TTHL_ARATH
ID TTHL_ARATH Reviewed; 324 AA.
AC Q9LVM5; Q2V2X6; Q2V2X7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Uric acid degradation bifunctional protein TTL;
DE AltName: Full=Transthyretin-like protein;
DE Includes:
DE RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
DE Short=OHCU decarboxylase;
DE EC=4.1.1.97;
DE Includes:
DE RecName: Full=5-hydroxyisourate hydrolase;
DE Short=HIU hydrolase;
DE Short=HIUHase;
DE EC=3.5.2.17;
GN Name=TTL; OrderedLocusNames=At5g58220; ORFNames=MCK7.9;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH BRI1.
RX PubMed=15319482; DOI=10.1105/tpc.104.023903;
RA Nam K.H., Li J.;
RT "The Arabidopsis transthyretin-like protein is a potential substrate of
RT BRASSINOSTEROID-INSENSITIVE 1.";
RL Plant Cell 16:2406-2417(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-161 IN COMPLEX WITH
RP (S)-ALLANTOIN, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=17567580; DOI=10.1074/jbc.m703211200;
RA Kim K., Park J., Rhee S.;
RT "Structural and functional basis for (S)-allantoin formation in the ureide
RT pathway.";
RL J. Biol. Chem. 282:23457-23464(2007).
CC -!- FUNCTION: Involved in the last two steps of the degradation of uric
CC acid, i.e. the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-
CC hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) and its stereoselective
CC decarboxylation to (S)-allantoin. Might function as a negative
CC regulator to modulate brassinosteroid-mediated plant growth.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-
CC dihydro-1H-imidazole-5-carboxylate + H(+); Xref=Rhea:RHEA:23736,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18072,
CC ChEBI:CHEBI:58639; EC=3.5.2.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-
CC carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:58639; EC=4.1.1.97;
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 2/3.
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 3/3.
CC -!- SUBUNIT: Interacts with BRI1. Homodimer. {ECO:0000269|PubMed:15319482,
CC ECO:0000269|PubMed:17567580}.
CC -!- INTERACTION:
CC Q9LVM5; O22476: BRI1; NbExp=3; IntAct=EBI-1803584, EBI-1797828;
CC Q9LVM5; Q8W4D8: DDL; NbExp=4; IntAct=EBI-1803584, EBI-2015534;
CC Q9LVM5; Q9LVM5: TTL; NbExp=4; IntAct=EBI-1803584, EBI-1803584;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Peroxisome {ECO:0000269|PubMed:17951448}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LVM5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LVM5-2; Sequence=VSP_030136;
CC Name=3;
CC IsoId=Q9LVM5-3; Sequence=VSP_030135;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- INDUCTION: Not regulated by plant steroids.
CC -!- DOMAIN: The N-terminal 29 amino acids are essential, but not
CC sufficient, for the interaction with BRI1.
CC -!- PTM: Phosphorylated by BRI1 in vitro.
CC -!- SIMILARITY: In the N-terminal section; belongs to the OHCU
CC decarboxylase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transthyretin
CC family. 5-hydroxyisourate hydrolase subfamily. {ECO:0000305}.
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DR EMBL; AB019228; BAA96913.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97018.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97019.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97020.1; -; Genomic_DNA.
DR EMBL; AY062771; AAL32849.1; -; mRNA.
DR EMBL; AY081647; AAM10209.1; -; mRNA.
DR EMBL; AK226943; BAE99013.1; -; mRNA.
DR RefSeq; NP_001032093.1; NM_001037016.2. [Q9LVM5-3]
DR RefSeq; NP_001032094.1; NM_001037017.3. [Q9LVM5-2]
DR RefSeq; NP_200630.1; NM_125207.5. [Q9LVM5-1]
DR PDB; 2Q37; X-ray; 2.50 A; A=1-161.
DR PDBsum; 2Q37; -.
DR AlphaFoldDB; Q9LVM5; -.
DR SMR; Q9LVM5; -.
DR BioGRID; 21178; 6.
DR IntAct; Q9LVM5; 3.
DR STRING; 3702.AT5G58220.1; -.
DR TCDB; 9.B.35.1.3; the putative thyronine-transporting transthyretin (transthyretin) family.
DR iPTMnet; Q9LVM5; -.
DR PaxDb; Q9LVM5; -.
DR PRIDE; Q9LVM5; -.
DR ProteomicsDB; 234627; -. [Q9LVM5-1]
DR DNASU; 835934; -.
DR EnsemblPlants; AT5G58220.1; AT5G58220.1; AT5G58220. [Q9LVM5-1]
DR EnsemblPlants; AT5G58220.2; AT5G58220.2; AT5G58220. [Q9LVM5-3]
DR EnsemblPlants; AT5G58220.3; AT5G58220.3; AT5G58220. [Q9LVM5-2]
DR GeneID; 835934; -.
DR Gramene; AT5G58220.1; AT5G58220.1; AT5G58220. [Q9LVM5-1]
DR Gramene; AT5G58220.2; AT5G58220.2; AT5G58220. [Q9LVM5-3]
DR Gramene; AT5G58220.3; AT5G58220.3; AT5G58220. [Q9LVM5-2]
DR KEGG; ath:AT5G58220; -.
DR Araport; AT5G58220; -.
DR TAIR; locus:2161208; AT5G58220.
DR eggNOG; KOG3006; Eukaryota.
DR HOGENOM; CLU_050809_0_0_1; -.
DR InParanoid; Q9LVM5; -.
DR OMA; EPEGHYH; -.
DR OrthoDB; 1216648at2759; -.
DR PhylomeDB; Q9LVM5; -.
DR BioCyc; ARA:AT5G58220-MON; -.
DR BioCyc; MetaCyc:AT5G58220-MON; -.
DR BRENDA; 4.1.1.97; 399.
DR UniPathway; UPA00394; UER00651.
DR UniPathway; UPA00394; UER00652.
DR EvolutionaryTrace; Q9LVM5; -.
DR PRO; PR:Q9LVM5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVM5; baseline and differential.
DR Genevisible; Q9LVM5; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IDA:TAIR.
DR GO; GO:0033971; F:hydroxyisourate hydrolase activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019428; P:allantoin biosynthetic process; IDA:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; IMP:TAIR.
DR GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05822; TLP_HIUase; 1.
DR Gene3D; 1.10.3330.10; -; 1.
DR Gene3D; 2.60.40.180; -; 1.
DR InterPro; IPR017129; HIU_hydrol/OHCU_decarb.
DR InterPro; IPR014306; Hydroxyisourate_hydrolase.
DR InterPro; IPR018020; OHCU_decarboxylase.
DR InterPro; IPR036778; OHCU_decarboxylase_sf.
DR InterPro; IPR023418; Thyroxine_BS.
DR InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR InterPro; IPR023419; Transthyretin_CS.
DR PANTHER; PTHR10395; PTHR10395; 1.
DR Pfam; PF09349; OHCU_decarbox; 1.
DR Pfam; PF00576; Transthyretin; 1.
DR PIRSF; PIRSF037178; UCP037178_transthyretin; 1.
DR PRINTS; PR00189; TRNSTHYRETIN.
DR SUPFAM; SSF158694; SSF158694; 1.
DR SUPFAM; SSF49472; SSF49472; 1.
DR TIGRFAMs; TIGR02962; hdxy_isourate; 1.
DR PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Decarboxylase; Hydrolase; Lyase; Membrane; Multifunctional enzyme;
KW Peroxisome; Phosphoprotein; Purine metabolism; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..324
FT /note="Uric acid degradation bifunctional protein TTL"
FT /id="PRO_0000050606"
FT REGION 2..161
FT /note="OHCU decarboxylase"
FT REGION 178..324
FT /note="HIU hydrolase"
FT ACT_SITE 58
FT /note="Proton donor; for OHCU decarboxylase activity"
FT BINDING 58..59
FT /ligand="substrate"
FT BINDING 80
FT /ligand="substrate"
FT BINDING 111..115
FT /ligand="substrate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 181..218
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_030135"
FT VAR_SEQ 181..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_030136"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2Q37"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2Q37"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:2Q37"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:2Q37"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:2Q37"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2Q37"
FT HELIX 90..107
FT /evidence="ECO:0007829|PDB:2Q37"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:2Q37"
FT HELIX 135..158
FT /evidence="ECO:0007829|PDB:2Q37"
SQ SEQUENCE 324 AA; 35564 MW; 99191F450BDE262F CRC64;
MAMEIGEDEW KVCCGSSEFA KQMSTSGPLT SQEAIYTARD IWFNQVNVTD WLEAFSAHPQ
IGNTPSPSIN SDFARRSVSE QSTAFATTSA SALQELAEWN VLYKKKFGFI FIICASGRTH
AEMLHALKER YENRPIVELE IAAMEQMKIT ELRMAKLFSD KAKVISETDS SSSPVSTKPQ
DRLRIIGGHL NVAAEAKAPK RSRPPITTHV LDVSRGAPAA GVEVHLEVWS GTTGPSFVHG
GGGVWSSVGT SATDRDGRSG PLMDLVDALN PGTYRISFDT AKYSPGCFFP YVSIVFQVTE
SQKWEHFHVP LLLAPFSFST YRGS
