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Q63042

- ALR_RAT

UniProt

Q63042 - ALR_RAT

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Protein
FAD-linked sulfhydryl oxidase ALR
Gene
Gfer, Alr
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

FAD.1 Publication

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi92 – 1009FAD
Nucleotide bindingi164 – 17613FAD
Add
BLAST
Nucleotide bindingi187 – 1882FAD

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 ALR
PRO_0000208550Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ63042.
PRIDEiQ63042.

Expressioni

Gene expression databases

GenevestigatoriQ63042.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017917.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ63042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 188101ERV/ALR sulfhydryl oxidase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5054.
GeneTreeiENSGT00390000001979.
HOGENOMiHOG000195924.
HOVERGENiHBG000235.
InParanoidiQ63042.
KOiK17783.
OMAiQKRDSKF.
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

MAAPSEPAGF PRGSRFSFLP GGAHSEMTDD LVTDARGRGA RHRKDNAPAA    50
APAPKGLEHG KRPCRACVDF KSWMRTQQKR DIKFREDCPQ DREELGRNTW 100
AFLHTLAAYY PDMPTPEQQQ DMAQFIHIFS KFYPCEECAE DIRKRIDRSQ 150
PDTSTRVSFS QWLCRLHNEV NRKLGKPDFD CSRVDERWRD GWKDGSCD 198
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.
The sequence BAA06399.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D30735 mRNA. Translation: BAA06399.1 . Different initiation.
AF197192 Genomic DNA. Translation: AAF12808.1 . Different initiation.
PIRi I80184.
RefSeqi NP_037354.2. NM_013222.2.
UniGenei Rn.11039.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OQC X-ray 1.80 A/B/C/D 74-198 [» ]
3R7C X-ray 2.40 A/B/C/D 74-198 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000017917.

Proteomic databases

PaxDbi Q63042.
PRIDEi Q63042.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000017917 ; ENSRNOP00000017917 ; ENSRNOG00000013370 .
GeneIDi 27100.
KEGGi rno:27100.
UCSCi RGD:61845. rat.

Organism-specific databases

CTDi 2671.
RGDi 61845. Gfer.

Phylogenomic databases

eggNOGi COG5054.
GeneTreei ENSGT00390000001979.
HOGENOMi HOG000195924.
HOVERGENi HBG000235.
InParanoidi Q63042.
KOi K17783.
OMAi QKRDSKF.
OrthoDBi EOG7HMS2X.
PhylomeDBi Q63042.
TreeFami TF105271.

Enzyme and pathway databases

BRENDAi 1.8.3.2. 5301.
Reactomei REACT_199211. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTracei Q63042.
NextBioi 608049.
PROi Q63042.

Gene expression databases

Genevestigatori Q63042.

Family and domain databases

Gene3Di 1.20.120.310. 1 hit.
InterProi IPR017905. ERV/ALR_sulphydryl_oxidase.
[Graphical view ]
Pfami PF04777. Evr1_Alr. 1 hit.
[Graphical view ]
SUPFAMi SSF69000. SSF69000. 1 hit.
PROSITEi PS51324. ERV_ALR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 102 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

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