[1]	NUCLEOTIDE SEQUENCE [MRNA]. Atanasova S., von Ahsen N., Schlumbohm C., Wieland E., Oellerich M., Armstrong V.; "Free radical scavenging enzymes in Callithrix jacchus."; Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Maintains high levels of reduced glutathione in the cytosol (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + NADP⁺ = glutathione disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer; disulfide-linked (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (By similarity). Cytoplasm (By similarity).

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

Name	Mitochondrial
Isoform ID	A2TIL1-1
This is the isoform sequence displayed in this entry.

Name	Cytoplasmic
Isoform ID	A2TIL1-2
Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity).
Features which should be applied to build the isoform sequence: VSP_030441.

SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase 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

EF203010; ABN05297.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

A2TIL1; 62-522.

ModBase

A2TIL1.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR006322; Glut_reduct_1.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01421; gluta_reduc_1; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

BLOCKS

A2TIL1.

Phylogenomic databases

HOVERGEN

A2TIL1; -.

Other

ProtoNet

A2TIL1.

UniRef

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

Keywords

Acetylation; Alternative initiation; Cytoplasm; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Phosphoprotein; Redox-active center; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 43`	`43`	`Mitochondrion (Potential).`
`CHAIN`	`44 522`	`479`	`Glutathione reductase, mitochondrial.`	`PRO_0000314948`
`NP_BIND`	`94 102`	`9`	`FAD (By similarity).`
`ACT_SITE`	`511 511`		`Proton acceptor (By similarity).`
`MOD_RES`	`65 65`		`Phosphotyrosine (By similarity).`
`DISULFID`	`102 107`		`Redox-active (By similarity).`
`DISULFID`	`134 134`		`Interchain (By similarity).`
`VAR_SEQ`	`1 43`		`Missing (in isoform Cytoplasmic).`	`VSP_030441`

Sequence information

Length: 522 AA [This is the length of the unprocessed precursor]

Molecular weight: 56193 Da [This is the MW of the unprocessed precursor]

CRC64: A952357C8E8E0E86 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALLPRALSS GGRPSWRRAA RASRGFPLPL PFPAAATHAL SRAMACRQEP QPQGPPPSAG 

        70         80         90        100        110        120 
AVVSYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS 

       130        140        150        160        170        180 
EFLHDHGDYG FSSCEGKFNW RVIKEKRDTY VSRLNTIYQN NLTKAHIEII HGHAVFTSDT 

       190        200        210        220        230        240 
KPTIEVSGRK YTAPHILIAT GGMPSSPHES QIPGASLGIT SDGFFELEEL PSRSVIVGAG 

       250        260        270        280        290        300 
YIAVEIAGIL SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQVKEVKK 

       310        320        330        340        350        360 
TSSGLEVSLV TAVPGRLPVM TTISDVDCLL WAIGRDPNSK GLSLNKLGIK TDDKGHIIVD 

       370        380        390        400        410        420 
EFQNTNVKGI YAVGDVCGKA LLTPVAIAAG RKLAHRLFEN KEDSKLDYNN IPTVVFSHPP 

       430        440        450        460        470        480 
IGTVGLTEDE AIHKYGKENV KIYSTSFTPM YHAVTKRKTK CVMKMVCAYE EEKVVGIHMQ 

       490        500        510        520 
GLGCDEMLQG FAVAVKMGAT KADFDNTVAI HPTSSEELVP LR

A2TIL1 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