ID   PSAF_SPIOL              Reviewed;         231 AA.
AC   P12355;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Photosystem I reaction center subunit III, chloroplastic;
DE   AltName: Full=Light-harvesting complex I 17 kDa protein;
DE   AltName: Full=PSI-F;
DE   Flags: Precursor;
GN   Name=PSAF;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3049152; DOI=10.1016/0014-5793(88)80205-9;
RA   Steppuhn J., Hermans J., Nechushtai R., Ljungberg U., Thuemmler F.,
RA   Lottspeich F., Herrmann R.G.;
RT   "Nucleotide sequence of cDNA clones encoding the entire precursor
RT   polypeptides for subunits IV and V of the photosystem I reaction center
RT   from spinach.";
RL   FEBS Lett. 237:218-224(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 78-91.
RA   Hippler M., Ratajczak R., Haehnel W.;
RT   "Identification of the plastocyanin binding subunit of photosystem I.";
RL   FEBS Lett. 250:280-284(1989).
CC   -!- FUNCTION: Probably participates in efficiency of electron transfer from
CC       plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria).
CC       This plastocyanin-docking protein contributes to the specific
CC       association of plastocyanin to PSI.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen.
CC   -!- SIMILARITY: Belongs to the PsaF family. {ECO:0000305}.
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DR   EMBL; X13133; CAA31523.1; -; mRNA.
DR   PIR; S00451; F1SP3.
DR   PDB; 2O01; X-ray; 3.40 A; F=78-231.
DR   PDB; 2WSC; X-ray; 3.30 A; F=1-231.
DR   PDB; 2WSE; X-ray; 3.49 A; F=1-231.
DR   PDB; 2WSF; X-ray; 3.48 A; F=1-231.
DR   PDB; 3LW5; X-ray; 3.30 A; F=78-231.
DR   PDB; 4XK8; X-ray; 2.80 A; F/f=78-228.
DR   PDB; 6LY5; EM; 2.38 A; f=78-228.
DR   PDBsum; 2O01; -.
DR   PDBsum; 2WSC; -.
DR   PDBsum; 2WSE; -.
DR   PDBsum; 2WSF; -.
DR   PDBsum; 3LW5; -.
DR   PDBsum; 4XK8; -.
DR   PDBsum; 6LY5; -.
DR   AlphaFoldDB; P12355; -.
DR   SMR; P12355; -.
DR   DIP; DIP-61659N; -.
DR   IntAct; P12355; 2.
DR   MINT; P12355; -.
DR   PRIDE; P12355; -.
DR   OrthoDB; 1476188at2759; -.
DR   EvolutionaryTrace; P12355; -.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0009538; C:photosystem I reaction center; IEA:InterPro.
DR   GO; GO:0051219; F:phosphoprotein binding; IPI:CAFA.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   DisProt; DP00990; -.
DR   Gene3D; 1.10.8.110; -; 1.
DR   InterPro; IPR003666; PSI_PsaF.
DR   InterPro; IPR036577; PSI_PsaF_sf.
DR   PANTHER; PTHR34939; PTHR34939; 1.
DR   Pfam; PF02507; PSI_PsaF; 1.
DR   SUPFAM; SSF81536; SSF81536; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Direct protein sequencing; Photosynthesis;
KW   Photosystem I; Plastid; Thylakoid; Transit peptide.
FT   TRANSIT         1..77
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           78..231
FT                   /note="Photosystem I reaction center subunit III,
FT                   chloroplastic"
FT                   /id="PRO_0000029346"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           89..106
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           114..136
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:3LW5"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           161..184
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           193..196
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           200..207
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           208..212
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           213..221
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   STRAND          224..227
FT                   /evidence="ECO:0007829|PDB:6LY5"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:2WSC"
SQ   SEQUENCE   231 AA;  25412 MW;  270E1BAC159D79B4 CRC64;
     MSFTIPTNLY KPLATKPKHL SSSSFAPRSK IVCQQENDQQ QPKKLELAKV GANAAAALAL
     SSVLLSSWSV APDAAMADIA GLTPCKESKQ FAKREKQALK KLQASLKLYA DDSAPALAIK
     ATMEKTKKRF DNYGKYGLLC GSDGLPHLIV SGDQRHWGEF ITPGILFLYI AGWIGWVGRS
     YLIAIRDEKK PTQKEIIIDV PLASSLLFRG FSWPVAAYRE LLNGELVDNN F