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Uric acid degradation bifunctional protein TTL (Transthyretin-like protein) [Includes: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97); 5-hydroxyisourate hydrolase (HIU hydrolase) (HIUHase) (EC 3.5.2.17)]

 TTHL_ARATH              Reviewed;         324 AA.
Q9LVM5; Q2V2X6; Q2V2X7;
21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 131.
RecName: Full=Uric acid degradation bifunctional protein TTL;
AltName: Full=Transthyretin-like protein;
Includes:
RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
Short=OHCU decarboxylase;
EC=4.1.1.97;
Includes:
RecName: Full=5-hydroxyisourate hydrolase;
Short=HIU hydrolase;
Short=HIUHase;
EC=3.5.2.17;
Name=TTL; OrderedLocusNames=At5g58220; ORFNames=MCK7.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH BRI1.
PubMed=15319482; DOI=10.1105/tpc.104.023903;
Nam K.H., Li J.;
"The Arabidopsis transthyretin-like protein is a potential substrate
of BRASSINOSTEROID-INSENSITIVE 1.";
Plant Cell 16:2406-2417(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-161 IN COMPLEX WITH
(S)-ALLANTOIN, SUBUNIT, AND REACTION MECHANISM.
PubMed=17567580; DOI=10.1074/jbc.M703211200;
Kim K., Park J., Rhee S.;
"Structural and functional basis for (S)-allantoin formation in the
ureide pathway.";
J. Biol. Chem. 282:23457-23464(2007).
-!- FUNCTION: Involved in the last two steps of the degradation of
uric acid, i.e. the hydrolysis of 5-hydroxyisourate (HIU) to 2-
oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) and its
stereoselective decarboxylation to (S)-allantoin. Might function
as a negative regulator to modulate brassinosteroid-mediated plant
growth.
-!- CATALYTIC ACTIVITY: 5-hydroxyisourate + H(2)O = 5-hydroxy-2-oxo-4-
ureido-2,5-dihydro-1H-imidazole-5-carboxylate.
-!- CATALYTIC ACTIVITY: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-
imidazole-5-carboxylate = (S)-allantoin + CO(2).
-!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
urate: step 2/3.
-!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
urate: step 3/3.
-!- SUBUNIT: Interacts with BRI1. Homodimer.
{ECO:0000269|PubMed:15319482, ECO:0000269|PubMed:17567580}.
-!- INTERACTION:
O22476:BRI1; NbExp=3; IntAct=EBI-1803584, EBI-1797828;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
Peroxisome {ECO:0000269|PubMed:17951448}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9LVM5-1; Sequence=Displayed;
Name=2;
IsoId=Q9LVM5-2; Sequence=VSP_030136;
Name=3;
IsoId=Q9LVM5-3; Sequence=VSP_030135;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
-!- INDUCTION: Not regulated by plant steroids.
-!- DOMAIN: The N-terminal 29 amino acids are essential, but not
sufficient, for the interaction with BRI1.
-!- PTM: Phosphorylated by BRI1 in vitro.
-!- SIMILARITY: In the N-terminal section; belongs to the OHCU
decarboxylase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transthyretin family. 5-hydroxyisourate hydrolase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB019228; BAA96913.1; -; Genomic_DNA.
EMBL; CP002688; AED97018.1; -; Genomic_DNA.
EMBL; CP002688; AED97019.1; -; Genomic_DNA.
EMBL; CP002688; AED97020.1; -; Genomic_DNA.
EMBL; AY062771; AAL32849.1; -; mRNA.
EMBL; AY081647; AAM10209.1; -; mRNA.
EMBL; AK226943; BAE99013.1; -; mRNA.
RefSeq; NP_001032093.1; NM_001037016.2. [Q9LVM5-3]
RefSeq; NP_001032094.1; NM_001037017.3. [Q9LVM5-2]
RefSeq; NP_200630.1; NM_125207.5. [Q9LVM5-1]
UniGene; At.27237; -.
PDB; 2Q37; X-ray; 2.50 A; A=1-161.
PDBsum; 2Q37; -.
ProteinModelPortal; Q9LVM5; -.
SMR; Q9LVM5; -.
BioGrid; 21178; 4.
IntAct; Q9LVM5; 1.
STRING; 3702.AT5G58220.1; -.
TCDB; 9.B.35.1.3; the putative thyronine-transporting transthyretin (transthyretin) family.
iPTMnet; Q9LVM5; -.
PaxDb; Q9LVM5; -.
DNASU; 835934; -.
EnsemblPlants; AT5G58220.1; AT5G58220.1; AT5G58220. [Q9LVM5-1]
EnsemblPlants; AT5G58220.2; AT5G58220.2; AT5G58220. [Q9LVM5-3]
EnsemblPlants; AT5G58220.3; AT5G58220.3; AT5G58220. [Q9LVM5-2]
GeneID; 835934; -.
Gramene; AT5G58220.1; AT5G58220.1; AT5G58220.
Gramene; AT5G58220.2; AT5G58220.2; AT5G58220.
Gramene; AT5G58220.3; AT5G58220.3; AT5G58220.
KEGG; ath:AT5G58220; -.
Araport; AT5G58220; -.
TAIR; locus:2161208; AT5G58220.
eggNOG; KOG3006; Eukaryota.
eggNOG; COG2351; LUCA.
HOGENOM; HOG000012804; -.
InParanoid; Q9LVM5; -.
KO; K13484; -.
OMA; LACCGST; -.
OrthoDB; EOG09360I5A; -.
PhylomeDB; Q9LVM5; -.
BioCyc; ARA:AT5G58220-MONOMER; -.
BioCyc; MetaCyc:AT5G58220-MONOMER; -.
BRENDA; 4.1.1.97; 399.
UniPathway; UPA00394; UER00651.
UniPathway; UPA00394; UER00652.
EvolutionaryTrace; Q9LVM5; -.
PRO; PR:Q9LVM5; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9LVM5; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IDA:TAIR.
GO; GO:0033971; F:hydroxyisourate hydrolase activity; IDA:TAIR.
GO; GO:0019428; P:allantoin biosynthetic process; IDA:TAIR.
GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
GO; GO:0051289; P:protein homotetramerization; IDA:TAIR.
GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; IMP:TAIR.
GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.3330.10; -; 1.
Gene3D; 2.60.40.180; -; 1.
InterPro; IPR017129; HIU_hydrol/OHCU_decarb.
InterPro; IPR014306; Hydroxyisourate_hydrolase.
InterPro; IPR018020; OHCU_decarboxylase.
InterPro; IPR036778; OHCU_decarboxylase_sf.
InterPro; IPR023418; Thyroxine_BS.
InterPro; IPR000895; Transthyretin/HIU_hydrolase.
InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
InterPro; IPR023419; Transthyretin_CS.
PANTHER; PTHR10395; PTHR10395; 1.
Pfam; PF09349; OHCU_decarbox; 1.
Pfam; PF00576; Transthyretin; 1.
PIRSF; PIRSF037178; UCP037178_transthyretin; 1.
PRINTS; PR00189; TRNSTHYRETIN.
SUPFAM; SSF158694; SSF158694; 1.
SUPFAM; SSF49472; SSF49472; 1.
TIGRFAMs; TIGR02962; hdxy_isourate; 1.
PROSITE; PS00768; TRANSTHYRETIN_1; 1.
PROSITE; PS00769; TRANSTHYRETIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Complete proteome; Decarboxylase; Hydrolase; Lyase; Membrane;
Multifunctional enzyme; Peroxisome; Phosphoprotein; Purine metabolism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 324 Uric acid degradation bifunctional
protein TTL.
/FTId=PRO_0000050606.
REGION 2 161 OHCU decarboxylase.
REGION 58 59 Substrate binding.
REGION 111 115 Substrate binding.
REGION 178 324 HIU hydrolase.
ACT_SITE 58 58 Proton donor; for OHCU decarboxylase
activity.
BINDING 80 80 Substrate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
VAR_SEQ 181 218 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_030135.
VAR_SEQ 181 193 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_030136.
HELIX 9 11 {ECO:0000244|PDB:2Q37}.
STRAND 13 15 {ECO:0000244|PDB:2Q37}.
HELIX 17 24 {ECO:0000244|PDB:2Q37}.
HELIX 31 44 {ECO:0000244|PDB:2Q37}.
HELIX 48 56 {ECO:0000244|PDB:2Q37}.
HELIX 82 85 {ECO:0000244|PDB:2Q37}.
HELIX 90 107 {ECO:0000244|PDB:2Q37}.
HELIX 120 130 {ECO:0000244|PDB:2Q37}.
HELIX 135 158 {ECO:0000244|PDB:2Q37}.
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


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