[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CSRP3, AND TISSUE SPECIFICITY. DOI=10.1016/S0006-291X(02)00768-4; PubMed=12127981 [NCBI, ExPASy, EBI, Israel, Japan] Flick M.J., Konieczny S.F.; "Identification of putative mammalian D-lactate dehydrogenase enzymes."; Biochem. Biophys. Res. Commun. 295:910-916(2002).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Brain, and Colon; 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).

Comments

CATALYTIC ACTIVITY: (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c.
COFACTOR: FAD (By similarity).
SUBUNIT: Interacts with CSRP3.
SUBCELLULAR LOCATION: Mitochondrion (By similarity).

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

Name	1
Isoform ID	Q86WU2-1
Note: No experimental confirmation available.
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q86WU2-2
Features which should be applied to build the isoform sequence: VSP_052253.

TISSUE SPECIFICITY: Expressed moderately in heart and liver and at lower levels in skeletal muscle and kidney.
SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
SEQUENCE CAUTION:
- Sequence=AAM50322.1; Type=Frameshift; Positions=Several;

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

AY092767; AAM50322.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC040279; AAH40279.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047902; AAH47902.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_705690.2; -.
NP_919417.1; -.

UniGene

Hs.380929

3D structure databases

ModBase

Q86WU2.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12892; -.

Organism-specific databases

HGNC:19708; LDHD.

607490; gene. [NCBI / EBI]

PharmGKB

PA134917525; -.

GeneCards

Q86WU2.

Gene expression databases

CleanEx

HS_LDHD; -.

GermOnline

ENSG00000166816; Homo sapiens.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR016167; FAD-bd_2_sub1.
IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
IPR004113; FAD-linked_oxidase_C.
IPR006094; Oxid_FAD_bind_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.

Pfam

PF02913; FAD-oxidase_C; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.

PROSITE

PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q86WU2.

Genome annotation databases

Ensembl

ENSG00000166816; Homo sapiens. [Contig view]

GeneID

197257; -.

KEGG

hsa:197257; -.

Phylogenomic databases

HOVERGEN

Q86WU2; -.

Other

LDHD; Homo sapiens.

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

Keywords

Alternative splicing; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Polymorphism; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 507`		`Probable D-lactate dehydrogenase, mitochondrial.`	`PRO_0000262952`
`DOMAIN`	`62 265`	`204`	`FAD-binding PCMH-type.`
`VAR_SEQ`	`211 233`		`Missing (in isoform 2).`	`VSP_052253`
`VARIANT`	`233 233`	`1`	`R -> K (in dbSNP:rs11644820 [NCBI]).`	`VAR_029561`
`CONFLICT`	`323 323`		`T -> I (in Ref. 1; AAM50322).`

Sequence information

Length: 507 AA [This is the length of the unprocessed precursor]

Molecular weight: 54871 Da [This is the MW of the unprocessed precursor]

CRC64: 5625743709939182 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARLLRSATW ELFPWRGYCS QKAKGELCRD FVEALKAVVG GSHVSTAAVV REQHGRDESV 

        70         80         90        100        110        120 
HRCEPPDAVV WPQNVEQVSR LAALCYRQGV PIIPFGTGTG LEGGVCAVQG GVCVNLTHMD 

       130        140        150        160        170        180 
RILELNQEDF SVVVEPGVTR KALNAHLRDS GLWFPVDPGA DASLCGMAAT GASGTNAVRY 

       190        200        210        220        230        240 
GTMRDNVLNL EVVLPDGRLL HTAGRGRHFR FGFWPEIPHH TAWYSPCVSL GRRKSAAGYN 

       250        260        270        280        290        300 
LTGLFVGSEG TLGLITATTL RLHPAPEATV AATCAFPSVQ AAVDSTVHIL QAAVPVARIE 

       310        320        330        340        350        360 
FLDEVMMDAC NRYSKLNCLV APTLFLEFHG SQQALEEQLQ RTEEIVQQNG ASDFSWAKEA 

       370        380        390        400        410        420 
EERSRLWTAR HNAWYAALAT RPGCKGYSTD VCVPISRLPE IVVQTKEDLN ASGLTGSIVG 

       430        440        450        460        470        480 
HVGDGNFHCI LLVNPDDAEE LGRVKAFAEQ LGRRALALHG TCTGEHGIGM GKRQLLQEEV 

       490        500 
GAVGVETMRQ LKAVLDPQGL MNPGKVL

Q86WU2 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