ALR_MOUSE
ID ALR_MOUSE Reviewed; 198 AA.
AC P56213; Q8CIF8; Q9JJE6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=FAD-linked sulfhydryl oxidase ALR;
DE EC=1.8.3.2;
DE AltName: Full=Augmenter of liver regeneration;
GN Name=Gfer; Synonyms=Alr; ORFNames=MNCb-0663;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=8900538; DOI=10.1007/bf03402206;
RA Giorda R., Hagiya M., Seki T., Shimonishi M., Sakai H., Michaelson J.,
RA Francavilla A., Starzl T.E., Trucco M.;
RT "Analysis of the structure and expression of the augmenter of liver
RT regeneration (ALR) gene.";
RL Mol. Med. 2:97-108(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-198.
RC STRAIN=C57BL/6 X CBA;
RA Cheng J., Zhong Y.W., Liu Y., Dong J., Yang J.Z., Chen J.M.;
RT "Cloning and sequence analysis of a mouse cDNA coding for augmenter of
RT liver regeneration.";
RL Zhonghua Gan Zang Bing Za Zhi 4:138-140(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that regenerates the redox-
CC active disulfide bonds in CHCHD4/MIA40, a chaperone essential for
CC disulfide bond formation and protein folding in the mitochondrial
CC intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient
CC intermolecular disulfide bridge with GFER/ERV1, resulting in
CC regeneration of the essential disulfide bonds in CHCHD4/MIA40, while
CC GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or
CC molecular oxygen (By similarity). {ECO:0000250|UniProtKB:P55789}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with CHCHD4/MIA40.
CC {ECO:0000250|UniProtKB:P55789}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P55789}. Mitochondrion
CC {ECO:0000250|UniProtKB:P55789}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the liver and in
CC testis. {ECO:0000269|PubMed:8900538}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD36987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U40494; AAD10339.1; -; Genomic_DNA.
DR EMBL; AB041561; BAA95045.1; -; mRNA.
DR EMBL; AK146579; BAE27275.1; -; mRNA.
DR EMBL; CH466606; EDL22354.1; -; Genomic_DNA.
DR EMBL; BC023941; AAH23941.1; -; mRNA.
DR EMBL; AF148688; AAD36987.1; ALT_INIT; mRNA.
DR CCDS; CCDS28492.1; -.
DR RefSeq; NP_075527.2; NM_023040.3.
DR AlphaFoldDB; P56213; -.
DR SMR; P56213; -.
DR BioGRID; 198079; 4.
DR STRING; 10090.ENSMUSP00000049186; -.
DR iPTMnet; P56213; -.
DR PhosphoSitePlus; P56213; -.
DR SwissPalm; P56213; -.
DR EPD; P56213; -.
DR jPOST; P56213; -.
DR MaxQB; P56213; -.
DR PaxDb; P56213; -.
DR PeptideAtlas; P56213; -.
DR PRIDE; P56213; -.
DR ProteomicsDB; 282076; -.
DR Antibodypedia; 42516; 274 antibodies from 31 providers.
DR DNASU; 11692; -.
DR Ensembl; ENSMUST00000046839; ENSMUSP00000049186; ENSMUSG00000040888.
DR Ensembl; ENSMUST00000234197; ENSMUSP00000157329; ENSMUSG00000040888.
DR Ensembl; ENSMUST00000234520; ENSMUSP00000157116; ENSMUSG00000040888.
DR GeneID; 11692; -.
DR KEGG; mmu:11692; -.
DR UCSC; uc008axr.1; mouse.
DR CTD; 2671; -.
DR MGI; MGI:107757; Gfer.
DR VEuPathDB; HostDB:ENSMUSG00000040888; -.
DR eggNOG; KOG3355; Eukaryota.
DR GeneTree; ENSGT00390000001979; -.
DR HOGENOM; CLU_070631_1_1_1; -.
DR InParanoid; P56213; -.
DR OMA; KPCRSCT; -.
DR OrthoDB; 1537996at2759; -.
DR PhylomeDB; P56213; -.
DR TreeFam; TF105271; -.
DR BioGRID-ORCS; 11692; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Gfer; mouse.
DR PRO; PR:P56213; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P56213; protein.
DR Bgee; ENSMUSG00000040888; Expressed in seminiferous tubule of testis and 259 other tissues.
DR ExpressionAtlas; P56213; baseline and differential.
DR Genevisible; P56213; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISS:UniProtKB.
DR GO; GO:0072717; P:cellular response to actinomycin D; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0097237; P:cellular response to toxic substance; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IBA:GO_Central.
DR GO; GO:0097421; P:liver regeneration; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR039799; ALR/ERV.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR PANTHER; PTHR12645; PTHR12645; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; FAD; Flavoprotein; Growth factor; Mitochondrion;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..198
FT /note="FAD-linked sulfhydryl oxidase ALR"
FT /id="PRO_0000208549"
FT DOMAIN 88..188
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92..100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 164..176
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 88
FT /note="Interchain (with C-197)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 135..138
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 164..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 197
FT /note="Interchain (with C-88)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT CONFLICT 40
FT /note="A -> P (in Ref. 1; AAD10339)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="A -> S (in Ref. 1; AAD10339, 5; AAH23941 and 6;
FT AAD36987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22877 MW; 4828C5D5B2F61054 CRC64;
MAAPSEPAGF PRGSRFSFLP GGARSEMTDD LVTDARGRGA RHRDDTTPAA APAPQGLEHG
KRPCRACVDF KSWMRTQQKR DIKFREDCPQ DREELGRHTW AFLHTLAAYY PDRPTPEQQQ
DMAQFIHIFS KFYPCEECAE DIRKRIGRNQ PDTSTRVSFS QWLCRLHNEV NRKLGKPDFD
CSRVDERWRD GWKDGSCD
