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Outer envelope pore protein 16-1, chloroplastic (Chloroplastic outer envelope pore protein of 16 kDa 1) (AtOEP16-1) (OEP16-1) (Outer plastid envelope protein 16-L) (AtOEP16-L) (Leave outer plastid envelope protein 16) (Protochlorophyllide-dependent translocon protein 16) (Ptc16)

 OP161_ARATH             Reviewed;         148 AA.
Q9ZV24; Q8LGH9;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
12-SEP-2018, entry version 110.
RecName: Full=Outer envelope pore protein 16-1, chloroplastic;
AltName: Full=Chloroplastic outer envelope pore protein of 16 kDa 1;
Short=AtOEP16-1;
Short=OEP16-1;
AltName: Full=Outer plastid envelope protein 16-L;
Short=AtOEP16-L;
Short=Leave outer plastid envelope protein 16;
AltName: Full=Protochlorophyllide-dependent translocon protein 16;
Short=Ptc16;
Name=OEP161; Synonyms=PTC16; OrderedLocusNames=At2g28900;
ORFNames=F8N16.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND REVIEW.
PubMed=17098851; DOI=10.1104/pp.106.090688;
Murcha M.W., Elhafez D., Lister R., Tonti-Filippini J.,
Baumgartner M., Philippar K., Carrie C., Mokranjac D., Soll J.,
Whelan J.;
"Characterization of the preprotein and amino acid transporter gene
family in Arabidopsis.";
Plant Physiol. 143:199-212(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY,
AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=cv. Wassilewskija;
PubMed=12766230; DOI=10.1074/mcp.M300030-MCP200;
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
Garin J., Joyard J., Rolland N.;
"Proteomics of the chloroplast envelope membranes from Arabidopsis
thaliana.";
Mol. Cell. Proteomics 2:325-345(2003).
[7]
GENE FAMILY.
PubMed=12649433; DOI=10.1110/ps.0237503;
Schleiff E., Eichacker L.A., Eckart K., Becker T., Mirus O., Stahl T.,
Soll J.;
"Prediction of the plant beta-barrel proteome: a case study of the
chloroplast outer envelope.";
Protein Sci. 12:748-759(2003).
[8]
FUNCTION AS PORA TRANSLOCASE.
PubMed=14769929; DOI=10.1073/pnas.0301962101;
Reinbothe S., Quigley F., Springer A., Schemenewitz A., Reinbothe C.;
"The outer plastid envelope protein Oep16: role as precursor
translocase in import of protochlorophyllide oxidoreductase A.";
Proc. Natl. Acad. Sci. U.S.A. 101:2203-2208(2004).
[9]
ACTIVITY REGULATION, AND INTERACTION WITH PPORA AND TOC33.
PubMed=15773849; DOI=10.1111/j.1365-313X.2005.02353.x;
Reinbothe S., Pollmann S., Springer A., James R.J., Tichtinsky G.,
Reinbothe C.;
"A role of Toc33 in the protochlorophyllide-dependent plastid import
pathway of NADPH:protochlorophyllide oxidoreductase (POR) A.";
Plant J. 42:1-12(2005).
[10]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16709189; DOI=10.1111/j.1365-313X.2006.02741.x;
Drea S.C., Lao N.T., Wolfe K.H., Kavanagh T.A.;
"Gene duplication, exon gain and neofunctionalization of OEP16-related
genes in land plants.";
Plant J. 46:723-735(2006).
[11]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GENE FAMILY.
PubMed=17202255; DOI=10.1073/pnas.0610062104;
Philippar K., Geis T., Ilkavets I., Oster U., Schwenkert S.,
Meurer J., Soll J.;
"Chloroplast biogenesis: the use of mutants to study the etioplast-
chloroplast transition.";
Proc. Natl. Acad. Sci. U.S.A. 104:678-683(2007).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=17261815; DOI=10.1073/pnas.0610934104;
Pollmann S., Springer A., Buhr F., Lahroussi A., Samol I.,
Bonneville J.-M., Tichtinsky G., von Wettstein D., Reinbothe C.,
Reinbothe S.;
"A plant porphyria related to defects in plastid import of
protochlorophyllide oxidoreductase A.";
Proc. Natl. Acad. Sci. U.S.A. 104:2019-2023(2007).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=19567834; DOI=10.1073/pnas.0902145106;
Pudelski B., Soll J., Philippar K.;
"A search for factors influencing etioplast-chloroplast transition.";
Proc. Natl. Acad. Sci. U.S.A. 106:12201-12206(2009).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21098557; DOI=10.1093/pcp/pcq176;
Samol I., Buhr F., Springer A., Pollmann S., Lahroussi A., Rossig C.,
von Wettstein D., Reinbothe C., Reinbothe S.;
"Implication of the oep16-1 mutation in a flu-independent, singlet
oxygen-regulated cell death pathway in Arabidopsis thaliana.";
Plant Cell Physiol. 52:84-95(2011).
[15]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=21098556; DOI=10.1093/pcp/pcq177;
Samol I., Rossig C., Buhr F., Springer A., Pollmann S., Lahroussi A.,
von Wettstein D., Reinbothe C., Reinbothe S.;
"The outer chloroplast envelope protein OEP16-1 for plastid import of
NADPH:protochlorophyllide oxidoreductase A in Arabidopsis thaliana.";
Plant Cell Physiol. 52:96-111(2011).
-!- FUNCTION: Voltage-dependent high-conductance channel with a slight
cation-selectivity; selective for amino acids but excludes
triosephosphates or uncharged sugars (By similarity). Non-
essential amino acid-selective channel protein and translocation
pore for NADPH:protochlorophyllide oxidoreductase A (PORA) and
possibly PORB. Involved in PORA precursor (pPORA) import and thus
confers photoprotection onto etiolated seedlings during greening.
{ECO:0000250, ECO:0000269|PubMed:14769929,
ECO:0000269|PubMed:17202255, ECO:0000269|PubMed:17261815,
ECO:0000269|PubMed:19567834, ECO:0000269|PubMed:21098556,
ECO:0000269|PubMed:21098557}.
-!- ACTIVITY REGULATION: Stimulated by GTP.
{ECO:0000269|PubMed:15773849}.
-!- SUBUNIT: Homodimer and oligomers in membrane (By similarity).
Forms large complexes including TOC33, pPORA and OEP161 during
pPORA import into plastids at the plastid envelope membrane.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Multi-
pass membrane protein. Plastid, etioplast membrane; Multi-pass
membrane protein.
-!- TISSUE SPECIFICITY: Expressed predominantly in leaves and
cotyledons. {ECO:0000269|PubMed:16709189,
ECO:0000269|PubMed:17202255}.
-!- INDUCTION: Transient reduction upon de-etiolation (illuminated 5-
day-old etiolated seedlings) (at protein level). Strongly induced
by low-temperature stress and weakly in response to osmotic
stress, salicylic acid (SA) and exogenous abscisic acid (ABA)
treatments. {ECO:0000269|PubMed:16709189,
ECO:0000269|PubMed:21098556}.
-!- DISRUPTION PHENOTYPE: Strong red Pchlide fluorescence after 3.5-4
days of growth in the dark, and cell death after subsequent
illumination. Conditional seedling lethal phenotype related to
defects in import and assembly of NADPH:protochlorophyllide
(Pchlide) oxidoreductase A; excess Pchlide accumulated in the dark
operates as photosensitizer and provokes cell death during
greening. {ECO:0000269|PubMed:17261815,
ECO:0000269|PubMed:19567834, ECO:0000269|PubMed:21098556,
ECO:0000269|PubMed:21098557}.
-!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. Plastid outer
envelope porin OEP16 (TC 1.B.30) subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; DQ386642; ABD48954.1; -; mRNA.
EMBL; AC005727; AAC79594.1; -; Genomic_DNA.
EMBL; CP002685; AEC08186.1; -; Genomic_DNA.
EMBL; AY045593; AAK73951.1; -; mRNA.
EMBL; AY093782; AAM10398.1; -; mRNA.
EMBL; AY084261; AAM60853.1; -; mRNA.
PIR; C84690; C84690.
RefSeq; NP_180456.1; NM_128449.3.
UniGene; At.25376; -.
BioGrid; 2789; 2.
IntAct; Q9ZV24; 1.
STRING; 3702.AT2G28900.1; -.
iPTMnet; Q9ZV24; -.
PaxDb; Q9ZV24; -.
PRIDE; Q9ZV24; -.
DNASU; 817439; -.
EnsemblPlants; AT2G28900.1; AT2G28900.1; AT2G28900.
GeneID; 817439; -.
Gramene; AT2G28900.1; AT2G28900.1; AT2G28900.
KEGG; ath:AT2G28900; -.
Araport; AT2G28900; -.
TAIR; locus:2053185; AT2G28900.
eggNOG; ENOG410IX6C; Eukaryota.
eggNOG; ENOG410YKVU; LUCA.
HOGENOM; HOG000239997; -.
InParanoid; Q9ZV24; -.
OMA; HTLKKMC; -.
OrthoDB; EOG09360R5Z; -.
PhylomeDB; Q9ZV24; -.
PRO; PR:Q9ZV24; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9ZV24; baseline and differential.
Genevisible; Q9ZV24; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
GO; GO:0034426; C:etioplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0005744; C:mitochondrial inner membrane presequence translocase complex; IBA:GO_Central.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0009527; C:plastid outer membrane; IDA:TAIR.
GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0015171; F:amino acid transmembrane transporter activity; IMP:TAIR.
GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0045037; P:protein import into chloroplast stroma; IDA:TAIR.
GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009749; P:response to glucose; IEP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
GO; GO:0009744; P:response to sucrose; IEP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
1: Evidence at protein level;
Chloroplast; Complete proteome; Ion transport; Membrane; Plastid;
Plastid outer membrane; Porin; Reference proteome; Transmembrane;
Transmembrane beta strand; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12766230}.
CHAIN 2 148 Outer envelope pore protein 16-1,
chloroplastic.
/FTId=PRO_0000415696.
TRANSMEM 75 91 Helical. {ECO:0000255}.
TRANSMEM 102 118 Helical. {ECO:0000255}.
TRANSMEM 125 142 Helical. {ECO:0000255}.
REGION 2 73 Contains 4 beta strands. {ECO:0000250}.
CONFLICT 54 54 D -> E (in Ref. 5; AAM60853).
{ECO:0000305}.
SEQUENCE 148 AA; 15482 MW; 5D62180BE3D843C3 CRC64;
MPSSTFSGTV STPKLSVAVD MGNPFLNLTV DAFLKIGAVG VTKSLAEDTY KAIDKGSLSK
STLEHALKKL CKEGVYWGAA GGVYIGTEYG IERIRGSRDW KNAMLAGAAT GAVLSAVGKK
GKDTIVIDAI LGGALATASQ FVNNHYFY


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