PSA2_ARATH
ID PSA2_ARATH Reviewed; 186 AA.
AC O64750;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic {ECO:0000303|PubMed:25228689};
DE Short=AtPSA2 {ECO:0000303|PubMed:25228689};
DE AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 3 {ECO:0000303|PubMed:15634699};
DE Flags: Precursor;
GN Name=PSA2 {ECO:0000303|PubMed:25228689};
GN Synonyms=EDA3 {ECO:0000303|PubMed:15634699};
GN OrderedLocusNames=At2g34860 {ECO:0000312|Araport:AT2G34860};
GN ORFNames=F19I3.9 {ECO:0000312|EMBL:AAC12826.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [5]
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25228689; DOI=10.1074/jbc.m114.587758;
RA Fristedt R., Williams-Carrier R., Merchant S.S., Barkan A.;
RT "A thylakoid membrane protein harboring a DnaJ-type zinc finger domain is
RT required for photosystem I accumulation in plants.";
RL J. Biol. Chem. 289:30657-30667(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27047527; DOI=10.3389/fpls.2016.00360;
RA Wang Y.W., Chen S.M., Wang W.J., Huang X.Q., Zhou C.F., Zhuang Z., Lu S.;
RT "The DnaJ-like zinc finger domain protein PSA2 affects light acclimation
RT and chloroplast development in Arabidopsis thaliana.";
RL Front. Plant Sci. 7:360-360(2016).
CC -!- FUNCTION: Involved in female gametophyte development. Required for
CC embryo sac development (PubMed:15634699). Nuclear genome-encoded factor
CC required for the accumulation of photosystem I (PSI) during plant
CC development (PubMed:25228689). Required for light acclimation and
CC chloroplast development (PubMed:27047527).
CC {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:25228689,
CC ECO:0000269|PubMed:27047527}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q6A662};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250|UniProtKB:Q6A662};
CC -!- SUBUNIT: Interacts in vitro with LTO1. {ECO:0000269|PubMed:25412899}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:27047527}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers. Expressed at low
CC levels in siliques. {ECO:0000269|PubMed:27047527}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to female gametophyte
CC development arrest at two-nuclear stage (PubMed:15634699). Seedling
CC lethality when homozygous. Pale green leaf, variegated leaf and slow
CC growing phenotype when grown on MS medium supplemented with sucrose
CC (PubMed:25228689, PubMed:27047527). {ECO:0000269|PubMed:15634699,
CC ECO:0000269|PubMed:25228689, ECO:0000269|PubMed:27047527}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR EMBL; AC004238; AAC12826.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09031.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09032.1; -; Genomic_DNA.
DR EMBL; AY099664; AAM20515.1; -; mRNA.
DR EMBL; AY128851; AAM91251.1; -; mRNA.
DR PIR; T00468; T00468.
DR RefSeq; NP_001078004.1; NM_001084535.1.
DR RefSeq; NP_181032.1; NM_129039.4.
DR AlphaFoldDB; O64750; -.
DR STRING; 3702.AT2G34860.2; -.
DR PaxDb; O64750; -.
DR PRIDE; O64750; -.
DR ProteomicsDB; 226342; -.
DR EnsemblPlants; AT2G34860.1; AT2G34860.1; AT2G34860.
DR EnsemblPlants; AT2G34860.2; AT2G34860.2; AT2G34860.
DR GeneID; 818051; -.
DR Gramene; AT2G34860.1; AT2G34860.1; AT2G34860.
DR Gramene; AT2G34860.2; AT2G34860.2; AT2G34860.
DR KEGG; ath:AT2G34860; -.
DR Araport; AT2G34860; -.
DR TAIR; locus:2044812; AT2G34860.
DR eggNOG; ENOG502RZYB; Eukaryota.
DR HOGENOM; CLU_072197_1_0_1; -.
DR InParanoid; O64750; -.
DR OMA; RQWMTAC; -.
DR OrthoDB; 1531365at2759; -.
DR PhylomeDB; O64750; -.
DR PRO; PR:O64750; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64750; baseline and differential.
DR Genevisible; O64750; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IBA:GO_Central.
DR GO; GO:0009561; P:megagametogenesis; IMP:TAIR.
DR GO; GO:0048564; P:photosystem I assembly; IMP:UniProtKB.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR SUPFAM; SSF57938; SSF57938; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Metal-binding; Plastid; Reference proteome; Repeat; Thylakoid;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..186
FT /note="Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic"
FT /id="PRO_0000434572"
FT REPEAT 102..109
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT REPEAT 113..120
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT REPEAT 139..146
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT REPEAT 150..157
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT ZN_FING 81..162
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6A662"
SQ SEQUENCE 186 AA; 19943 MW; 86BD8981B3E6E603 CRC64;
MAASSSHLFA LPSPASPFLS APNRNRVRVL AKSCPENQSF DSNDSDSSSE TTHKAQGDQK
SVSRRQWMTA CVCASAALIS NSYTFVSVQS AAALDKKPGG SCRNCQGSGA VLCDMCGGTG
KWKALNRKRA KDVYEFTECP NCYGRGKLVC PVCLGTGLPN NKGLLRRPGA RELLEKMYNG
RLLPDS
