PSBW_SPIOL
ID PSBW_SPIOL Reviewed; 137 AA.
AC Q41387; Q9S8E2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Photosystem II reaction center W protein, chloroplastic;
DE AltName: Full=PSII 6.1 kDa protein;
DE Flags: Precursor;
GN Name=psbW {ECO:0000303|PubMed:7568046};
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], SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND POSSIBLE TOPOLOGY.
RX PubMed=7568046; DOI=10.1073/pnas.92.19.8930;
RA Lorkovic Z.J., Schroeder W.P., Pakrasi H.B., Irrgang K.-D., Herrmann R.G.,
RA Oelmueller R.;
RT "Molecular characterization of PsbW, a nuclear-encoded component of the
RT photosystem II reaction center complex in spinach.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8930-8934(1995).
RN [2]
RP PROTEIN SEQUENCE OF 84-103, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=2644131; DOI=10.1016/0014-5793(89)80482-x;
RA Ikeuchi M., Takio K., Inoue Y.;
RT "N-terminal sequencing of photosystem II low-molecular-mass proteins. 5 and
RT 4.1 kDa components of the O2-evolving core complex from higher plants.";
RL FEBS Lett. 242:263-269(1989).
RN [3]
RP PROTEIN SEQUENCE OF 84-102, VARIANT GLN-89, SUBUNIT, SUBCELLULAR LOCATION,
RP AND POSSIBLE TOPOLOGY.
RX PubMed=7615565; DOI=10.1074/jbc.270.29.17588;
RA Irrgang K.-D., Shi L.X., Funk C., Schroder W.P.;
RT "A nuclear-encoded subunit of the photosystem II reaction center.";
RL J. Biol. Chem. 270:17588-17593(1995).
RN [4]
RP PROTEIN SEQUENCE OF 84-95, SUBUNIT, AND SUBCELLULAR LOCATION.
RA Schroeder W.P., Henrysson T., Aakerlund H.-E.;
RT "Characterization of low molecular mass proteins of photosystem II by N-
RT terminal sequencing.";
RL FEBS Lett. 235:289-292(1988).
RN [5]
RP PROTEIN SEQUENCE OF 84-91, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RX PubMed=9632665; DOI=10.1074/jbc.273.26.16122;
RA Zheleva D., Sharma J., Panico M., Morris H.R., Barber J.;
RT "Isolation and characterization of monomeric and dimeric CP47-reaction
RT center photosystem II complexes.";
RL J. Biol. Chem. 273:16122-16127(1998).
CC -!- FUNCTION: Stabilizes dimeric photosystem II (PSII). In its absence no
CC dimeric PSII accumulates and there is a reduction of monomeric PSII (By
CC similarity). {ECO:0000250|UniProtKB:Q39194}.
CC -!- SUBUNIT: Part of the photosystem II complex. PSII is composed of 1 copy
CC each of membrane proteins PsbA, PsbB, PsbC, PsbD, numerous small
CC proteins, at least 3 peripheral proteins of the oxygen-evolving complex
CC and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000269|PubMed:2644131, ECO:0000269|PubMed:7615565,
CC ECO:0000269|PubMed:9632665, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:2644131, ECO:0000269|PubMed:7615565,
CC ECO:0000269|PubMed:9632665, ECO:0000269|Ref.4}; Single-pass membrane
CC protein {ECO:0000269|PubMed:7615565, ECO:0000305|PubMed:7568046}.
CC Note=The N-terminus is found within the thylakoid lumen
CC (PubMed:7568046, PubMed:7615565). {ECO:0000305|PubMed:7568046}.
CC -!- DEVELOPMENTAL STAGE: Found in etioplastic PSII (i.e. before PSII is
CC fully assembled and functional). {ECO:0000269|PubMed:7568046}.
CC -!- MASS SPECTROMETRY: Mass=5927.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9632665};
CC -!- SIMILARITY: Belongs to the psbW 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; X85038; CAA59409.1; -; mRNA.
DR PIR; S53025; S53025.
DR PDB; 3JCU; EM; 3.20 A; W/w=1-137.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; Q41387; -.
DR SMR; Q41387; -.
DR DIP; DIP-62027N; -.
DR IntAct; Q41387; 1.
DR OrthoDB; 1650754at2759; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR009806; PSII_PsbW_class2.
DR PANTHER; PTHR34552; PTHR34552; 1.
DR Pfam; PF07123; PsbW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Membrane;
KW Photosynthesis; Photosystem II; Plastid; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 65..83
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:2644131,
FT ECO:0000269|PubMed:7615565, ECO:0000269|PubMed:9632665,
FT ECO:0000269|Ref.4"
FT CHAIN 84..137
FT /note="Photosystem II reaction center W protein,
FT chloroplastic"
FT /id="PRO_0000005340"
FT TOPO_DOM 84..103
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:7568046,
FT ECO:0000305|PubMed:7615565"
FT TRANSMEM 104..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..137
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:7568046,
FT ECO:0000305|PubMed:7615565"
FT VARIANT 89
FT /note="M -> Q"
FT /evidence="ECO:0000269|PubMed:7615565"
FT CONFLICT 101
FT /note="S -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 103..124
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 137 AA; 14177 MW; 8DDE38CD7C32ED24 CRC64;
MATITASSSA SLVARASLVH NSRVGVSSSP ILGLPSMTKR SKVTCSIENK PSTTETTTTT
NKSMGASLLA AAAAATISNP AMALVDERMS TEGTGLPFGL SNNLLGWILF GVFGLIWALY
FVYASGLEED EESGLSL