NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).

[2]

NUCLEOTIDE SEQUENCE [MRNA] OF 17-421 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
STRAIN=Wistar;
DOI=10.1074/jbc.M105929200; PubMed=11431483 [NCBI, ExPASy, EBI, Israel, Japan]
Vaz F.M., Ofman R., Westinga K., Back J.W., Wanders R.J.A.;
"Molecular and biochemical characterization of rat epsilon-N-trimethyllysine hydroxylase, the first enzyme of carnitine biosynthesis.";
J. Biol. Chem. 276:33512-33517(2001).

Comments

FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
CATALYTIC ACTIVITY: N₆,N₆,N⁶-trimethyl-L-lysine + 2-oxoglutarate + O₂ = 3-hydroxy-N₆,N₆,N⁶-trimethyl-L-lysine + succinate + CO₂.
COFACTOR: Iron.
COFACTOR: Ascorbate.
PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Mitochondrion matrix.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q91ZW6-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q91ZW6-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_021580.

SIMILARITY: Belongs to the gamma-BBH/TMLD family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC085923; AAH85923.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF374406; AAL01252.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_596878.2; -.

UniGene

Rn.3607

3D structure databases

ModBase

Q91ZW6.

Organism-specific databases

RGD

620629; Tmlhe.

Gene expression databases

ArrayExpress

Q91ZW6; -.

GermOnline

ENSRNOG00000000729; Rattus norvegicus.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0031418;	Molecular function: L-ascorbic acid binding (inferred from electronic annotation from InterPro).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0050353;	Molecular function: trimethyllysine dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0045329;	Biological process: carnitine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003819; Taurine_dOase.
IPR012776; Trimethyllysine_dOase.
Graphical view of domain structure.

PANTHER

PTHR10696:SF2; tMLys_dOase; 1.

Pfam

PF02668; TauD; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02410; carnitine_TMLD; 1.

ProtoNet

Q91ZW6.

Genome annotation databases

Ensembl

ENSRNOG00000000729; Rattus norvegicus. [Contig view]

GeneID

170898; -.

KEGG

rno:170898; -.

NMPDR

fig|10116.3.peg.17238; -.

Phylogenomic databases

HOVERGEN

Q91ZW6; -.

Other

NextBio

621309; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Carnitine biosynthesis; Dioxygenase; Direct protein sequencing; Iron; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 421`		`Trimethyllysine dioxygenase, mitochondrial.`	`PRO_0000002797`
`VAR_SEQ`	`62 62`		`L -> LGTKPRALRLLEL (in isoform 2).`	`VSP_021580`

Sequence information

Length: 421 AA [This is the length of the unprocessed precursor]

Molecular weight: 49568 Da [This is the MW of the unprocessed precursor]

CRC64: 487AB5FCA0D02D25 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWYHKLLHQQ SRLQNLMKRG DIAHGLRLSG FKSLFPFSLH WCHTASKSVN CTWHQHEDHL 

        70         80         90        100        110        120 
ELQYASTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTIR LDESTLFFTW 

       130        140        150        160        170        180 
PDGHVTRYDL DWLVKNSYEG QKQEVIQPRV LWNAKLYQDA QLPSVDFQGF LETKEGLKKF 

       190        200        210        220        230        240 
LQNFLLYGIA FVENVPPTQE HTEKLARRVS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 

       250        260        270        280        290        300 
RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAQQ VLQRAPEEFD LLSQVPLKHE 

       310        320        330        340        350        360 
YIENVGQCHN HMIGVGPILN IYPWNKELYL IRYNNYDRAV INTVPYDVVR RWYAAHRTLT 

       370        380        390        400        410        420 
TELRRPENEL WVKLKPGKVL FIDNWRVLHG RESFTGYRQL CGCYLTRDDV LNTARILGLH 


A

Q91ZW6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools