OP162_ARATH
ID OP162_ARATH Reviewed; 178 AA.
AC Q0WMZ5; O23464; Q8L9N5;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Outer envelope pore protein 16-2, chloroplastic;
DE AltName: Full=Chloroplastic outer envelope pore protein of 16 kDa 2;
DE Short=AtOEP16-2;
DE Short=OEP16-2;
DE AltName: Full=Outer plastid envelope protein 16-S;
DE Short=AtOEP16-S;
DE Short=Seeds outer plastid envelope protein 16;
GN Name=OEP162; OrderedLocusNames=At4g16160; ORFNames=dl4120w, FCAALL.207;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 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 [7]
RP INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [8]
RP 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 [9]
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).
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 {ECO:0000250, ECO:0000269|PubMed:17202255}.
CC -!- SUBUNIT: Homodimer and oligomers in membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:17098851, ECO:0000269|PubMed:17202255}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:17098851,
CC ECO:0000269|PubMed:17202255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0WMZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WMZ5-2; Sequence=VSP_042320;
CC -!- TISSUE SPECIFICITY: Detected in pollen and seeds. Present in leaves and
CC cotyledons. {ECO:0000269|PubMed:16709189, ECO:0000269|PubMed:17202255}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed during the maturation phase in
CC seeds and pollen grains, both desiccation-tolerant tissues.
CC {ECO:0000269|PubMed:16709189}.
CC -!- INDUCTION: Regulated by ABI3 and ABI5. {ECO:0000269|PubMed:16709189}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. Plastid outer
CC envelope porin OEP16 (TC 1.B.30) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10395.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78658.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97340; CAB10395.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161543; CAB78658.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83705.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83706.1; -; Genomic_DNA.
DR EMBL; AK229661; BAF01505.1; -; mRNA.
DR EMBL; AY088334; AAM65873.1; -; mRNA.
DR PIR; A71428; A71428.
DR RefSeq; NP_567488.1; NM_117712.2. [Q0WMZ5-2]
DR RefSeq; NP_849394.1; NM_179063.2. [Q0WMZ5-1]
DR AlphaFoldDB; Q0WMZ5; -.
DR STRING; 3702.AT4G16160.2; -.
DR TCDB; 1.B.30.1.2; the plastid outer envelope porin of 16 kda (oep16) family.
DR PaxDb; Q0WMZ5; -.
DR PRIDE; Q0WMZ5; -.
DR ProMEX; Q0WMZ5; -.
DR ProteomicsDB; 248896; -. [Q0WMZ5-1]
DR DNASU; 827308; -.
DR EnsemblPlants; AT4G16160.1; AT4G16160.1; AT4G16160. [Q0WMZ5-2]
DR EnsemblPlants; AT4G16160.2; AT4G16160.2; AT4G16160. [Q0WMZ5-1]
DR GeneID; 827308; -.
DR Gramene; AT4G16160.1; AT4G16160.1; AT4G16160. [Q0WMZ5-2]
DR Gramene; AT4G16160.2; AT4G16160.2; AT4G16160. [Q0WMZ5-1]
DR KEGG; ath:AT4G16160; -.
DR Araport; AT4G16160; -.
DR TAIR; locus:2130135; AT4G16160.
DR eggNOG; ENOG502RY7Z; Eukaryota.
DR InParanoid; Q0WMZ5; -.
DR OMA; HIVQCAI; -.
DR PhylomeDB; Q0WMZ5; -.
DR PRO; PR:Q0WMZ5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WMZ5; baseline and differential.
DR Genevisible; Q0WMZ5; AT.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0009527; C:plastid outer membrane; ISS: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:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR045238; Tim23-like.
DR PANTHER; PTHR15371; PTHR15371; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Ion transport; Membrane; Plastid;
KW Plastid outer membrane; Porin; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transmembrane helix; Transport.
FT CHAIN 1..178
FT /note="Outer envelope pore protein 16-2, chloroplastic"
FT /id="PRO_0000415697"
FT TRANSMEM 103..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..102
FT /note="Contains beta strands"
FT /evidence="ECO:0000250"
FT VAR_SEQ 59..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_042320"
SQ SEQUENCE 178 AA; 18714 MW; 17CDF6186A41FE82 CRC64;
MEKSGGRIVM DEIRSFEKAH LFDLGHPLLN RIADSFVKAA GVGALQAVSR EAYFTVVDGA
GFDSNNVGPP SEITGNKKHR FPNLRGESSK SLDALVKNTG KESLQWGLAA GLYSGITYGM
TEVRGGAHDW RNSAVAGALT GAAMAMTTSE RTSHEQVVQS ALTGAAISTA ANLLSSVF
