:2115110; AT4G37200.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_064833_1_0_1; -.
DR InParanoid; O23166; -.
DR OMA; DNTKWLP; -.
DR OrthoDB; 1584124at2759; -.
DR PhylomeDB; O23166; -.
DR PRO; PR:O23166; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23166; baseline and differential.
DR Genevisible; O23166; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; IDA:UniProtKB.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR GO; GO:0010190; P:cytochrome b6f complex assembly; IMP:TAIR.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR044241; TxlA/HCF164.
DR PANTHER; PTHR47353; PTHR47353; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Electron transport; Membrane; Plastid;
KW Redox-active center; Reference proteome; Thylakoid; Transit peptide;
KW Transport.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..261
FT /note="Thioredoxin-like protein HCF164, chloroplastic"
FT /id="PRO_0000394543"
FT DOMAIN 101..229
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 39..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT DISULFID 150..153
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 261 AA; 28745 MW; 34FD1A09BD125D26 CRC64;
MARLVFSLNL PSSHGFNLSP RNLQSFFVTQ TGAPRFRAVR CKPNPESSET KQEKLVIDNG
ETSSASKEVE SSSSVADSSS SSSSGFPESP NKDINRRVAA VTVIAALSLF VSTRLDFGIS
LKDLTASALP YEEALSNGKP TVVEFYADWC EVCRELAPDV YKIEQQYKDK VNFVMLNVDN
TKWEQELDEF GVEGIPHFAF LDREGNEEGN VVGRLPRQYL VENVNALAAG KQSIPYARAV
GQYSSSESRK VHQVTDPLSH G
