ALR_HUMAN
ID ALR_HUMAN Reviewed; 205 AA.
AC P55789; Q53YM6; Q8TAH6; Q9H290; Q9UK40;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=FAD-linked sulfhydryl oxidase ALR;
DE EC=1.8.3.2;
DE AltName: Full=Augmenter of liver regeneration;
DE Short=hERV1;
DE AltName: Full=Hepatopoietin;
GN Name=GFER; Synonyms=ALR, HERV1, HPO;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu M.-M., He F.-C., Wei H.-D., Zhou W.-Q.;
RT "Genomic structure, chromosomal localization, and characterization of a
RT functional promoter for human hepatopoietin (HPO) gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Li Y., Xing G.-C., He F.-C., Wei H.-D., Zhang C.-G., Zhu L., Yu Y.-T.;
RT "HERV different transcription sequence.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RA Jun L., Wangxiang X., Xiaoming Y.;
RT "Isolation of human HPO cDNA from human liver tissue.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Dai W.-J., Jiang H.-C.;
RT "Human augmenter of liver regeneration/hepatopoietin gene open reading
RT frame sequence.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-205.
RC TISSUE=Placenta, and Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-205.
RX PubMed=10712775;
RA Cheng J., Zhong Y.;
RT "Cloning and sequence analysis of human genomic DNA of augmenter of liver
RT regeneration hepatitis.";
RL Zhonghua Gan Zang Bing Za Zhi 8:12-14(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-205.
RC TISSUE=Renal cyst lining cell;
RX PubMed=8575761; DOI=10.1006/geno.1995.9950;
RA Lisowsky T., Weinstat-Saslow D.L., Barton N., Reeders S.T., Schneider M.C.;
RT "A new human gene located in the PKD1 region of chromosome 16 is a
RT functional homologue to ERV1 of yeast.";
RL Genomics 29:690-697(1995).
RN [9]
RP ALTERNATIVE SPLICING, AND SUBUNIT.
RX PubMed=12180965; DOI=10.1046/j.1432-1033.2002.03054.x;
RA Li Y., Wei K., Lu C., Li Y., Li M., Xing G., Wei H., Wang Q., Chen J.,
RA Wu C., Chen H., Yang S., He F.;
RT "Identification of hepatopoietin dimerization, its interacting regions and
RT alternative splicing of its transcription.";
RL Eur. J. Biochem. 269:3888-3893(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19397338; DOI=10.1021/bi900347v;
RA Daithankar V.N., Farrell S.R., Thorpe C.;
RT "Augmenter of liver regeneration: substrate specificity of a flavin-
RT dependent oxidoreductase from the mitochondrial intermembrane space.";
RL Biochemistry 48:4828-4837(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHCHD4.
RX PubMed=23676665; DOI=10.1091/mbc.e12-12-0862;
RA Fischer M., Horn S., Belkacemi A., Kojer K., Petrungaro C., Habich M.,
RA Ali M., Kuettner V., Bien M., Kauff F., Dengjel J., Herrmann J.M.,
RA Riemer J.;
RT "Protein import and oxidative folding in the mitochondrial intermembrane
RT space of intact mammalian cells.";
RL Mol. Biol. Cell 24:2160-2170(2013).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23186364; DOI=10.1111/tra.12030;
RA Sztolsztener M.E., Brewinska A., Guiard B., Chacinska A.;
RT "Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial
RT biogenesis of human MIA40.";
RL Traffic 14:309-320(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 81-205, CATALYTIC ACTIVITY,
RP FUNCTION, SUBUNIT, DISULFIDE BONDS, FAD-BINDING SITES, AND CHARACTERIZATION
RP OF VARIANT MPMCD HIS-194.
RX PubMed=20593814; DOI=10.1021/bi100912m;
RA Daithankar V.N., Schaefer S.A., Dong M., Bahnson B.J., Thorpe C.;
RT "Structure of the human sulfhydryl oxidase augmenter of liver regeneration
RT and characterization of a human mutation causing an autosomal recessive
RT myopathy.";
RL Biochemistry 49:6737-6745(2010).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-205 IN COMPLEX WITH FAD,
RP FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS, AND INTERACTION WITH CHCHD4.
RX PubMed=21383138; DOI=10.1073/pnas.1014542108;
RA Banci L., Bertini I., Calderone V., Cefaro C., Ciofi-Baffoni S., Gallo A.,
RA Kallergi E., Lionaki E., Pozidis C., Tokatlidis K.;
RT "Molecular recognition and substrate mimicry drive the electron-transfer
RT process between MIA40 and ALR.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4811-4816(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 91-205, FUNCTION, CATALYTIC
RP ACTIVITY, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=22224850; DOI=10.1021/ja209881f;
RA Banci L., Bertini I., Calderone V., Cefaro C., Ciofi-Baffoni S., Gallo A.,
RA Tokatlidis K.;
RT "An electron-transfer path through an extended disulfide relay system: the
RT case of the redox protein ALR.";
RL J. Am. Chem. Soc. 134:1442-1445(2012).
RN [19]
RP VARIANT MPMCD HIS-194, CHARACTERIZATION OF VARIANT MPMCD HIS-194, AND
RP TISSUE SPECIFICITY.
RX PubMed=19409522; DOI=10.1016/j.ajhg.2009.04.004;
RA Di Fonzo A., Ronchi D., Lodi T., Fassone E., Tigano M., Lamperti C.,
RA Corti S., Bordoni A., Fortunato F., Nizzardo M., Napoli L., Donadoni C.,
RA Salani S., Saladino F., Moggio M., Bresolin N., Ferrero I., Comi G.P.;
RT "The mitochondrial disulfide relay system protein GFER is mutated in
RT autosomal-recessive myopathy with cataract and combined respiratory-chain
RT deficiency.";
RL Am. J. Hum. Genet. 84:594-604(2009).
CC -!- FUNCTION: [Isoform 1]: FAD-dependent sulfhydryl oxidase that
CC regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a
CC chaperone essential for disulfide bond formation and protein folding in
CC the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40
CC forms a transient intermolecular disulfide bridge with GFER/ERV1,
CC resulting in regeneration of the essential disulfide bonds in
CC CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons
CC to cytochrome c or molecular oxygen. {ECO:0000269|PubMed:19397338,
CC ECO:0000269|PubMed:20593814, ECO:0000269|PubMed:21383138,
CC ECO:0000269|PubMed:22224850, ECO:0000269|PubMed:23186364,
CC ECO:0000269|PubMed:23676665}.
CC -!- FUNCTION: [Isoform 2]: May act as an autocrine hepatotrophic growth
CC factor promoting liver regeneration.
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 Evidence={ECO:0000269|PubMed:20593814, ECO:0000269|PubMed:22224850};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654,
CC ECO:0000269|PubMed:20593814, ECO:0000269|PubMed:21383138};
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form heterodimers of isoform
CC 1 and isoform 2 (PubMed:12180965, PubMed:20593814, PubMed:21383138,
CC PubMed:22224850). Interacts with CHCHD4/MIA40 (PubMed:23676665,
CC PubMed:21383138). {ECO:0000269|PubMed:12180965,
CC ECO:0000269|PubMed:20593814, ECO:0000269|PubMed:21383138,
CC ECO:0000269|PubMed:22224850, ECO:0000269|PubMed:23676665}.
CC -!- INTERACTION:
CC P55789; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-718281, EBI-742388;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion intermembrane space.
CC Mitochondrion {ECO:0000269|PubMed:23676665}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=HPO-205, lfALR;
CC IsoId=P55789-1; Sequence=Displayed;
CC Name=2; Synonyms=HPO-125, sfALR;
CC IsoId=P55789-2; Sequence=VSP_040393;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in the
CC testis and liver and low expression in the muscle.
CC {ECO:0000269|PubMed:19409522}.
CC -!- DISEASE: Myopathy, mitochondrial progressive, with congenital cataract,
CC hearing loss and developmental delay (MPMCD) [MIM:613076]: A disease
CC characterized by progressive myopathy and partial combined respiratory-
CC chain deficiency, congenital cataract, sensorineural hearing loss, and
CC developmental delay. {ECO:0000269|PubMed:19409522,
CC ECO:0000269|PubMed:20593814}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96390.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD36986.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD56538.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH02429.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH28348.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF183892; AAD56538.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF124604; AAD17328.1; -; mRNA.
DR EMBL; AF306863; AAG38105.1; -; mRNA.
DR EMBL; AY550027; AAS55642.1; -; mRNA.
DR EMBL; AC005606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002429; AAH02429.1; ALT_INIT; mRNA.
DR EMBL; BC028348; AAH28348.2; ALT_INIT; mRNA.
DR EMBL; AF146394; AAD36986.1; ALT_INIT; Genomic_DNA.
DR EMBL; U31176; AAA96390.2; ALT_FRAME; mRNA.
DR CCDS; CCDS32368.1; -. [P55789-1]
DR RefSeq; NP_005253.3; NM_005262.2. [P55789-1]
DR PDB; 3MBG; X-ray; 1.85 A; A/B/C=81-205.
DR PDB; 3O55; X-ray; 1.90 A; A=81-205.
DR PDB; 3TK0; X-ray; 1.61 A; A=81-205.
DR PDB; 3U2L; X-ray; 1.95 A; A=91-205.
DR PDB; 3U2M; X-ray; 2.00 A; A=91-205.
DR PDB; 3U5S; X-ray; 1.50 A; A=82-203.
DR PDB; 4LDK; X-ray; 2.04 A; A=81-205.
DR PDBsum; 3MBG; -.
DR PDBsum; 3O55; -.
DR PDBsum; 3TK0; -.
DR PDBsum; 3U2L; -.
DR PDBsum; 3U2M; -.
DR PDBsum; 3U5S; -.
DR PDBsum; 4LDK; -.
DR AlphaFoldDB; P55789; -.
DR BMRB; P55789; -.
DR SMR; P55789; -.
DR BioGRID; 108939; 89.
DR IntAct; P55789; 29.
DR MINT; P55789; -.
DR STRING; 9606.ENSP00000248114; -.
DR ChEMBL; CHEMBL1741189; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugCentral; P55789; -.
DR GlyGen; P55789; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55789; -.
DR MetOSite; P55789; -.
DR PhosphoSitePlus; P55789; -.
DR BioMuta; GFER; -.
DR DMDM; 218511915; -.
DR EPD; P55789; -.
DR jPOST; P55789; -.
DR MassIVE; P55789; -.
DR MaxQB; P55789; -.
DR PaxDb; P55789; -.
DR PeptideAtlas; P55789; -.
DR PRIDE; P55789; -.
DR ProteomicsDB; 56865; -. [P55789-1]
DR ProteomicsDB; 56866; -. [P55789-2]
DR Antibodypedia; 42516; 274 antibodies from 31 providers.
DR DNASU; 2671; -.
DR Ensembl; ENST00000248114.7; ENSP00000248114.6; ENSG00000127554.13. [P55789-1]
DR GeneID; 2671; -.
DR KEGG; hsa:2671; -.
DR MANE-Select; ENST00000248114.7; ENSP00000248114.6; NM_005262.3; NP_005253.3.
DR UCSC; uc002cob.4; human. [P55789-1]
DR CTD; 2671; -.
DR DisGeNET; 2671; -.
DR GeneCards; GFER; -.
DR HGNC; HGNC:4236; GFER.
DR HPA; ENSG00000127554; Low tissue specificity.
DR MalaCards; GFER; -.
DR MIM; 600924; gene.
DR MIM; 613076; phenotype.
DR neXtProt; NX_P55789; -.
DR OpenTargets; ENSG00000127554; -.
DR Orphanet; 330054; Congenital cataract-progressive muscular hypotonia-hearing loss-developmental delay syndrome.
DR PharmGKB; PA28648; -.
DR VEuPathDB; HostDB:ENSG00000127554; -.
DR eggNOG; KOG3355; Eukaryota.
DR GeneTree; ENSGT00390000001979; -.
DR HOGENOM; CLU_070631_1_1_1; -.
DR InParanoid; P55789; -.
DR OMA; KPCRSCT; -.
DR OrthoDB; 1537996at2759; -.
DR PhylomeDB; P55789; -.
DR TreeFam; TF105271; -.
DR BRENDA; 1.8.3.2; 2681.
DR PathwayCommons; P55789; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; P55789; -.
DR SIGNOR; P55789; -.
DR BioGRID-ORCS; 2671; 559 hits in 1102 CRISPR screens.
DR EvolutionaryTrace; P55789; -.
DR GeneWiki; GFER; -.
DR GenomeRNAi; 2671; -.
DR Pharos; P55789; Tchem.
DR PRO; PR:P55789; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P55789; protein.
DR Bgee; ENSG00000127554; Expressed in vena cava and 128 other tissues.
DR ExpressionAtlas; P55789; baseline and differential.
DR Genevisible; P55789; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA: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; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
DR DisProt; DP02875; -.
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 3D-structure; Alternative splicing; Cataract; Cytoplasm; Deafness;
KW Disease variant; Disulfide bond; FAD; Flavoprotein; Growth factor;
KW Mitochondrion; Oxidoreductase; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Secreted.
FT CHAIN 1..205
FT /note="FAD-linked sulfhydryl oxidase ALR"
FT /id="PRO_0000208548"
FT DOMAIN 95..195
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21383138"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21383138"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21383138"
FT BINDING 171..183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21383138"
FT BINDING 194..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21383138"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT DISULFID 95
FT /note="Interchain (with C-204)"
FT DISULFID 142..145
FT /note="Redox-active"
FT DISULFID 171..188
FT DISULFID 204
FT /note="Interchain (with C-95)"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.4"
FT /id="VSP_040393"
FT VARIANT 166
FT /note="F -> L (in dbSNP:rs36041021)"
FT /id="VAR_061994"
FT VARIANT 194
FT /note="R -> H (in MPMCD; less stable than the wild-type
FT protein within the mitochondria, increased rate of
FT dissociation of FAD by about 45-fold; dbSNP:rs121908192)"
FT /evidence="ECO:0000269|PubMed:19409522,
FT ECO:0000269|PubMed:20593814"
FT /id="VAR_063435"
FT CONFLICT 30
FT /note="L -> S (in Ref. 7; AAA96390)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="Q -> R (in Ref. 3; AAG38105)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="K -> E (in Ref. 3; AAG38105)"
FT /evidence="ECO:0000305"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3U5S"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3U5S"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:3U5S"
FT HELIX 123..139
FT /evidence="ECO:0007829|PDB:3U5S"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:3U5S"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:3U5S"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3U5S"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:3U5S"
SQ SEQUENCE 205 AA; 23449 MW; 43CBF8CCB5BA91C8 CRC64;
MAAPGERGRF HGGNLFFLPG GARSEMMDDL ATDARGRGAG RRDAAASAST PAQAPTSDSP
VAEDASRRRP CRACVDFKTW MRTQQKRDTK FREDCPPDRE ELGRHSWAVL HTLAAYYPDL
PTPEQQQDMA QFIHLFSKFY PCEECAEDLR KRLCRNHPDT RTRACFTQWL CHLHNEVNRK
LGKPDFDCSK VDERWRDGWK DGSCD
