EGY1_ARATH
ID EGY1_ARATH Reviewed; 548 AA.
AC Q949Y5; Q9LHR6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable zinc metalloprotease EGY1, chloroplastic;
DE EC=3.4.24.-;
DE AltName: Full=Protein AMMONIUM OVERLY SENSITIVE 1;
DE AltName: Full=Protein ETHYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN 1;
DE Short=AtEGY1;
DE Flags: Precursor;
GN Name=EGY1; Synonyms=AMOS1; OrderedLocusNames=At5g35220;
GN ORFNames=T25C13.100;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND DISRUPTION
RP PHENOTYPE.
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18097640; DOI=10.1007/s11103-007-9273-5;
RA Guo D., Gao X., Li H., Zhang T., Chen G., Huang P., An L., Li N.;
RT "EGY1 plays a role in regulation of endodermal plastid size and number that
RT are involved in ethylene-dependent gravitropism of light-grown Arabidopsis
RT hypocotyls.";
RL Plant Mol. Biol. 66:345-360(2008).
RN [6]
RP FUNCTION.
RX PubMed=23064408; DOI=10.1104/pp.112.206508;
RA Li B., Li Q., Xiong L., Kronzucker H.J., Kramer U., Shi W.;
RT "Arabidopsis plastid AMOS1/EGY1 integrates abscisic acid signaling to
RT regulate global gene expression response to ammonium stress.";
RL Plant Physiol. 160:2040-2051(2012).
CC -!- FUNCTION: Membrane-associated and ATP-independent metalloprotease
CC required for development of both thylakoid grana and well-organized
CC lamellae in chloroplast. Required for the accumulation of chlorophyll
CC and chlorophyll a/b binding (CAB) proteins (from both PS I and PS II)
CC in chloroplast membranes, and for grana formation and normal
CC chloroplast development. Involved in the regulation of nuclear gene
CC expression in response to ammonium stress and interacts with ABA
CC signaling. Carries out beta-casein degradation in an ATP-independent
CC manner in vitro. {ECO:0000269|PubMed:15659096,
CC ECO:0000269|PubMed:18097640, ECO:0000269|PubMed:23064408}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Note=Localizes in endodermal
CC and cortex plastids.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, cotyledons, hypocotyls,
CC stems, flowers and siliques. {ECO:0000269|PubMed:15659096}.
CC -!- INDUCTION: By ethylene. Down-regulated by dark.
CC {ECO:0000269|PubMed:15659096}.
CC -!- DISRUPTION PHENOTYPE: Reduced chlorophyll accumulation, defects in
CC chloroplast development and abnormal hypocotyl gravicurvature.
CC {ECO:0000269|PubMed:15659096, ECO:0000269|PubMed:18097640}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98209.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002031; BAA98209.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93947.1; -; Genomic_DNA.
DR EMBL; AY050809; AAK92744.1; -; mRNA.
DR EMBL; BT001978; AAN71977.1; -; mRNA.
DR RefSeq; NP_198372.1; NM_122913.4.
DR AlphaFoldDB; Q949Y5; -.
DR STRING; 3702.AT5G35220.1; -.
DR MEROPS; M50.A02; -.
DR iPTMnet; Q949Y5; -.
DR PaxDb; Q949Y5; -.
DR PRIDE; Q949Y5; -.
DR ProteomicsDB; 220754; -.
DR EnsemblPlants; AT5G35220.1; AT5G35220.1; AT5G35220.
DR GeneID; 833476; -.
DR Gramene; AT5G35220.1; AT5G35220.1; AT5G35220.
DR KEGG; ath:AT5G35220; -.
DR Araport; AT5G35220; -.
DR TAIR; locus:2182372; AT5G35220.
DR eggNOG; ENOG502QUAP; Eukaryota.
DR HOGENOM; CLU_028221_1_1_1; -.
DR InParanoid; Q949Y5; -.
DR OMA; NKYNLFM; -.
DR OrthoDB; 1393607at2759; -.
DR PhylomeDB; Q949Y5; -.
DR PRO; PR:Q949Y5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q949Y5; baseline and differential.
DR Genevisible; Q949Y5; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
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:0004222; F:metalloendopeptidase activity; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0009959; P:negative gravitropism; IMP:TAIR.
DR GO; GO:0048564; P:photosystem I assembly; IMP:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0060359; P:response to ammonium ion; IMP:TAIR.
DR GO; GO:0043157; P:response to cation stress; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR InterPro; IPR044838; EGY1-like.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR31412; PTHR31412; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Developmental protein; Hydrolase; Membrane; Metalloprotease;
KW Plastid; Protease; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..18
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 19..548
FT /note="Probable zinc metalloprotease EGY1, chloroplastic"
FT /id="PRO_0000428645"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 61..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 59501 MW; D8120CC9B3EFF287 CRC64;
MGTLTSVAFA AAVNIRFRSF HRENIKTTIT TLPKWQKRLC FSSTEDSHRF RIAKCLGNDE
NSNRDDSIGE NGETHKSSVV KTATFEEEDE ETSKSSSTTS SSNEFGSDKT SMPSTIDPTY
SSFQIDSFKL MELLGPEKVD PADVKLIKDK LFGYSTFWVT KEEPFGDLGE GILFLGNLRG
KKEDVFAKLQ RKLVEVASDK YNLFMIEEPN SEGPDPRGGA RVSFGLLRKE VSEPGPTTLW
QYVIALILFL LTIGSSVELG IASQINRLPP EVVKYFTDPN AVEPPDMELL YPFVDAALPL
AYGVLGILLF HELGHFLAAV PKKVKLSIPY FIPNITLGSF GAITQFKSIL PDRSTKVDIS
LAGPFAGAAL SVSMFAVGLF LSTEPDAAND LVQVPSMLFQ GSLLLGLISR ATLGYAALHA
ATVSIHPLVI AGWCGLTTTA FNMLPVGCLD GGRAVQGAFG KNALVTFGLS TYVMLGLRVL
GGPLALPWGL YVLICQRTPE KPCLNDVTEV GTWRKALVGI ALILVVLTLL PVWDELAEEV
GIGLVTTF
