TTM2_ARATH
ID TTM2_ARATH Reviewed; 674 AA.
AC Q9C664;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Inorganic pyrophosphatase TTM2 {ECO:0000305};
DE EC=3.6.1.1 {ECO:0000269|PubMed:28733390};
DE AltName: Full=Triphosphate tunnel metalloenzyme 2 {ECO:0000303|PubMed:25185123};
DE Short=AtTTM2 {ECO:0000303|PubMed:25185123};
GN Name=TTM2 {ECO:0000303|PubMed:25185123};
GN OrderedLocusNames=At1g26190 {ECO:0000312|Araport:AT1G26190};
GN ORFNames=F28B23.13 {ECO:0000312|EMBL:AAG50674.1};
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;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, REPRESSION BY HYALOPERONOSPORA
RP ARABIDOPSIDIS; SALICYLIC ACID; BENZOTHIADIAZOLE AND PATHOGEN-ASSOCIATED
RP MOLECULAR PATTERNS, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=25185123; DOI=10.1104/pp.114.248757;
RA Ung H., Moeder W., Yoshioka K.;
RT "Arabidopsis triphosphate tunnel metalloenzyme2 is a negative regulator of
RT the salicylic acid-mediated feedback amplification loop for defense
RT responses.";
RL Plant Physiol. 166:1009-1021(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=28733390; DOI=10.1104/pp.17.00700;
RA Ung H., Karia P., Ebine K., Ueda T., Yoshioka K., Moeder W.;
RT "Triphosphate tunnel metalloenzyme function in senescence highlights a
RT biological diversification of this protein superfamily.";
RL Plant Physiol. 175:473-485(2017).
CC -!- FUNCTION: Exhibits pyrophosphatase activity with stronger affinity for
CC pyrophosphate (PPi), moderate affinity for ATP and ADP, and weak
CC affinity for tripolyphosphate (PPPi) (PubMed:25185123,
CC PubMed:28733390). No activity observed toward uridine substrate
CC (PubMed:28733390). Negative regulator of the salicylic acid (SA)-
CC mediated amplification of defense responses against both virulent and
CC avirulent pathogens, including oomycetes (e.g. H.arabidopsidis) and
CC bacteria (e.g. P.syringae). Represses systemic acquired resistance
CC (SAR) (PubMed:25185123). {ECO:0000269|PubMed:25185123,
CC ECO:0000269|PubMed:28733390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC Evidence={ECO:0000269|PubMed:28733390};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28733390};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for pyrophosphate {ECO:0000269|PubMed:28733390};
CC Vmax=366 nmol/min/ug enzyme with pyrophosphate as substrate
CC {ECO:0000269|PubMed:28733390};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:28733390};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:28733390}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the shoot apices of
CC inflorescences. {ECO:0000269|PubMed:28733390}.
CC -!- INDUCTION: Repressed by the oomycete pathogen H.arabidopsidis.
CC Negatively regulated by salicylic acid (SA), benzothiadiazole (BTH) and
CC pathogen-associated molecular patterns (PAMP, e.g. flg22).
CC {ECO:0000269|PubMed:25185123}.
CC -!- DISRUPTION PHENOTYPE: Enhanced hypersensitive response, elevated
CC pathogen resistance against both virulent and avirulent pathogens (e.g.
CC isolates Emwa1 and Emco5 of the oomycete pathogen H.arabidopsidis, the
CC bacterial pathogen P.syringae DC3000 (AvrRps4)). Elevated accumulation
CC of salicylic acid (SA) and conjugates (e.g. salicylic acid glucoside
CC (SAG)) upon infection. Stronger systemic acquired resistance (SAR).
CC These increased defense responses are PAD4-, ICS1- and NPR1-dependent.
CC {ECO:0000269|PubMed:25185123}.
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DR EMBL; AC079829; AAG50674.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30659.1; -; Genomic_DNA.
DR EMBL; AY091017; AAM14039.1; -; mRNA.
DR EMBL; AY117297; AAM51372.1; -; mRNA.
DR PIR; B86388; B86388.
DR RefSeq; NP_173944.1; NM_102384.4.
DR AlphaFoldDB; Q9C664; -.
DR SMR; Q9C664; -.
DR STRING; 3702.AT1G26190.1; -.
DR iPTMnet; Q9C664; -.
DR PaxDb; Q9C664; -.
DR PRIDE; Q9C664; -.
DR DNASU; 839160; -.
DR EnsemblPlants; AT1G26190.1; AT1G26190.1; AT1G26190.
DR GeneID; 839160; -.
DR Gramene; AT1G26190.1; AT1G26190.1; AT1G26190.
DR KEGG; ath:AT1G26190; -.
DR Araport; AT1G26190; -.
DR TAIR; locus:2028809; AT1G26190.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_028566_0_0_1; -.
DR InParanoid; Q9C664; -.
DR OrthoDB; 295827at2759; -.
DR PhylomeDB; Q9C664; -.
DR BioCyc; ARA:AT1G26190-MON; -.
DR PRO; PR:Q9C664; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C664; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016462; F:pyrophosphatase activity; IDA:TAIR.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1902289; P:negative regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0010113; P:negative regulation of systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0002239; P:response to oomycetes; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR Pfam; PF01928; CYTH; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Hypersensitive response; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Plant defense; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..674
FT /note="Inorganic pyrophosphatase TTM2"
FT /id="PRO_0000444984"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 248..410
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT REGION 457..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 76007 MW; 8B60E446FF9F16AF CRC64;
MGQDSNGIEF HQKRHGLLKD QVQLVKRRDS IRYEIVSIQD RLSFEKGFFA VIRACQLLSQ
KNDGIILVGV AGPSGAGKTV FTEKILNFLP SVAVISMDNY NDSSRIVDGN FDDPRLTDYD
TLLKNLEDLK EGKQVEVPIY DFKSSSRVGY RTLDVPPSRI VIIEGIYALS EKLRPLLDLR
VSVTGGVHFD LVKRVLRDIQ RAGQQPEEII HQISETVYPM YKAFIEPDLQ TAQIKIINKF
NPFTGFQSPT YILKSRKEVS VDQIKAVLSD GHTETKEETY DIYLLPPGED PESCQSYLRM
RNKDGKYSLM FEEWVTDTPF VISPRITFEV SVRLLGGLMA LGYTIATILK RNSHVFATDK
VFVKIDWLEQ LNRHYMQVQG KDRQLVQSTA EQLGLEGSFI PRTYIEQIQL EKLINEVMAL
PDDLKNKLSL DEDLVSSSSP KEALLRASAD RVAMRNKNLK RGMSHSYSTQ RDKNLSKLAG
YSSSDRRYEE RNHDSPANEG FMTLLSEQIS SLNERMDEFT SRIEELNSKL SCNKNSPTQQ
SLSIQTEVCN GSAPTSYFIS GLDNGCLTNS IMPHSSSSSQ LAKDSPLMEE ISTISRGQRQ
VMHQLDNLCN LMRESSAERS RLARTGSSNS GNRGRSSKSS FLSNVESNKL PLVLTVAICS
IGIIVIKSYI NKRQ
