OHP1_ARATH
ID OHP1_ARATH Reviewed; 110 AA.
AC O81208; Q8LE25;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Light-harvesting complex-like protein OHP1, chloroplastic {ECO:0000305};
DE AltName: Full=High-light-induced protein {ECO:0000303|PubMed:10794534};
DE Short=AtHLIP {ECO:0000303|PubMed:10794534};
DE AltName: Full=One helix protein {ECO:0000303|PubMed:10794534};
DE AltName: Full=One helix protein 1 {ECO:0000305};
DE AltName: Full=Protein LIGHT-HARVESTING LIKE 2 {ECO:0000303|PubMed:29438089};
DE AltName: Full=Protein PIGMENT DEFECTIVE 335 {ECO:0000305};
DE Flags: Precursor;
GN Name=OHP1 {ECO:0000305};
GN Synonyms=APG16 {ECO:0000303|PubMed:29438089},
GN HLIP {ECO:0000303|PubMed:10794534}, LIL2 {ECO:0000303|PubMed:29438089},
GN OHP {ECO:0000303|PubMed:10794534}, PDE335 {ECO:0000305};
GN OrderedLocusNames=At5g02120 {ECO:0000312|Araport:AT5G02120};
GN ORFNames=T7H20.170 {ECO:0000312|EMBL:CAB82985.1};
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], SUBCELLULAR LOCATION, INDUCTION BY HIGH LIGHT,
RP AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=10794534; DOI=10.1023/a:1006365213954;
RA Jansson S., Andersson J., Kim S.J., Jackowski G.;
RT "An Arabidopsis thaliana protein homologous to cyanobacterial high-light-
RT inducible proteins.";
RL Plant Mol. Biol. 42:345-351(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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, SUBUNIT, INTERACTION
RP WITH HCF244, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY HIGH
RP LIGHT.
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 OHP2 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 OHP2 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-69; ASN-72 AND ARG-74.
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 in the thylakoid membrane in
CC response to light stress (Probable). Involved in photosystems I (PSI)
CC and II (PSII) core proteins function (PubMed:29438089). Forms a
CC trimeric complex with OHP2 and HCF244 that is required to promote PSII
CC core subunit assembly (PubMed:29930106, PubMed:30397023). The trimeric
CC complex forms a transient PSII reaction center-like complex with PsbA,
CC PsbD, PsbE, PsbF and PsbI subunits in thylakoids for early assembly of
CC PSII as well as PSII repair (PubMed:30397023). The trimeric complex is
CC required for the recruitment of ribosomes to the psbA mRNA during PSII
CC biogenesis and repair (PubMed:31991763). Forms an heterodimer with OHP1
CC that binds chlorophylls and carotenoids, and that may function in the
CC delivery of pigments to the PsbA subunit of PSII (PubMed:32071152).
CC {ECO:0000269|PubMed:29438089, ECO:0000269|PubMed:29930106,
CC ECO:0000269|PubMed:30397023, ECO:0000269|PubMed:31991763,
CC ECO:0000269|PubMed:32071152, ECO:0000305|PubMed:10794534}.
CC -!- SUBUNIT: May bind chlorophyll and form dimers in the thylakoid membrane
CC (Probable). Component of a high molecular weight complex containing
CC OHP1, OHP2 and HCF244, and PSII core proteins D1/D2, HCF136 and HCF173
CC (PubMed:29438089). Interacts with HCF244 (PubMed:29438089) (Probable).
CC Forms a trimeric complex with OHP2 and HCF244 that mutually stabilizes
CC each subunit (PubMed:29930106, PubMed:30397023).
CC {ECO:0000269|PubMed:29438089, ECO:0000269|PubMed:29930106,
CC ECO:0000269|PubMed:30397023, ECO:0000305|PubMed:10794534}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10794534, ECO:0000269|PubMed:29438089,
CC ECO:0000269|PubMed:30397023}; Single-pass membrane protein
CC {ECO:0000255}. Note=Associated with both photosystems I and II.
CC {ECO:0000269|PubMed:10794534}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in cotyledons and shoot apices.
CC {ECO:0000269|PubMed:29438089}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in seedling cotyledons and shoot
CC apices in young and mature plants. {ECO:0000269|PubMed:29438089}.
CC -!- INDUCTION: Induced by exposure to high light (PubMed:10794534,
CC PubMed:29438089, PubMed:30489183). Expression follows circadian diurnal
CC fluctuations with highest levels before and shortly after the light
CC phase (PubMed:10794534). {ECO:0000269|PubMed:10794534,
CC ECO:0000269|PubMed:29438089, 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 (PubMed:29438089). Impaired photosystem II (PSII) core protein function
CC and reduced levels of photosystem I core proteins (PubMed:29438089).
CC {ECO:0000269|PubMed:29438089}.
CC -!- SIMILARITY: Belongs to the ELIP/psbS family. {ECO:0000305}.
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DR EMBL; AF054617; AAC25108.1; -; mRNA.
DR EMBL; AL162508; CAB82985.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90433.1; -; Genomic_DNA.
DR EMBL; AY062846; AAL32924.1; -; mRNA.
DR EMBL; AY081584; AAM10146.1; -; mRNA.
DR EMBL; AY085659; AAM62880.1; -; mRNA.
DR PIR; T48233; T48233.
DR RefSeq; NP_195832.1; NM_120290.3.
DR AlphaFoldDB; O81208; -.
DR SMR; O81208; -.
DR STRING; 3702.AT5G02120.1; -.
DR PaxDb; O81208; -.
DR PRIDE; O81208; -.
DR ProteomicsDB; 249357; -.
DR EnsemblPlants; AT5G02120.1; AT5G02120.1; AT5G02120.
DR GeneID; 831799; -.
DR Gramene; AT5G02120.1; AT5G02120.1; AT5G02120.
DR KEGG; ath:AT5G02120; -.
DR Araport; AT5G02120; -.
DR TAIR; locus:2185193; AT5G02120.
DR eggNOG; ENOG502SDR8; Eukaryota.
DR HOGENOM; CLU_153514_0_1_1; -.
DR InParanoid; O81208; -.
DR OMA; THCHGRR; -.
DR OrthoDB; 1545227at2759; -.
DR PhylomeDB; O81208; -.
DR PRO; PR:O81208; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O81208; baseline and differential.
DR Genevisible; O81208; AT.
DR GO; GO:0009507; C:chloroplast; 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:0009523; C:photosystem II; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0010207; P:photosystem II assembly; IMP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB.
PE 1: Evidence at protein level;
KW Chlorophyll; Chloroplast; Chromophore; Membrane; Photosynthesis;
KW Photosystem II; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..110
FT /note="Light-harvesting complex-like protein OHP1,
FT chloroplastic"
FT /id="PRO_0000422366"
FT TOPO_DOM 42..74
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:30397023"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..110
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:30397023"
FT MUTAGEN 69
FT /note="E->A: Abolishes chlorophyll binding of OHP1 and OHP2
FT heterodimer; when associated with A-72 and A-74."
FT /evidence="ECO:0000269|PubMed:32071152"
FT MUTAGEN 72
FT /note="N->A: Abolishes chlorophyll binding of OHP1 and OHP2
FT heterodimer; when associated with A-69 and A-74."
FT /evidence="ECO:0000269|PubMed:32071152"
FT MUTAGEN 74
FT /note="R->A: Abolishes chlorophyll binding of OHP1 and OHP2
FT heterodimer; when associated with A-69 and A-72."
FT /evidence="ECO:0000269|PubMed:32071152"
FT CONFLICT 29
FT /note="C -> Y (in Ref. 5; AAM62880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12010 MW; 2B2DC6C2FD369A3A CRC64;
MSSSPLSSSL FHPLSTLSTH CHGRRQNLCF NRKQQPFVVR AAKLPEGVIV PKAQPKSQPA
FLGFTQTAEI WNSRACMIGL IGTFIVELIL NKGILELIGV EIGKGLDLPL
