EGY3_ARATH
ID EGY3_ARATH Reviewed; 573 AA.
AC Q9LMU1; Q0WWS5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable zinc metallopeptidase EGY3, chloroplastic;
DE EC=3.4.24.-;
DE AltName: Full=Protein ETHYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN 3;
DE Short=AtEGY3;
DE Flags: Precursor;
GN Name=EGY3; OrderedLocusNames=At1g17870; ORFNames=F2H15.10;
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;
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 [4]
RP GENE FAMILY.
RX PubMed=15659096; DOI=10.1111/j.1365-313x.2004.02308.x;
RA Chen G., Bi Y.R., Li N.;
RT "EGY1 encodes a membrane-associated and ATP-independent metalloprotease
RT that is required for chloroplast development.";
RL Plant J. 41:364-375(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- FUNCTION: Probable membrane-associated metalloprotease that may be
CC involved in chloroplast development. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AC034106; AAF97267.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29646.1; -; Genomic_DNA.
DR EMBL; AK226263; BAE98423.1; -; mRNA.
DR PIR; H86313; H86313.
DR RefSeq; NP_173229.1; NM_101650.3.
DR AlphaFoldDB; Q9LMU1; -.
DR STRING; 3702.AT1G17870.1; -.
DR PaxDb; Q9LMU1; -.
DR PRIDE; Q9LMU1; -.
DR ProteomicsDB; 220757; -.
DR EnsemblPlants; AT1G17870.1; AT1G17870.1; AT1G17870.
DR GeneID; 838366; -.
DR Gramene; AT1G17870.1; AT1G17870.1; AT1G17870.
DR KEGG; ath:AT1G17870; -.
DR Araport; AT1G17870; -.
DR TAIR; locus:2030938; AT1G17870.
DR eggNOG; ENOG502QQ7R; Eukaryota.
DR HOGENOM; CLU_032693_0_0_1; -.
DR InParanoid; Q9LMU1; -.
DR OMA; DRYAWGF; -.
DR OrthoDB; 1393607at2759; -.
DR PhylomeDB; Q9LMU1; -.
DR PRO; PR:Q9LMU1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMU1; baseline and differential.
DR Genevisible; Q9LMU1; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR InterPro; IPR044838; EGY1-like.
DR PANTHER; PTHR31412; PTHR31412; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Hydrolase; Membrane; Metalloprotease; Plastid;
KW Protease; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..573
FT /note="Probable zinc metallopeptidase EGY3, chloroplastic"
FT /id="PRO_0000428650"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 38..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..185
FT /evidence="ECO:0000255"
FT COMPBIAS 48..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 405
FT /note="I -> M (in Ref. 3; BAE98423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 62718 MW; C36FEFEE138B051C CRC64;
MASLFVSTPS SSLTLKSCHS LHLRRFDRAE FSNFGKASVN QTTRSRHSLR CSAEDDRVRE
PVNEAPSPVA LAEEQKEDHD NNNAPPSPES SEEEEEKKSK QQEMDWKTDE EFKKFMGNPS
IEAAIKLEKT RTDRKLKELN KESNSENPII GIYNSLARDS LTKEKERLEK AEETFKALDL
NKLKSCFGFD TFFATDVRRF GDGGIFIGNL RKPIDEVTPK LEAKLSEAAG RDVVVWFMEE
RSNEITKQVC MVQPKAEIDL QFESTRLSTP WGYVSAIALC VTTFGTIALM SGFFLKPDAT
FDDYIANVVP LFGGFLSILG VSEIATRVTA ARHGVKLSPS FLVPSNWTGC LGVMNNYESL
LPNKKALFDI PVARTASAYL TSLLLAAAAF ISDGSFNGGD NALYIRPQFF DNNPLLSFVQ
FVVGPYADDL GNVLPNAVEG VGVPVDPLAF AGLLGMVVTS LNLLPCGRLE GGRIAQAMFG
RSTAAILSFT TSLLLGIGGL SGSVLCLAWG LFATFFRGGE ETPAKDEITP VGDDRFAWGI
VLGLICFLTL FPNSGGTFST SFFNGPFFRG DDF
