UniProt Accession

 ALR_HUMAN; P55789; Q53YM6; Q8TAH6; Q9H290; Q9UK40 

Genbank Protein ID

 AF183892; AF124604; AF306863; AY550027; AC005606; BC002429; BC028348; AF146394; U31176 

Genbank Nucleotide ID

 AAD56538.1; AAD17328.1; AAG38105.1; AAS55642.1; AAH02429.1; AAH28348.2; AAD36986.1; AAA96390.2 

Protein Name

 FAD-linked sulfhydryl oxidase ALR 

Protein Synonyms/Alias

 Augmenter of liver regeneration; hERV1; Hepatopoietin 

Gene Name

 GFER 

Gene Synonyms/Alias

 ALR; HERV1; HPO 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
78	CRACVDFKTWMRTQQ	ubiquitination	[1, 2, 3]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Isoform 1: 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. 

Sequence Annotation

 DOMAIN 95 195 ERV/ALR sulfhydryl oxidase.
 NP_BIND 99 107 FAD.
 NP_BIND 171 183 FAD.
 NP_BIND 194 195 FAD.
 BINDING 111 111 FAD.
 BINDING 140 140 FAD.
 MOD_RES 59 59 Phosphoserine.
 DISULFID 95 95 Interchain (with C-204).
 DISULFID 142 145 Redox-active.
 DISULFID 171 188
 DISULFID 204 204 Interchain (with C-95).  

Keyword

 3D-structure; Alternative splicing; Cataract; Complete proteome; Cytoplasm; Disease mutation; Disulfide bond; FAD; Flavoprotein; Growth factor; Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Secreted. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 205 AA 

Protein Sequence

Gene Ontology

 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
 GO:0015035; F:protein disulfide oxidoreductase activity; IDA:UniProtKB.
 GO:0016972; F:thiol oxidase activity; IEA:EC.
 GO:0008283; P:cell proliferation; NAS:UniProtKB.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0006626; P:protein targeting to mitochondrion; TAS:Reactome.
 GO:0007283; P:spermatogenesis; NAS:UniProtKB. 

Interpro

 IPR017905; ERV/ALR_sulphydryl_oxidase.
 IPR006863; Evr1_Alr. 

Pfam

 PF04777; Evr1_Alr 

SMART

  

PROSITE

 PS51324; ERV_ALR 

PRINTS