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CJD1_ARATH
ID   CJD1_ARATH              Reviewed;         294 AA.
AC   Q93WG3; Q8H167; Q8LB27; Q9FRS1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Protein CHLOROPLAST J-LIKE DOMAIN 1, chloroplastic {ECO:0000303|PubMed:22028775};
DE   Flags: Precursor;
GN   Name=CJD1 {ECO:0000303|PubMed:22028775};
GN   OrderedLocusNames=At1g08640 {ECO:0000312|Araport:AT1G08640};
GN   ORFNames=F22O13.12 {ECO:0000312|EMBL:AAF99779.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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=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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ARC6, SUBCELLULAR
RP   LOCATION, AND TOPOLOGY.
RC   STRAIN=cv. Columbia;
RX   PubMed=22028775; DOI=10.1371/journal.pone.0025368;
RA   Ajjawi I., Coku A., Froehlich J.E., Yang Y., Osteryoung K.W., Benning C.,
RA   Last R.L.;
RT   "A J-like protein influences fatty acid composition of chloroplast lipids
RT   in Arabidopsis.";
RL   PLoS ONE 6:e25368-e25368(2011).
CC   -!- FUNCTION: Probably involved in the regulation of the fatty acid
CC       metabolic process in chloroplasts, especially chloroplastic
CC       galactolipids monogalactosyldiacylglycerol (MGDG) and
CC       digalactosyldiacylglycerol (DGDG). {ECO:0000269|PubMed:22028775}.
CC   -!- SUBUNIT: Interacts (via J-like domain) with ARC6 (via J domain).
CC       {ECO:0000269|PubMed:22028775}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000269|PubMed:22028775}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Altered fatty acid profiles with a slight
CC       increase of 16:1delta7 and 18:1delta9 leaf monounsaturated fatty acids
CC       and subtle decrease of 16:3 and 18:3 polyunsaturated fatty acids,
CC       chloroplastic galactolipids monogalactosyldiacylglycerol (MGDG) and
CC       digalactosyldiacylglycerol (DGDG) being the main lipid types affected
CC       (PubMed:22028775). Abnormally large chloroplasts (PubMed:22028775). The
CC       double mutant arc6 cjd1 exhibits both phenotypes of single mutants cjd1
CC       and arc6 including altered fatty acid profiles and heterogeneous
CC       chloroplasts sizes and shapes, respectively (PubMed:22028775).
CC       {ECO:0000269|PubMed:22028775}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF99779.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC003981; AAF99779.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28325.1; -; Genomic_DNA.
DR   EMBL; AF370182; AAK43997.1; -; mRNA.
DR   EMBL; AY059140; AAL15246.1; -; mRNA.
DR   EMBL; BT000664; AAN31811.1; -; mRNA.
DR   EMBL; AY087461; AAM65006.1; -; mRNA.
DR   PIR; H86218; H86218.
DR   PIR; T00717; T00717.
DR   RefSeq; NP_563823.1; NM_100737.4.
DR   AlphaFoldDB; Q93WG3; -.
DR   SMR; Q93WG3; -.
DR   STRING; 3702.AT1G08640.1; -.
DR   PaxDb; Q93WG3; -.
DR   PRIDE; Q93WG3; -.
DR   ProteomicsDB; 187626; -.
DR   EnsemblPlants; AT1G08640.1; AT1G08640.1; AT1G08640.
DR   GeneID; 837386; -.
DR   Gramene; AT1G08640.1; AT1G08640.1; AT1G08640.
DR   KEGG; ath:AT1G08640; -.
DR   Araport; AT1G08640; -.
DR   TAIR; locus:2025660; AT1G08640.
DR   eggNOG; ENOG502QQTX; Eukaryota.
DR   HOGENOM; CLU_079739_0_0_1; -.
DR   InParanoid; Q93WG3; -.
DR   OMA; DEGRMMR; -.
DR   OrthoDB; 1455981at2759; -.
DR   PhylomeDB; Q93WG3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q93WG3; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031969; C:chloroplast membrane; IDA:TAIR.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:TAIR.
DR   InterPro; IPR021788; CPP1-like.
DR   PANTHER; PTHR33372; PTHR33372; 1.
DR   Pfam; PF11833; CPP1-like; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; Plastid; Plastid inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..294
FT                   /note="Protein CHLOROPLAST J-LIKE DOMAIN 1, chloroplastic"
FT                   /id="PRO_0000454659"
FT   TOPO_DOM        59..164
FT                   /note="Stromal"
FT                   /evidence="ECO:0000305|PubMed:22028775"
FT   TRANSMEM        165..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..233
FT                   /note="Chloroplast intermembrane"
FT                   /evidence="ECO:0000305|PubMed:22028775"
FT   TRANSMEM        234..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..275
FT                   /note="Stromal"
FT                   /evidence="ECO:0000305|PubMed:22028775"
FT   TRANSMEM        276..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294
FT                   /note="Chloroplast intermembrane"
FT                   /evidence="ECO:0000305|PubMed:22028775"
FT   REGION          74..152
FT                   /note="J-like domain"
FT                   /evidence="ECO:0000303|PubMed:22028775"
FT   CONFLICT        85
FT                   /note="E -> K (in Ref. 4; AAM65006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="M -> I (in Ref. 3; AAN31811)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  32902 MW;  23229ABC25AC10D6 CRC64;
     MAPALSTSCS SVMAFSTSNA LRYHHPQISL RNSLRAPKSP SFVRLPLGKV LQSRIVIRAA
     SSAAGNPQSD ADFNPYEVLG VNPIEGFDKI KQTYGRKLKD AQRSGDEATA ALLEKAYDKL
     MYAQLMNRKK GVTFGSFKVS KDIKYADKQP IIPWGPRFSR SSKNDMLINL AISVVFSAWI
     AIKRNVEYKP LQFMSFVFVY RIFEKLKSFE APSSPIYNEE GEESGRGLRM GKRLLRSLSL
     VFGSILLASL AYTGFLNGIE YMGYSIPMVL YNNQELIVTA SSAFMLYVIA SFYR
 
 
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