ID   DGS1_ARATH              Reviewed;         602 AA.
AC   Q8GUK1; Q8GWL0; Q94CL3;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Protein DGS1, mitochondrial {ECO:0000305};
DE   AltName: Full=Protein DGD1 SUPPRESSOR 1 {ECO:0000303|PubMed:18208519};
DE   Flags: Precursor;
GN   Name=DGS1 {ECO:0000303|PubMed:18208519};
GN   OrderedLocusNames=At5g12290 {ECO:0000312|Araport:AT5G12290};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-457.
RX   PubMed=18208519; DOI=10.1111/j.1365-313x.2008.03417.x;
RA   Xu C., Moellering E.R., Fan J., Benning C.;
RT   "Mutation of a mitochondrial outer membrane protein affects chloroplast
RT   lipid biosynthesis.";
RL   Plant J. 54:163-175(2008).
CC   -!- FUNCTION: Involved in galactoglycerolipid biosynthesis. May contribute
CC       to an intracellular signal that regulates an alternative DGD1-
CC       independent galactoglycerolipid biosynthesis pathway in chloroplasts.
CC       {ECO:0000269|PubMed:18208519}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:18208519}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC42890.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL592312; CAC42890.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED91788.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68882.1; -; Genomic_DNA.
DR   EMBL; AK118777; BAC43370.1; -; mRNA.
DR   EMBL; BT002450; AAO00810.1; -; mRNA.
DR   EMBL; BT008365; AAP37724.1; -; mRNA.
DR   RefSeq; NP_001330600.1; NM_001343234.1.
DR   RefSeq; NP_568262.2; NM_121267.5.
DR   AlphaFoldDB; Q8GUK1; -.
DR   STRING; 3702.AT5G12290.1; -.
DR   iPTMnet; Q8GUK1; -.
DR   PaxDb; Q8GUK1; -.
DR   PRIDE; Q8GUK1; -.
DR   ProteomicsDB; 224039; -.
DR   EnsemblPlants; AT5G12290.1; AT5G12290.1; AT5G12290.
DR   EnsemblPlants; AT5G12290.4; AT5G12290.4; AT5G12290.
DR   GeneID; 831104; -.
DR   Gramene; AT5G12290.1; AT5G12290.1; AT5G12290.
DR   Gramene; AT5G12290.4; AT5G12290.4; AT5G12290.
DR   KEGG; ath:AT5G12290; -.
DR   Araport; AT5G12290; -.
DR   TAIR; locus:505006597; AT5G12290.
DR   eggNOG; ENOG502QTT6; Eukaryota.
DR   HOGENOM; CLU_035193_0_0_1; -.
DR   InParanoid; Q8GUK1; -.
DR   OMA; QFWQSRA; -.
DR   OrthoDB; 688996at2759; -.
DR   PhylomeDB; Q8GUK1; -.
DR   PRO; PR:Q8GUK1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8GUK1; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0032991; C:protein-containing complex; IDA:TAIR.
DR   GO; GO:0019375; P:galactolipid biosynthetic process; IMP:TAIR.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:TAIR.
DR   InterPro; IPR013946; NCA2.
DR   PANTHER; PTHR28234; PTHR28234; 1.
DR   Pfam; PF08637; NCA2; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..602
FT                   /note="Protein DGS1, mitochondrial"
FT                   /id="PRO_0000435794"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         457
FT                   /note="D->N: In dgs1; partially restores
FT                   digalactoglycerolipid content in the dgd1 mutant."
FT                   /evidence="ECO:0000269|PubMed:18208519"
FT   CONFLICT        154
FT                   /note="D -> G (in Ref. 3; BAC43370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   602 AA;  68894 MW;  446D017974ADEAED CRC64;
     MDSQPPVNES TPSTALSNFG ELVPFYSSYL WNRLASLLPT SKPIFLGKIS NLYRQTVSRK
     RSISFPLPLP SDFPSSSTIT SNVSADTARI HGVLEEIMAD VLSNLHDIQK SLDFWRSRAE
     GSNARKAYFM IFERGPTAFV NESTKFVSKS LSEDSAMQHL CQSSSSHMTE RMRVLVELRS
     ALASFIAQLY VELDKRGEDL VKIPEKALPS LLAVINGLFS NLEGSFSHLH AVRECDSSVD
     GSYPMPLVFD RLPEVNEEGS QWTDCELTDA INLVHKNLEK LNSYLSVMVG KHRKPRRMTL
     YWVRYTCGAV GLSVFSIWLL RHSSLMGSSD IENWVHDAKE ATMSFFSDHV EQPLLSIRDE
     LFDTFRKRHK GVMETEEVQL TQDSLHRMLR NFCEQATREK VPDNASDQEM LEVVMNRYEK
     ELVHPIHNLL SGELARGLLI QVQKLKLDIE TAMLELDQIL RANEINFAIL AALPAFFLSI
     VMLTVLRTWL KKDSKAQGRG RIARIHRRLL VVEIEKRIMQ YQSYIEQGRD KDAETVFGLL
     IYSLERLYRV VEKPARATDE WDLVKQDLIE LGRPQQQTSY KLTVTQRLVT VYDCLLPTLK
     RQ