OEP16_PEA
ID OEP16_PEA Reviewed; 146 AA.
AC Q41050;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Outer envelope pore protein 16, chloroplastic;
DE AltName: Full=Chloroplastic outer envelope pore protein of 16 kDa;
GN Name=OEP16;
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 [MRNA], FUNCTION, SUBUNIT, AND BETA STRANDS.
RC STRAIN=cv. Golf; TISSUE=Leaf;
RX PubMed=9256512; DOI=10.1073/pnas.94.17.9504;
RA Pohlmeyer K., Soll J., Steinkamp T., Hinnah S., Wagner R.;
RT "Isolation and characterization of an amino acid-selective channel protein
RT present in the chloroplastic outer envelope membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9504-9509(1997).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10998242; DOI=10.1021/bi001034m;
RA Linke D., Frank J., Holzwarth J.F., Soll J., Boettcher C., Fromme P.;
RT "In vitro reconstitution and biophysical characterization of OEP16, an
RT outer envelope pore protein of pea chloroplasts.";
RL Biochemistry 39:11050-11056(2000).
RN [3]
RP FUNCTION, TOPOLOGY, AND MUTAGENESIS OF CYS-71.
RX PubMed=10766798; DOI=10.1074/jbc.275.16.11758;
RA Steinkamp T., Hill K., Hinnah S.C., Wagner R., Roehl T., Pohlmeyer K.,
RA Soll J.;
RT "Identification of the pore-forming region of the outer chloroplast
RT envelope protein OEP16.";
RL J. Biol. Chem. 275:11758-11764(2000).
RN [4]
RP FUNCTION, TOPOLOGY, AND SUBUNIT.
RX PubMed=21878393; DOI=10.1016/j.pep.2011.08.004;
RA Ni D.Q., Zook J., Klewer D.A., Nieman R.A., Soll J., Fromme P.;
RT "Isolation, folding and structural investigations of the amino acid
RT transporter OEP16.";
RL Protein Expr. Purif. 80:157-168(2011).
CC -!- FUNCTION: Voltage-dependent high-conductance channel with a slight
CC cation-selectivity; selective for amino acids but excludes
CC triosephosphates or uncharged sugars. Non-essential amino acid-
CC selective channel protein and translocation pore for
CC NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB.
CC {ECO:0000269|PubMed:10766798, ECO:0000269|PubMed:21878393,
CC ECO:0000269|PubMed:9256512}.
CC -!- SUBUNIT: Homodimer and oligomers in membrane.
CC {ECO:0000269|PubMed:21878393, ECO:0000269|PubMed:9256512}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Plastid,
CC etioplast membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. Plastid outer
CC envelope porin OEP16 (TC 1.B.30) subfamily. {ECO:0000305}.
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DR EMBL; Z73553; CAA97910.1; -; mRNA.
DR PIR; T06471; T06471.
DR AlphaFoldDB; Q41050; -.
DR BMRB; Q41050; -.
DR SMR; Q41050; -.
DR TCDB; 1.B.30.1.1; the plastid outer envelope porin of 16 kda (oep16) family.
DR EnsemblPlants; Psat5g284600.2; Psat5g284600.2.cds; Psat5g284600.
DR Gramene; Psat5g284600.2; Psat5g284600.2.cds; Psat5g284600.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034426; C:etioplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IDA:UniProtKB.
DR InterPro; IPR045238; Tim23-like.
DR PANTHER; PTHR15371; PTHR15371; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Ion transport; Membrane; Plastid; Plastid outer membrane;
KW Porin; Transmembrane; Transmembrane beta strand; Transmembrane helix;
KW Transport.
FT CHAIN 1..146
FT /note="Outer envelope pore protein 16, chloroplastic"
FT /id="PRO_0000415700"
FT TRANSMEM 75..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..73
FT /note="Contains 4 beta strands"
FT MUTAGEN 71
FT /note="C->S: Loss of CuCl(2) sensitivity of the channel."
FT /evidence="ECO:0000269|PubMed:10766798"
SQ SEQUENCE 146 AA; 15490 MW; B72E24ABF6AAC2AB CRC64;
MPRSSFSGSL SSPKLDVVID MGNPFLNLTV DGFLKIGAVA ATRSVAEDTF HIIRKGSISS
NDFEKSLKKM CKEGAYWGAI AGVYVGMEYG VERIRGTRDW KNAMFGGAVT GALVSAASNN
KKDKIAVDAI TGAAIATAAE FINYLT