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Reviewed, UniProtKB/Swiss-Prot P56213 (ALR_MOUSE)

Last modified November 3, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation By similarity.

Catalytic activity

4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O.

Cofactor

FAD By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Ontologies

Keywords
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionthiol oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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

Amino acid modifications

Disulfide bond88Interchain (with C-124) By similarity
Disulfide bond135 ↔ 138Redox-active Potential
Disulfide bond164 ↔ 181 By similarity
Disulfide bond197Interchain (with C-15) 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
P56213-1 [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]Giorda R., Trucco M.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: 16141072] [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: 15489334] [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

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.
IPIIPI00410978.
RefSeqNP_075527.2.
UniGeneMm.28124

3D structure databases

HSSPHSSP built from PDB template 1OQC based on UniProtKB Q63042.
SMRP56213. Positions 13-124.
ModBaseSearch...

Protein-protein interaction databases

STRINGP56213.

PTM databases

PhosphoSiteP56213.

Proteomic databases

PRIDEP56213.

Genome annotation databases

EnsemblENSMUST00000046839; ENSMUSP00000049186; ENSMUSG00000040888; Mus musculus. [Genome view]
GeneID11692.
KEGGmmu:11692.
UCSCuc008axr.1. mouse.

Organism-specific databases

CTD11692.
MGIMGI:107757. Gfer.

Phylogenomic databases

HOVERGENP56213.
OMACTDFKSW.

Enzyme and pathway databases

BRENDA1.8.3.2. 244.

Gene expression databases

ArrayExpressP56213.
BgeeP56213.
GenevestigatorP56213.
GermOnlineENSMUSG00000040888. Mus musculus.

Family and domain databases

InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
IPR006863. Evr1_Alr.
[Graphical view]
Gene3DG3DSA:1.20.120.310. Evr1_Alr. 1 hit.
PfamPF04777. Evr1_Alr. 1 hit.
[Graphical view]
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: November 3, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents