MPRO1_ARATH
ID MPRO1_ARATH Reviewed; 710 AA.
AC F4HTQ1; Q9FXD5;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable thimet oligopeptidase;
DE EC=3.4.24.15;
DE AltName: Full=Zincin-like metalloproteases-like protein 1;
GN OrderedLocusNames=At1g67690; ORFNames=F12A21.16;
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).
CC -!- FUNCTION: Involved in cytoplasmic peptide degradation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues at
CC P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15
CC residues.; EC=3.4.24.15;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG28905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008113; AAG28905.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34682.1; -; Genomic_DNA.
DR RefSeq; NP_564902.4; NM_105437.5.
DR AlphaFoldDB; F4HTQ1; -.
DR SMR; F4HTQ1; -.
DR STRING; 3702.AT1G67690.1; -.
DR MEROPS; M03.A03; -.
DR iPTMnet; F4HTQ1; -.
DR PaxDb; F4HTQ1; -.
DR PRIDE; F4HTQ1; -.
DR ProteomicsDB; 239073; -.
DR EnsemblPlants; AT1G67690.1; AT1G67690.1; AT1G67690.
DR GeneID; 843094; -.
DR Gramene; AT1G67690.1; AT1G67690.1; AT1G67690.
DR KEGG; ath:AT1G67690; -.
DR Araport; AT1G67690; -.
DR TAIR; locus:2008600; AT1G67690.
DR eggNOG; KOG2089; Eukaryota.
DR HOGENOM; CLU_001805_2_1_1; -.
DR InParanoid; F4HTQ1; -.
DR OMA; WSSVIAK; -.
DR OrthoDB; 642479at2759; -.
DR PRO; PR:F4HTQ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HTQ1; baseline and differential.
DR Genevisible; F4HTQ1; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 1.20.1050.40; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..710
FT /note="Probable thimet oligopeptidase"
FT /id="PRO_0000425140"
FT ACT_SITE 503
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 710 AA; 80291 MW; 2C718ADA8F2CF64B CRC64;
MTENEGNDKK IEGSNPKKKL NVVTFTGAAG LLGLAVSFAI FTFKSHKQKS KKKGLPGCDT
VCVNLSAKEI LDLAEEIIHK STRVHDAVAL VSLDKLSYEN VVLPLAELEA RQLSLIQCCV
FPKMLSPHDN VRKASTEAEQ KIDAHILSCR KREDVYRIIK IYAAKGESIS PEAKCYLQCL
VRDFEDNGLN LTAIKREEVE RLKYEIDELS LRYIQNLNED SSCLFFTEDE LAGLPLEFLQ
NLEKTQNKEF KLTLESRHVA AILELCKIAK TRKTVAMAYG KRCGDTNIPV LQRLVQSRHR
LACVCGYAHF ADYALDRRMS KTSMRVIRFL EDISSSLTDL AIREFSILED LKRKEEGEIP
FGVEDLLYYI KRVEELQFDL DFGDIRQYFP VNLVLSGIFK ICQDLFGIKF EEVTEVDVWY
HDIRAFAVFD SGSGKLLGYF YLDMFTREGK CNHSCVVALQ NNALFSNGAC QIPVALLIAQ
FAKDGSGEAV PLGFSDVVNL FHEFGHVVQH ICNRASFARF SGLRVDPDFR EIPSQLLENW
CYESFTLKLI SGYRQDITKP LVDEVCKTLK RWRYSFSALK SLQEILYCLF DQIIYSDDDA
DLLQLIRSLH PKVMIGLPVV EGTNPASCFP RAVIGSEATC YSRLWSEVYA ADIFASKFGD
GHPNLYAGLQ FRDKVLAPGG GKEPMELLTN FLGREPSTQA FIASRTNYSL
