ARASP_ARATH
ID ARASP_ARATH Reviewed; 447 AA.
AC O80885;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Membrane metalloprotease ARASP, chloroplastic {ECO:0000303|PubMed:16413549};
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ARASP {ECO:0000303|PubMed:16413549};
GN OrderedLocusNames=At2g32480 {ECO:0000312|Araport:AT2G32480};
GN ORFNames=T26B15.4 {ECO:0000312|EMBL:AAC25930.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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.
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 [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP 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:0000269|PubMed:16413549}.
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:0000269|PubMed:16413549}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=O80885-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in green seedlings and cotyledons. Low
CC levels of expression in roots, siliques and seeds.
CC {ECO:0000269|PubMed:16413549}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:16413549}.
CC -!- SIMILARITY: Belongs to the peptidase M50A family. {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; AC004681; AAC25930.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08691.1; -; Genomic_DNA.
DR EMBL; AF386983; AAK62428.1; -; mRNA.
DR EMBL; BT006594; AAP31938.1; -; mRNA.
DR EMBL; AY085846; AAM63060.1; -; mRNA.
DR PIR; T02547; T02547.
DR RefSeq; NP_565745.1; NM_128807.1. [O80885-1]
DR AlphaFoldDB; O80885; -.
DR SMR; O80885; -.
DR STRING; 3702.AT2G32480.1; -.
DR MEROPS; M50.A10; -.
DR iPTMnet; O80885; -.
DR PaxDb; O80885; -.
DR PRIDE; O80885; -.
DR ProteomicsDB; 240604; -. [O80885-1]
DR EnsemblPlants; AT2G32480.1; AT2G32480.1; AT2G32480. [O80885-1]
DR GeneID; 817809; -.
DR Gramene; AT2G32480.1; AT2G32480.1; AT2G32480. [O80885-1]
DR KEGG; ath:AT2G32480; -.
DR Araport; AT2G32480; -.
DR TAIR; locus:2060295; AT2G32480.
DR eggNOG; ENOG502QT40; Eukaryota.
DR InParanoid; O80885; -.
DR OMA; FAKIFKV; -.
DR PhylomeDB; O80885; -.
DR PRO; PR:O80885; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80885; baseline and differential.
DR Genevisible; O80885; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
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; TAS:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF13180; PDZ_2; 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 Alternative splicing; Chloroplast; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Plastid; Plastid inner membrane; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..73
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 74..447
FT /note="Membrane metalloprotease ARASP, chloroplastic"
FT /id="PRO_0000432414"
FT TRANSMEM 177..197
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT DOMAIN 202..244
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 447 AA; 48726 MW; 152A261C32920664 CRC64;
MLLNISSSPI SHRNPHFLSN FNNPISYFPR RSKTHLSKSH FFPKFTPLSN QSLKNRVLFG
NKRYPDGERF DFRSRAISGI DLGSFESVLE AIAVLTTIIV VHESGHFLAA SLQGIHVSKF
AIGFGPILAK FDYNNVEYSL RAFPLGGFVG FPDNDPDSEI PIDDENLLKN RPTLDRSIVV
SAGIIANVIF AYAIIFVQVL SVGLPVQEAF PGVLVPEVKT FSAASRDGLL SGDVILAVDG
TELSKTGPDA VSKIVDIVKR NPKSNVVFRI ERGGEDFDIR VTPDKNFDGT GKIGVQLSPN
VRITKVRPRN IPETFRFVGR EFMGLSSNVL DGLKQTFFNF SQTASKVAGP VAIIAVGAEV
ARSNIDGLYQ FAALLNINLA VINLLPLPAL DGGTLALILL EAVRGGKKLP VEVEQGIMSS
GIMLVIFLGL FLIVKDTLSL DFIKEML
