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Protein

FAD-linked sulfhydryl oxidase ALR

Gene

Gfer

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. May have a function in liver regeneration and spermatogenesis.1 Publication

Catalytic activityi

2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.

Cofactori

FAD1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041FAD2 Publications
Binding sitei133 – 1331FAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi92 – 1009FAD2 Publications
Nucleotide bindingi164 – 17613FAD2 PublicationsAdd
BLAST
Nucleotide bindingi187 – 1882FAD2 Publications

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: UniProtKB
  2. protein disulfide oxidoreductase activity Source: UniProtKB
  3. thiol oxidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.8.3.2. 5301.
ReactomeiREACT_199211. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD-linked sulfhydryl oxidase ALR (EC:1.8.3.2)
Alternative name(s):
Augmenter of liver regeneration
Gene namesi
Name:Gfer
Synonyms:Alr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi61845. Gfer.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198FAD-linked sulfhydryl oxidase ALRPRO_0000208550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi88 – 88Interchain (with C-197)1 PublicationPROSITE-ProRule annotation
Disulfide bondi135 ↔ 138Redox-active1 PublicationPROSITE-ProRule annotation
Disulfide bondi164 ↔ 1811 PublicationPROSITE-ProRule annotation
Disulfide bondi197 – 197Interchain (with C-88)1 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ63042.
PRIDEiQ63042.

Expressioni

Gene expression databases

ExpressionAtlasiQ63042. baseline.
GenevestigatoriQ63042.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017917.

Structurei

Secondary structure

1
198
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi92 – 10817Combined sources
Helixi116 – 13217Combined sources
Helixi136 – 14813Combined sources
Helixi156 – 17318Combined sources
Helixi181 – 1833Combined sources
Helixi184 – 1885Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OQCX-ray1.80A/B/C/D74-198[»]
3R7CX-ray2.40A/B/C/D74-198[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 188101ERV/ALR sulfhydryl oxidasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ERV/ALR sulfhydryl oxidase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5054.
GeneTreeiENSGT00390000001979.
HOGENOMiHOG000195924.
HOVERGENiHBG000235.
InParanoidiQ63042.
KOiK17783.
OMAiMDDLATD.
OrthoDBiEOG7HMS2X.
PhylomeDBiQ63042.
TreeFamiTF105271.

Family and domain databases

Gene3Di1.20.120.310. 1 hit.
InterProiIPR017905. ERV/ALR_sulphydryl_oxidase.
[Graphical view]
PfamiPF04777. Evr1_Alr. 1 hit.
[Graphical view]
SUPFAMiSSF69000. SSF69000. 1 hit.
PROSITEiPS51324. ERV_ALR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63042-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPSEPAGF PRGSRFSFLP GGAHSEMTDD LVTDARGRGA RHRKDNAPAA
60 70 80 90 100
APAPKGLEHG KRPCRACVDF KSWMRTQQKR DIKFREDCPQ DREELGRNTW
110 120 130 140 150
AFLHTLAAYY PDMPTPEQQQ DMAQFIHIFS KFYPCEECAE DIRKRIDRSQ
160 170 180 190
PDTSTRVSFS QWLCRLHNEV NRKLGKPDFD CSRVDERWRD GWKDGSCD
Length:198
Mass (Da):22,837
Last modified:December 16, 2008 - v2
Checksum:i46AD9BEC2EF0C393
GO

Sequence cautioni

The sequence AAF12808.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA06399.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30735 mRNA. Translation: BAA06399.1. Different initiation.
AF197192 Genomic DNA. Translation: AAF12808.1. Different initiation.
PIRiI80184.
RefSeqiNP_037354.2. NM_013222.2.
UniGeneiRn.11039.

Genome annotation databases

EnsembliENSRNOT00000017917; ENSRNOP00000017917; ENSRNOG00000013370.
GeneIDi27100.
KEGGirno:27100.
UCSCiRGD:61845. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30735 mRNA. Translation: BAA06399.1. Different initiation.
AF197192 Genomic DNA. Translation: AAF12808.1. Different initiation.
PIRiI80184.
RefSeqiNP_037354.2. NM_013222.2.
UniGeneiRn.11039.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OQCX-ray1.80A/B/C/D74-198[»]
3R7CX-ray2.40A/B/C/D74-198[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017917.

Proteomic databases

PaxDbiQ63042.
PRIDEiQ63042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017917; ENSRNOP00000017917; ENSRNOG00000013370.
GeneIDi27100.
KEGGirno:27100.
UCSCiRGD:61845. rat.

Organism-specific databases

CTDi2671.
RGDi61845. Gfer.

Phylogenomic databases

eggNOGiCOG5054.
GeneTreeiENSGT00390000001979.
HOGENOMiHOG000195924.
HOVERGENiHBG000235.
InParanoidiQ63042.
KOiK17783.
OMAiMDDLATD.
OrthoDBiEOG7HMS2X.
PhylomeDBiQ63042.
TreeFamiTF105271.

Enzyme and pathway databases

BRENDAi1.8.3.2. 5301.
ReactomeiREACT_199211. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiQ63042.
NextBioi608049.
PROiQ63042.

Gene expression databases

ExpressionAtlasiQ63042. baseline.
GenevestigatoriQ63042.

Family and domain databases

Gene3Di1.20.120.310. 1 hit.
InterProiIPR017905. ERV/ALR_sulphydryl_oxidase.
[Graphical view]
PfamiPF04777. Evr1_Alr. 1 hit.
[Graphical view]
SUPFAMiSSF69000. SSF69000. 1 hit.
PROSITEiPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: expression of biologically active recombinant ALR and demonstration of tissue distribution."
    Hagiya M., Francavilla A., Polimeno L., Ihara I., Sakai H., Seki T., Shimonishi M., Porter K.A., Starzl T.E.
    Proc. Natl. Acad. Sci. U.S.A. 91:8142-8146(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN LIVER REGENERATION.
    Strain: Fischer 344.
    Tissue: Liver.
  2. "Cloning and analysis of the genomic DNA sequence of augmenter of liver regeneration from rat."
    Dong J., Cheng J., Wang Q., Shi S., Wang G., Si C.
    Chin. Med. Sci. J. 17:63-67(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
  3. "The crystal structure of augmenter of liver regeneration: a mammalian FAD-dependent sulfhydryl oxidase."
    Wu C.-K., Dailey T.A., Dailey H.A., Wang B.-C., Rose J.P.
    Protein Sci. 12:1109-1118(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT, COFACTOR, DISULFIDE BONDS.
  4. "The structure of augmenter of liver regeneration crystallized in the presence of 50 mM CdCl2 reveals a novel Cd2Cl4O6 cluster that aids in crystal packing."
    Florence Q., Wu C.K., Habel J., Swindell J.T. II, Wang B.C., Rose J.P.
    Acta Crystallogr. D 68:1128-1133(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 74-198 IN COMPLEX WITH FAD, SUBUNIT.

Entry informationi

Entry nameiALR_RAT
AccessioniPrimary (citable) accession number: Q63042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 16, 2008
Last modified: January 7, 2015
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.