OHP2_ARATH
ID OHP2_ARATH Reviewed; 172 AA.
AC Q9FEC1; Q8LG09;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Light-harvesting complex-like protein OHP2, chloroplastic {ECO:0000305};
DE AltName: Full=One-helix protein 2 {ECO:0000303|PubMed:12805611};
DE AltName: Full=Protein LIGHT-HARVESTING LIKE 6 {ECO:0000303|PubMed:29438089};
DE Flags: Precursor;
GN Name=OHP2 {ECO:0000303|PubMed:12805611};
GN Synonyms=LIL6 {ECO:0000303|PubMed:29438089};
GN OrderedLocusNames=At1g34000 {ECO:0000312|Araport:AT1G34000,
GN ECO:0000312|EMBL:AEE31656.1};
GN ORFNames=F12G12.18 {ECO:0000312|EMBL:AAG12539.1},
GN T15K4.5 {ECO:0000312|EMBL:AAG12849.1};
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, TOPOLOGY, AND
RP INDUCTION BY HIGH LIGHT.
RX PubMed=12805611; DOI=10.1104/pp.102.019281;
RA Andersson U., Heddad M., Adamska I.;
RT "Light stress-induced one-helix protein of the chlorophyll a/b-binding
RT family associated with photosystem I.";
RL Plant Physiol. 132:811-820(2003).
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].
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=29438089; DOI=10.1104/pp.17.01782;
RA Myouga F., Takahashi K., Tanaka R., Nagata N., Kiss A.Z., Funk C.,
RA Nomura Y., Nakagami H., Jansson S., Shinozaki K.;
RT "Stable accumulation of photosystem II requires ONE-HELIX PROTEIN1 (OHP1)
RT of the light harvesting-like family.";
RL Plant Physiol. 176:2277-2291(2018).
RN [7]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=30489183; DOI=10.1080/15592324.2018.1550317;
RA Hey D., Grimm B.;
RT "Requirement of ONE-HELIX PROTEIN 1 (OHP1) in early Arabidopsis seedling
RT development and under high light intensity.";
RL Plant Signal. Behav. 13:e1550317-e1550317(2018).
RN [8]
RP FUNCTION, AND INTERACTION WITH OHP1 AND HCF244.
RX PubMed=29930106; DOI=10.1104/pp.18.00540;
RA Hey D., Grimm B.;
RT "ONE-HELIX PROTEIN2 (OHP2) is required for the stability of OHP1 and
RT assembly factor HCF244 and is functionally linked to PSII biogenesis.";
RL Plant Physiol. 177:1453-1472(2018).
RN [9]
RP FUNCTION, INTERACTION WITH OHP1 AND HCF244, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=30397023; DOI=10.1104/pp.18.01231;
RA Li Y., Liu B., Zhang J., Kong F., Zhang L., Meng H., Li W., Rochaix J.D.,
RA Li D., Peng L.;
RT "OHP1, OHP2, and HCF244 form a transient functional complex with the
RT photosystem II reaction center.";
RL Plant Physiol. 179:195-208(2019).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF GLU-130; ASN-133 AND ARG-135.
RX PubMed=32071152; DOI=10.1104/pp.19.01304;
RA Hey D., Grimm B.;
RT "ONE-HELIX PROTEIN1 and 2 form heterodimers to bind chlorophyll in
RT photosystem II biogenesis.";
RL Plant Physiol. 183:179-193(2020).
RN [11]
RP FUNCTION.
RX PubMed=31991763; DOI=10.3390/plants9020152;
RA Chotewutmontri P., Williams-Carrier R., Barkan A.;
RT "Exploring the Link between Photosystem II Assembly and Translation of the
RT Chloroplast psbA mRNA.";
RL Plants (Basel) 9:0-0(2020).
CC -!- FUNCTION: May play a photoprotective role within PSI in response to
CC light stress (PubMed:12805611). Forms a trimeric complex with OHP1 and
CC HCF244 that is required to promote PSII core subunit assembly
CC (PubMed:29930106, PubMed:30397023). The trimeric complex forms a
CC transient PSII reaction center-like complex with PsbA, PsbD, PsbE, PsbF
CC and PsbI subunits in thylakoids for early assembly of PSII as well as
CC PSII repair (PubMed:30397023). The trimeric complex is required for the
CC recruitment of ribosomes to the psbA mRNA during PSII biogenesis and
CC repair (PubMed:31991763). Forms an heterodimer with OHP1 that binds
CC chlorophylls and carotenoids, and that may function in the delivery of
CC pigments to the PsbA subunit of PSII (PubMed:32071152).
CC {ECO:0000269|PubMed:12805611, ECO:0000269|PubMed:29930106,
CC ECO:0000269|PubMed:30397023, ECO:0000269|PubMed:31991763,
CC ECO:0000269|PubMed:32071152}.
CC -!- SUBUNIT: Component of a high molecular weight complex containing OHP1,
CC OHP2 and HCF244, and PSII core proteins D1/D2, HCF136 and HCF173
CC (PubMed:29438089). Forms a trimeric complex with OHP1 and HCF244 that
CC mutually stabilizes each subunit (PubMed:29930106, PubMed:30397023).
CC {ECO:0000269|PubMed:29438089, ECO:0000269|PubMed:29930106,
CC ECO:0000269|PubMed:30397023}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:12805611, ECO:0000269|PubMed:29438089,
CC ECO:0000269|PubMed:30397023}; Single-pass membrane protein
CC {ECO:0000255}. Note=Associates with PSI under low or high light
CC conditions. {ECO:0000269|PubMed:12805611}.
CC -!- INDUCTION: Induced by exposure to high light.
CC {ECO:0000269|PubMed:12805611, ECO:0000269|PubMed:30489183}.
CC -!- DISRUPTION PHENOTYPE: High light sensitivity leading to stunted growth
CC with pale-green leaves on agar plates, but unable to grow on soil.
CC {ECO:0000269|PubMed:29438089}.
CC -!- SIMILARITY: Belongs to the ELIP/psbS family. {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; AY057393; AAL25838.1; -; mRNA.
DR EMBL; AC015446; AAG12539.1; -; Genomic_DNA.
DR EMBL; AC079286; AAG12849.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31656.1; -; Genomic_DNA.
DR EMBL; AF378874; AAK55677.1; -; mRNA.
DR EMBL; AY045977; AAK76651.1; -; mRNA.
DR EMBL; AY050472; AAK91485.1; -; mRNA.
DR EMBL; AY091438; AAM14377.1; -; mRNA.
DR EMBL; AY084529; AAM61097.1; -; mRNA.
DR PIR; G86463; G86463.
DR RefSeq; NP_564432.3; NM_103122.4.
DR AlphaFoldDB; Q9FEC1; -.
DR SMR; Q9FEC1; -.
DR IntAct; Q9FEC1; 1.
DR STRING; 3702.AT1G34000.1; -.
DR iPTMnet; Q9FEC1; -.
DR PaxDb; Q9FEC1; -.
DR PRIDE; Q9FEC1; -.
DR ProteomicsDB; 249358; -.
DR EnsemblPlants; AT1G34000.1; AT1G34000.1; AT1G34000.
DR GeneID; 840297; -.
DR Gramene; AT1G34000.1; AT1G34000.1; AT1G34000.
DR KEGG; ath:AT1G34000; -.
DR Araport; AT1G34000; -.
DR TAIR; locus:2008996; AT1G34000.
DR eggNOG; ENOG502RXUG; Eukaryota.
DR HOGENOM; CLU_105635_0_0_1; -.
DR InParanoid; Q9FEC1; -.
DR OMA; IRCSQTE; -.
DR OrthoDB; 1503023at2759; -.
DR PhylomeDB; Q9FEC1; -.
DR PRO; PR:Q9FEC1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FEC1; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
DR GO; GO:0009642; P:response to light intensity; IEP:TAIR.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Thylakoid;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 44..172
FT /note="Light-harvesting complex-like protein OHP2,
FT chloroplastic"
FT /id="PRO_0000437946"
FT TOPO_DOM 44..135
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:12805611,
FT ECO:0000269|PubMed:30397023"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..172
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:12805611,
FT ECO:0000269|PubMed:30397023"
FT REGION 45..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 130
FT /note="E->A: Abolishes chlorophyll binding of OHP1 and OHP2
FT heterodimer; when associated with A-133 and A-135."
FT /evidence="ECO:0000269|PubMed:32071152"
FT MUTAGEN 133
FT /note="N->A: Abolishes chlorophyll binding of OHP1 and OHP2
FT heterodimer; when associated with A-130 and A-135."
FT /evidence="ECO:0000269|PubMed:32071152"
FT MUTAGEN 135
FT /note="R->A: Abolishes chlorophyll binding of OHP1 and OHP2
FT heterodimer; when associated with A-130 and A-133."
FT /evidence="ECO:0000269|PubMed:32071152"
FT CONFLICT 58
FT /note="T -> A (in Ref. 5; AAM61097)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="P -> A (in Ref. 5; AAM61097)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="Missing (in Ref. 5; AAM61097)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..87
FT /note="AVAV -> SVAI (in Ref. 5; AAM61097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 18665 MW; 472C10BE9E8FB519 CRC64;
MSVASPIQCI RILNPSSSSS SSTASSSFRF STTTKPCVFI IRCSQTEGPL RRPSAPPTLR
EPQKPVPPSQ PSSSPPPSPP PQKAVAVDGK SVTTVEFQRQ KAKELQEYFK QKKLEAAGQG
PFFGFQPKNE ISNGRWAMFG FAVGMLTEYA TGSDLVDQVK ILLSNFGILD LE
