ARAS2_ARATH
ID ARAS2_ARATH Reviewed; 441 AA.
AC O23053; Q8L738;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable membrane metalloprotease ARASP2, chloroplastic {ECO:0000305};
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ARASP2 {ECO:0000305};
GN OrderedLocusNames=At1g05140 {ECO:0000312|Araport:AT1G05140};
GN ORFNames=YUP8H12.25 {ECO:0000312|EMBL:AAB71464.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 IDENTIFICATION.
RX PubMed=12185496; DOI=10.1007/s00294-002-0309-8;
RA Sokolenko A., Pojidaeva E., Zinchenko V., Panichkin V., Glaser V.M.,
RA Herrmann R.G., Shestakov S.V.;
RT "The gene complement for proteolysis in the cyanobacterium Synechocystis
RT sp. PCC 6803 and Arabidopsis thaliana chloroplasts.";
RL Curr. Genet. 41:291-310(2002).
RN [5]
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=16413549; DOI=10.1016/j.febslet.2005.12.098;
RA Bolter B., Nada A., Fulgosi H., Soll J.;
RT "A chloroplastic inner envelope membrane protease is essential for plant
RT development.";
RL FEBS Lett. 580:789-794(2006).
CC -!- FUNCTION: Metalloprotease essential for chloroplast and plant
CC development. May be involved in regulated intramembrane proteolysis
CC (RIP). {ECO:0000250|UniProtKB:O80885}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q57837};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16413549}.
CC -!- SIMILARITY: Belongs to the peptidase M50A family. {ECO:0000305}.
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DR EMBL; AC000098; AAB71464.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27794.1; -; Genomic_DNA.
DR EMBL; AY062687; AAL32765.1; -; mRNA.
DR EMBL; AY139975; AAM98118.1; -; mRNA.
DR PIR; F86185; F86185.
DR RefSeq; NP_563729.1; NM_100392.4.
DR AlphaFoldDB; O23053; -.
DR SMR; O23053; -.
DR STRING; 3702.AT1G05140.1; -.
DR MEROPS; M50.003; -.
DR iPTMnet; O23053; -.
DR PaxDb; O23053; -.
DR PRIDE; O23053; -.
DR ProteomicsDB; 244478; -.
DR EnsemblPlants; AT1G05140.1; AT1G05140.1; AT1G05140.
DR GeneID; 839307; -.
DR Gramene; AT1G05140.1; AT1G05140.1; AT1G05140.
DR KEGG; ath:AT1G05140; -.
DR Araport; AT1G05140; -.
DR TAIR; locus:2207145; AT1G05140.
DR eggNOG; ENOG502QT40; Eukaryota.
DR HOGENOM; CLU_025778_1_1_1; -.
DR InParanoid; O23053; -.
DR OMA; GPTQYNP; -.
DR OrthoDB; 1599175at2759; -.
DR PhylomeDB; O23053; -.
DR PRO; PR:O23053; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23053; baseline and differential.
DR Genevisible; O23053; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Hydrolase; Membrane; Metal-binding; Metalloprotease; Plastid;
KW Plastid inner membrane; Protease; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..84
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 85..441
FT /note="Probable membrane metalloprotease ARASP2,
FT chloroplastic"
FT /id="PRO_0000432415"
FT TRANSMEM 171..191
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT DOMAIN 196..249
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CONFLICT 190
FT /note="F -> L (in Ref. 3; AAM98118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 47775 MW; 0919B8C6D7C6ADD6 CRC64;
MLLNISSSPI SHRIPHFLSD FNNPTSNFPP KSKTHLPKSN LSTLSNHSLY GTKNRAFYKN
KRNPYNRTQA LGRFDFGSLE SVLEASAVLT AIIVVHETGH FLAASLQGIR VSKFAIGFGP
ILAKFNSNNV EYSLRAFPLG GFVGFPDNDP DSDIPVDDRN LLKNRPILDR VIVVSAGIVA
NVIFAYAIIF TQVVSVGLPV QESFPGVLVP DVKSFSAASR DGLLPGDVIL AVDGTELSNS
GSDSVSKVVD VVKRNPEHNV LLRIERGKES FEIRITPDKS FDGTGKIGVQ LSPNVRFGKV
RPKNIPETFS FAGREFFGLS YNVLDSLKQT FLNFSQTASK VAGPVAIIAV GAEVARSNAD
GLYQFAALLN LNLAVINLLP LPALDGGTLA LILLEAVRGG RKLPLEVEQG IMSSGIMLVL
FLGLFLIVKD TLNLDFIKEM L
