OEP21_PEA
ID OEP21_PEA Reviewed; 177 AA.
AC Q9SM57;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Outer envelope pore protein 21, chloroplastic;
DE AltName: Full=Chloroplastic outer envelope pore protein of 21 kDa;
DE Short=gOEP21;
GN Name=OEP21;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Golf; TISSUE=Leaf;
RX PubMed=10523295; DOI=10.1093/emboj/18.20.5505;
RA Boelter B., Soll J., Hill K., Hemmler R., Wagner R.;
RT "A rectifying ATP-regulated solute channel in the chloroplastic outer
RT envelope from pea.";
RL EMBO J. 18:5505-5516(1999).
RN [2]
RP FUNCTION, TOPOLOGY, AND MUTAGENESIS OF 163-PHE--LYS-168.
RC STRAIN=cv. Golf;
RX PubMed=16473880; DOI=10.1074/jbc.m513586200;
RA Hemmler R., Becker T., Schleiff E., Boelter B., Stahl T., Soll J.,
RA Goetze T.A., Braams S., Wagner R.;
RT "Molecular properties of Oep21, an ATP-regulated anion-selective solute
RT channel from the outer chloroplast membrane.";
RL J. Biol. Chem. 281:12020-12029(2006).
CC -!- FUNCTION: Voltage-dependent rectifying anion channel that facilitates
CC the translocation between chloroplast and cytoplasm of phosphorylated
CC carbohydrates such as triosephosphate, 3-phosphoglycerate and inorganic
CC phosphate (Pi) depending of ATP to triosephosphate ratio in the
CC plastidial intermembrane space; in high triosephosphate/ATP conditions
CC (e.g. photosynthesis), export of triosphosphate from chloroplast
CC (outward rectifying channels), but in high ATP/triosephosphate
CC conditions (e.g. dark phase), import of phosphosolutes (inward
CC rectifying channels). {ECO:0000269|PubMed:10523295,
CC ECO:0000269|PubMed:16473880}.
CC -!- SUBCELLULAR LOCATION: Plastid, etioplast membrane
CC {ECO:0000269|PubMed:10523295}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10523295}. Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:10523295}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10523295}. Note=Present in non-green root plastids.
CC -!- TISSUE SPECIFICITY: Present in roots, shoots and leaves.
CC {ECO:0000269|PubMed:10523295}.
CC -!- SIMILARITY: Belongs to the plastid outer envelope porin OEP21 (TC
CC 1.B.29) family. {ECO:0000305}.
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DR EMBL; AJ009987; CAB58442.1; -; Genomic_DNA.
DR PDB; 7BGH; NMR; -; A=1-177.
DR PDBsum; 7BGH; -.
DR AlphaFoldDB; Q9SM57; -.
DR SMR; Q9SM57; -.
DR TCDB; 1.B.29.1.1; the plastid outer envelope porin of 21 kda (oep21) family.
DR EnsemblPlants; Psat5g008840.1; Psat5g008840.1.cds; Psat5g008840.
DR Gramene; Psat5g008840.1; Psat5g008840.1.cds; Psat5g008840.
DR GO; GO:0034426; C:etioplast membrane; IDA:UniProtKB.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IDA:UniProtKB.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR GO; GO:0044070; P:regulation of anion transport; IDA:UniProtKB.
DR InterPro; IPR034575; OEP21.
DR PANTHER; PTHR35993; PTHR35993; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Ion transport; Membrane; Plastid;
KW Plastid outer membrane; Porin; Transmembrane; Transmembrane beta strand;
KW Transport.
FT CHAIN 1..177
FT /note="Outer envelope pore protein 21, chloroplastic"
FT /id="PRO_0000415551"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..31
FT /note="Beta stranded; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..55
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..65
FT /note="Beta stranded; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..91
FT /note="Beta stranded; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..97
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..107
FT /note="Beta stranded; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..130
FT /note="Beta stranded; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..137
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..147
FT /note="Beta stranded; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..162
FT /note="Beta stranded; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..168
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..177
FT /note="Beta stranded; Name=8"
FT /evidence="ECO:0000255"
FT MUTAGEN 163..168
FT /note="Missing: Reduced ion selectivity tuning."
FT /evidence="ECO:0000269|PubMed:16473880"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 13..25
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 44..54
FT /evidence="ECO:0007829|PDB:7BGH"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 79..95
FT /evidence="ECO:0007829|PDB:7BGH"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 100..113
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:7BGH"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:7BGH"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7BGH"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:7BGH"
SQ SEQUENCE 177 AA; 20444 MW; 0540BA372BA6B76B CRC64;
METSLRYGGD SKALKIHAKE KLRIDTNTFF QVRGGLDTKT GQPSSGSALI RHFYPNFSAT
LGVGVRYDKQ DSVGVRYAKN DKLRYTVLAK KTFPVTNDGL VNFKIKGGCD VDQDFKEWKS
RGGAEFSWNV FNFQKDQDVR LRIGYEAFEQ VPYLQIRENN WTFNADYKGR WNVRYDL
