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P56213 (ALR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAD-linked sulfhydryl oxidase ALR

EC=1.8.3.2
Alternative name(s):
Augmenter of liver regeneration
Gene names
Name:Gfer
Synonyms:Alr
ORF Names:MNCb-0663
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm. Mitochondrion intermembrane space By similarity.

Tissue specificity

Preferentially expressed in the liver and in testis. Ref.1

Sequence similarities

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Sequence caution

The sequence AAD36987.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198FAD-linked sulfhydryl oxidase ALR
PRO_0000208549

Regions

Domain88 – 188101ERV/ALR sulfhydryl oxidase
Nucleotide binding92 – 1009FAD By similarity
Nucleotide binding164 – 17613FAD By similarity
Nucleotide binding187 – 1882FAD By similarity

Sites

Binding site1041FAD By similarity
Binding site1331FAD By similarity

Amino acid modifications

Disulfide bond88Interchain (with C-197) By similarity
Disulfide bond135 ↔ 138Redox-active By similarity
Disulfide bond164 ↔ 181 By similarity
Disulfide bond197Interchain (with C-88) By similarity

Experimental info

Sequence conflict401A → P in AAD10339. Ref.1
Sequence conflict491A → S in AAD10339. Ref.1
Sequence conflict491A → S in AAH23941. Ref.5
Sequence conflict491A → S in AAD36987. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P56213 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 4828C5D5B2F61054

FASTA19822,877
        10         20         30         40         50         60 
MAAPSEPAGF PRGSRFSFLP GGARSEMTDD LVTDARGRGA RHRDDTTPAA APAPQGLEHG 

        70         80         90        100        110        120 
KRPCRACVDF KSWMRTQQKR DIKFREDCPQ DREELGRHTW AFLHTLAAYY PDRPTPEQQQ 

       130        140        150        160        170        180 
DMAQFIHIFS KFYPCEECAE DIRKRIGRNQ PDTSTRVSFS QWLCRLHNEV NRKLGKPDFD 

       190 
CSRVDERWRD GWKDGSCD 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the structure and expression of the augmenter of liver regeneration (ALR) gene."
Giorda R., Hagiya M., Seki T., Shimonishi M., Sakai H., Michaelson J., Francavilla A., Starzl T.E., Trucco M.
Mol. Med. 2:97-108(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: C57BL/6 X CBA.
[2]"Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[6]"Cloning and sequence analysis of a mouse cDNA coding for augmenter of liver regeneration."
Cheng J., Zhong Y.W., Liu Y., Dong J., Yang J.Z., Chen J.M.
Zhonghua Gan Zang Bing Za Zhi 4:138-140(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-198.
Strain: C57BL/6 X CBA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40494 Genomic DNA. Translation: AAD10339.1.
AB041561 mRNA. Translation: BAA95045.1.
AK146579 mRNA. Translation: BAE27275.1.
CH466606 Genomic DNA. Translation: EDL22354.1.
BC023941 mRNA. Translation: AAH23941.1.
AF148688 mRNA. Translation: AAD36987.1. Different initiation.
CCDSCCDS28492.1.
RefSeqNP_075527.2. NM_023040.3.
UniGeneMm.28124.

3D structure databases

ProteinModelPortalP56213.
SMRP56213. Positions 86-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP56213. 2 interactions.
MINTMINT-4129999.

PTM databases

PhosphoSiteP56213.

Proteomic databases

PaxDbP56213.
PRIDEP56213.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046839; ENSMUSP00000049186; ENSMUSG00000040888.
GeneID11692.
KEGGmmu:11692.
UCSCuc008axr.1. mouse.

Organism-specific databases

CTD2671.
MGIMGI:107757. Gfer.

Phylogenomic databases

eggNOGCOG5054.
GeneTreeENSGT00390000001979.
HOGENOMHOG000195924.
HOVERGENHBG000235.
InParanoidQ9JJE6.
KOK17783.
OMAQKRDSKF.
OrthoDBEOG7HMS2X.
PhylomeDBP56213.
TreeFamTF105271.

Gene expression databases

BgeeP56213.
GenevestigatorP56213.

Family and domain databases

Gene3D1.20.120.310. 1 hit.
InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
[Graphical view]
PfamPF04777. Evr1_Alr. 1 hit.
[Graphical view]
SUPFAMSSF69000. SSF69000. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279349.
PROP56213.
SOURCESearch...

Entry information

Entry nameALR_MOUSE
AccessionPrimary (citable) accession number: P56213
Secondary accession number(s): Q8CIF8, Q9JJE6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot