OP161_ARATH
ID OP161_ARATH Reviewed; 148 AA.
AC Q9ZV24; Q8LGH9;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Outer envelope pore protein 16-1, chloroplastic;
DE AltName: Full=Chloroplastic outer envelope pore protein of 16 kDa 1;
DE Short=AtOEP16-1;
DE Short=OEP16-1;
DE AltName: Full=Outer plastid envelope protein 16-L;
DE Short=AtOEP16-L;
DE Short=Leave outer plastid envelope protein 16;
DE AltName: Full=Protochlorophyllide-dependent translocon protein 16;
DE Short=Ptc16;
GN Name=OEP161; Synonyms=PTC16; OrderedLocusNames=At2g28900;
GN ORFNames=F8N16.19;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND REVIEW.
RX PubMed=17098851; DOI=10.1104/pp.106.090688;
RA Murcha M.W., Elhafez D., Lister R., Tonti-Filippini J., Baumgartner M.,
RA Philippar K., Carrie C., Mokranjac D., Soll J., Whelan J.;
RT "Characterization of the preprotein and amino acid transporter gene family
RT in Arabidopsis.";
RL Plant Physiol. 143:199-212(2007).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [7]
RP GENE FAMILY.
RX PubMed=12649433; DOI=10.1110/ps.0237503;
RA Schleiff E., Eichacker L.A., Eckart K., Becker T., Mirus O., Stahl T.,
RA Soll J.;
RT "Prediction of the plant beta-barrel proteome: a case study of the
RT chloroplast outer envelope.";
RL Protein Sci. 12:748-759(2003).
RN [8]
RP FUNCTION AS PORA TRANSLOCASE.
RX PubMed=14769929; DOI=10.1073/pnas.0301962101;
RA Reinbothe S., Quigley F., Springer A., Schemenewitz A., Reinbothe C.;
RT "The outer plastid envelope protein Oep16: role as precursor translocase in
RT import of protochlorophyllide oxidoreductase A.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2203-2208(2004).
RN [9]
RP ACTIVITY REGULATION, AND INTERACTION WITH PPORA AND TOC33.
RX PubMed=15773849; DOI=10.1111/j.1365-313x.2005.02353.x;
RA Reinbothe S., Pollmann S., Springer A., James R.J., Tichtinsky G.,
RA Reinbothe C.;
RT "A role of Toc33 in the protochlorophyllide-dependent plastid import
RT pathway of NADPH:protochlorophyllide oxidoreductase (POR) A.";
RL Plant J. 42:1-12(2005).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16709189; DOI=10.1111/j.1365-313x.2006.02741.x;
RA Drea S.C., Lao N.T., Wolfe K.H., Kavanagh T.A.;
RT "Gene duplication, exon gain and neofunctionalization of OEP16-related
RT genes in land plants.";
RL Plant J. 46:723-735(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=17202255; DOI=10.1073/pnas.0610062104;
RA Philippar K., Geis T., Ilkavets I., Oster U., Schwenkert S., Meurer J.,
RA Soll J.;
RT "Chloroplast biogenesis: the use of mutants to study the etioplast-
RT chloroplast transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:678-683(2007).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=17261815; DOI=10.1073/pnas.0610934104;
RA Pollmann S., Springer A., Buhr F., Lahroussi A., Samol I.,
RA Bonneville J.-M., Tichtinsky G., von Wettstein D., Reinbothe C.,
RA Reinbothe S.;
RT "A plant porphyria related to defects in plastid import of
RT protochlorophyllide oxidoreductase A.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2019-2023(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19567834; DOI=10.1073/pnas.0902145106;
RA Pudelski B., Soll J., Philippar K.;
RT "A search for factors influencing etioplast-chloroplast transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12201-12206(2009).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21098557; DOI=10.1093/pcp/pcq176;
RA Samol I., Buhr F., Springer A., Pollmann S., Lahroussi A., Rossig C.,
RA von Wettstein D., Reinbothe C., Reinbothe S.;
RT "Implication of the oep16-1 mutation in a flu-independent, singlet oxygen-
RT regulated cell death pathway in Arabidopsis thaliana.";
RL Plant Cell Physiol. 52:84-95(2011).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21098556; DOI=10.1093/pcp/pcq177;
RA Samol I., Rossig C., Buhr F., Springer A., Pollmann S., Lahroussi A.,
RA von Wettstein D., Reinbothe C., Reinbothe S.;
RT "The outer chloroplast envelope protein OEP16-1 for plastid import of
RT NADPH:protochlorophyllide oxidoreductase A in Arabidopsis thaliana.";
RL Plant Cell Physiol. 52:96-111(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 (By similarity). Non-essential
CC amino acid-selective channel protein and translocation pore for
CC NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB.
CC Involved in PORA precursor (pPORA) import and thus confers
CC photoprotection onto etiolated seedlings during greening. {ECO:0000250,
CC ECO:0000269|PubMed:14769929, ECO:0000269|PubMed:17202255,
CC ECO:0000269|PubMed:17261815, ECO:0000269|PubMed:19567834,
CC ECO:0000269|PubMed:21098556, ECO:0000269|PubMed:21098557}.
CC -!- ACTIVITY REGULATION: Stimulated by GTP. {ECO:0000269|PubMed:15773849}.
CC -!- SUBUNIT: Homodimer and oligomers in membrane (By similarity). Forms
CC large complexes including TOC33, pPORA and OEP161 during pPORA import
CC into plastids at the plastid envelope membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Multi-pass
CC membrane protein. Plastid, etioplast membrane; Multi-pass membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in leaves and cotyledons.
CC {ECO:0000269|PubMed:16709189, ECO:0000269|PubMed:17202255}.
CC -!- INDUCTION: Transient reduction upon de-etiolation (illuminated 5-day-
CC old etiolated seedlings) (at protein level). Strongly induced by low-
CC temperature stress and weakly in response to osmotic stress, salicylic
CC acid (SA) and exogenous abscisic acid (ABA) treatments.
CC {ECO:0000269|PubMed:16709189, ECO:0000269|PubMed:21098556}.
CC -!- DISRUPTION PHENOTYPE: Strong red Pchlide fluorescence after 3.5-4 days
CC of growth in the dark, and cell death after subsequent illumination.
CC Conditional seedling lethal phenotype related to defects in import and
CC assembly of NADPH:protochlorophyllide (Pchlide) oxidoreductase A;
CC excess Pchlide accumulated in the dark operates as photosensitizer and
CC provokes cell death during greening. {ECO:0000269|PubMed:17261815,
CC ECO:0000269|PubMed:19567834, ECO:0000269|PubMed:21098556,
CC ECO:0000269|PubMed:21098557}.
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; DQ386642; ABD48954.1; -; mRNA.
DR EMBL; AC005727; AAC79594.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08186.1; -; Genomic_DNA.
DR EMBL; AY045593; AAK73951.1; -; mRNA.
DR EMBL; AY093782; AAM10398.1; -; mRNA.
DR EMBL; AY084261; AAM60853.1; -; mRNA.
DR PIR; C84690; C84690.
DR RefSeq; NP_180456.1; NM_128449.3.
DR AlphaFoldDB; Q9ZV24; -.
DR SMR; Q9ZV24; -.
DR BioGRID; 2789; 4.
DR IntAct; Q9ZV24; 1.
DR STRING; 3702.AT2G28900.1; -.
DR iPTMnet; Q9ZV24; -.
DR PaxDb; Q9ZV24; -.
DR PRIDE; Q9ZV24; -.
DR ProteomicsDB; 249364; -.
DR DNASU; 817439; -.
DR EnsemblPlants; AT2G28900.1; AT2G28900.1; AT2G28900.
DR GeneID; 817439; -.
DR Gramene; AT2G28900.1; AT2G28900.1; AT2G28900.
DR KEGG; ath:AT2G28900; -.
DR Araport; AT2G28900; -.
DR TAIR; locus:2053185; AT2G28900.
DR eggNOG; ENOG502RZS0; Eukaryota.
DR HOGENOM; CLU_100380_2_0_1; -.
DR InParanoid; Q9ZV24; -.
DR OMA; HTLKKMC; -.
DR OrthoDB; 1501446at2759; -.
DR PhylomeDB; Q9ZV24; -.
DR PRO; PR:Q9ZV24; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV24; baseline and differential.
DR Genevisible; Q9ZV24; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0034426; C:etioplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009527; C:plastid outer membrane; IDA:TAIR.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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; Reference proteome; Transmembrane; Transmembrane beta strand;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12766230"
FT CHAIN 2..148
FT /note="Outer envelope pore protein 16-1, chloroplastic"
FT /id="PRO_0000415696"
FT TRANSMEM 75..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 2..73
FT /note="Contains 4 beta strands"
FT /evidence="ECO:0000250"
FT CONFLICT 54
FT /note="D -> E (in Ref. 5; AAM60853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 15482 MW; 5D62180BE3D843C3 CRC64;
MPSSTFSGTV STPKLSVAVD MGNPFLNLTV DAFLKIGAVG VTKSLAEDTY KAIDKGSLSK
STLEHALKKL CKEGVYWGAA GGVYIGTEYG IERIRGSRDW KNAMLAGAAT GAVLSAVGKK
GKDTIVIDAI LGGALATASQ FVNNHYFY
