ID DAOA_HUMAN Reviewed; 153 AA. AC P59103; A6NKG7; Q0VAE6; Q5VX59; Q86Y17; Q8IWM4; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 27-MAR-2024, entry version 146. DE RecName: Full=D-amino acid oxidase regulator; DE AltName: Full=Protein G72; GN Name=DAOA; Synonyms=G72; 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 / MRNA] (ISOFORM 1), VARIANT LYS-30, RP FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH DAO, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND INVOLVEMENT IN SCZD. RX PubMed=12364586; DOI=10.1073/pnas.182412499; RA Chumakov I., Blumenfeld M., Guerassimenko O., Cavarec L., Palicio M., RA Abderrahim H., Bougueleret L., Barry C., Tanaka H., La Rosa P., Puech A., RA Tahri N., Cohen-Akenine A., Delabrosse S., Lissarrague S., Picard F.-P., RA Maurice K., Essioux L., Millasseau P., Grel P., Debailleul V., Simon A.-M., RA Caterina D., Dufaure I., Malekzadeh K., Belova M., Luan J.-J., Bouillot M., RA Sambucy J.-L., Primas G., Saumier M., Boubkiri N., Martin-Saumier S., RA Nasroune M., Peixoto H., Delaye A., Pinchot V., Bastucci M., Guillou S., RA Chevillon M., Sainz-Fuertes R., Meguenni S., Aurich-Costa J., Cherif D., RA Gimalac A., Van Duijn C., Gauvreau D., Ouellette G., Fortier I., RA Raelson J., Sherbatich T., Riazanskay N., Rogaev E., Raeymaekers P., RA Aerssens J., Konings F., Luyten W., Macciardi F., Sham P.C., Straub R.E., RA Weinberger D.R., Cohen N., Cohen D.; RT "Genetic and physiological data implicating the new human gene G72 and the RT gene for D-amino acid oxidase in schizophrenia."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13675-13680(2002). RN [2] RP ERRATUM OF PUBMED:12364586. RX DOI=10.1073/pnas.262645899; RA Chumakov I., Blumenfeld M., Guerassimenko O., Cavarec L., Palicio M., RA Abderrahim H., Bougueleret L., Barry C., Tanaka H., La Rosa P., Puech A., RA Tahri N., Cohen-Akenine A., Delabrosse S., Lissarrague S., Picard F.-P., RA Maurice K., Essioux L., Millasseau P., Grel P., Debailleul V., Simon A.-M., RA Caterina D., Dufaure I., Malekzadeh K., Belova M., Luan J.-J., Bouillot M., RA Sambucy J.-L., Primas G., Saumier M., Boubkiri N., Martin-Saumier S., RA Nasroune M., Peixoto H., Delaye A., Pinchot V., Bastucci M., Guillou S., RA Chevillon M., Sainz-Fuertes R., Meguenni S., Aurich-Costa J., Cherif D., RA Gimalac A., Van Duijn C., Gauvreau D., Ouellette G., Fortier I., RA Raelson J., Sherbatich T., Riazanskay N., Rogaev E., Raeymaekers P., RA Aerssens J., Konings F., Luyten W., Macciardi F., Sham P.C., Straub R.E., RA Weinberger D.R., Cohen N., Cohen D.; RL Proc. Natl. Acad. Sci. U.S.A. 99:17221-17221(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Brain, and Testis; RX PubMed=12647258; DOI=10.1086/374822; RA Hattori E., Liu C., Badner J.A., Bonner T.I., Christian S.L., RA Maheshwari M., Detera-Wadleigh S.D., Gibbs R.A., Gershon E.S.; RT "Polymorphisms at the G72/G30 gene locus, on 13q33, are associated with RT bipolar disorder in two independent pedigree series."; RL Am. J. Hum. Genet. 72:1131-1140(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Amygdala; RA Cheng L., Gershon E.S., Liu C.; RT "Expression profile of G72 gene in human brain and G72 transgenic mice RT brain."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [8] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [9] RP FUNCTION, INTERACTION WITH DAO, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=18544534; DOI=10.1074/jbc.m709153200; RA Sacchi S., Bernasconi M., Martineau M., Mothet J.P., Ruzzene M., RA Pilone M.S., Pollegioni L., Molla G.; RT "pLG72 modulates intracellular D-serine levels through its interaction with RT D-amino acid oxidase: effect on schizophrenia susceptibility."; RL J. Biol. Chem. 283:22244-22256(2008). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17684499; DOI=10.1038/sj.mp.4002052; RA Kvajo M., Dhilla A., Swor D.E., Karayiorgou M., Gogos J.A.; RT "Evidence implicating the candidate schizophrenia/bipolar disorder RT susceptibility gene G72 in mitochondrial function."; RL Mol. Psychiatry 13:685-696(2008). RN [11] RP FUNCTION, AND INTERACTION WITH DAO. RX PubMed=20521334; DOI=10.1002/pro.429; RA Caldinelli L., Molla G., Bracci L., Lelli B., Pileri S., Cappelletti P., RA Sacchi S., Pollegioni L.; RT "Effect of ligand binding on human D-amino acid oxidase: implications for RT the development of new drugs for schizophrenia treatment."; RL Protein Sci. 19:1500-1512(2010). RN [12] RP FUNCTION, AND INTERACTION WITH DAO. RX PubMed=21679769; DOI=10.1016/j.mcn.2011.06.001; RA Sacchi S., Cappelletti P., Giovannardi S., Pollegioni L.; RT "Evidence for the interaction of D-amino acid oxidase with pLG72 in a glial RT cell line."; RL Mol. Cell. Neurosci. 48:20-28(2011). RN [13] RP FUNCTION, AND INTERACTION WITH DAO. RX PubMed=24362575; DOI=10.3390/ijms15010029; RA Chang S.L., Hsieh C.H., Chen Y.J., Wang C.M., Shih C.S., Huang P.W., RA Mir A., Lane H.Y., Tsai G.E., Chang H.T.; RT "The C-terminal region of G72 increases D-amino acid oxidase activity."; RL Int. J. Mol. Sci. 15:29-43(2013). RN [14] RP INTERACTION WITH MSRB2, AND SUBCELLULAR LOCATION. RX PubMed=25078755; DOI=10.1007/s10571-014-0087-0; RA Otte D.M., Rasko T., Wang M., Dreiseidler M., Drews E., Schrage H., RA Wojtalla A., Hoehfeld J., Wanker E., Zimmer A.; RT "Identification of the mitochondrial MSRB2 as a binding partner of LG72."; RL Cell. Mol. Neurobiol. 34:1123-1130(2014). RN [15] RP FUNCTION. RX PubMed=29114206; DOI=10.3389/fnmol.2017.00342; RA Jagannath V., Brotzakis Z.F., Parrinello M., Walitza S., Gruenblatt E.; RT "Controversial Effects of D-Amino Acid Oxidase Activator (DAOA)/G72 on D- RT Amino Acid Oxidase (DAO) Activity in Human Neuronal, Astrocyte and Kidney RT Cell Lines: The N-methyl D-aspartate (NMDA) Receptor Hypofunction Point of RT View."; RL Front. Mol. Neurosci. 10:342-342(2017). RN [16] RP FUNCTION, AND INTERACTION WITH SOD1. RX PubMed=30037290; DOI=10.1080/10715762.2018.1504293; RA Wang M., Saw H.P., Cui F.F., Lin S.Y., Chang H.T., Chiu C.D.; RT "pLG72 induces superoxide radicals via interaction and aggregation with RT SOD1."; RL Free Radic. Res. 52:970-976(2018). RN [17] RP FUNCTION, INTERACTION WITH DDO, AND MUTAGENESIS OF ARG-30. RX PubMed=37805834; DOI=10.1002/pro.4802; RA Rabattoni V., Motta Z., Miceli M., Molla G., Fissore A., Adinolfi S., RA Pollegioni L., Sacchi S.; RT "On the regulation of human D-aspartate oxidase."; RL Protein Sci. 32:e4802-e4802(2023). CC -!- FUNCTION: May suppress DAO (D-amino acid oxidase) and SOD1 activity and CC promote their degradation (PubMed:18544534, PubMed:20521334, CC PubMed:21679769, PubMed:30037290). Has conversely also been suggested CC to function as a DAO activator (PubMed:12364586, PubMed:24362575, CC PubMed:29114206). May stimulate the degradation of DDO (D-aspartate CC oxidase) (PubMed:37805834). May play a role in mitochondrial fission CC (PubMed:17684499). {ECO:0000269|PubMed:12364586, CC ECO:0000269|PubMed:17684499, ECO:0000269|PubMed:18544534, CC ECO:0000269|PubMed:20521334, ECO:0000269|PubMed:21679769, CC ECO:0000269|PubMed:24362575, ECO:0000269|PubMed:29114206, CC ECO:0000269|PubMed:30037290, ECO:0000269|PubMed:37805834}. CC -!- SUBUNIT: Interacts with DAO (D-amino acid oxidase); the interaction is CC direct, can occur in the presence or absence of FAD or substrate bound CC to DAO, and results in a complex containing two DAO homodimers and two CC DAOA monomers (PubMed:12364586, PubMed:18544534, PubMed:20521334, CC PubMed:21679769, PubMed:24362575). Interacts with DDO (D-aspartate CC oxidase); the interaction is direct (PubMed:37805834). Interacts wih CC SOD1; the interaction is direct (PubMed:30037290). Interacts with CC MSRB2; the interaction is direct (PubMed:25078755). CC {ECO:0000269|PubMed:12364586, ECO:0000269|PubMed:18544534, CC ECO:0000269|PubMed:20521334, ECO:0000269|PubMed:21679769, CC ECO:0000269|PubMed:24362575, ECO:0000269|PubMed:25078755, CC ECO:0000269|PubMed:30037290, ECO:0000269|PubMed:37805834}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18544534}. CC Golgi apparatus {ECO:0000269|PubMed:12364586, CC ECO:0000269|PubMed:18544534}. Mitochondrion CC {ECO:0000269|PubMed:17684499, ECO:0000269|PubMed:25078755}. Note=May CC transiently pass through the Golgi apparatus. CC {ECO:0000269|PubMed:18544534}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=LG72; CC IsoId=P59103-1; Sequence=Displayed; CC Name=2; Synonyms=SG72; CC IsoId=P59103-2; Sequence=VSP_004053, VSP_004054; CC Name=3; CC IsoId=P59103-3; Sequence=VSP_044292; CC Name=4; CC IsoId=P59103-4; Sequence=VSP_044293; CC -!- TISSUE SPECIFICITY: Expressed in the amygdala and in astrocytes of the CC cortex (at protein level) (PubMed:18544534, PubMed:17684499, CC PubMed:12364586). Expressed in the caudate nucleus, spinal cord and CC testis (PubMed:12364586). {ECO:0000269|PubMed:12364586, CC ECO:0000269|PubMed:17684499, ECO:0000269|PubMed:18544534}. CC -!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial CC psychotic disorder or group of disorders characterized by disturbances CC in the form and content of thought (e.g. delusions, hallucinations), in CC mood (e.g. inappropriate affect), in sense of self and relationship to CC the external world (e.g. loss of ego boundaries, withdrawal), and in CC behavior (e.g bizarre or apparently purposeless behavior). Although it CC affects emotions, it is distinguished from mood disorders in which such CC disturbances are primary. Similarly, there may be mild impairment of CC cognitive function, and it is distinguished from the dementias in which CC disturbed cognitive function is considered primary. Some patients CC manifest schizophrenic as well as bipolar disorder symptoms and are CC often given the diagnosis of schizoaffective disorder. CC {ECO:0000269|PubMed:12364586}. Note=Disease susceptibility may be CC associated with variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- CAUTION: PubMed:12364586, PubMed:24362575, and PubMed:29114206 show CC that DAOA activates DAO, however the results could not be reproduced by CC PubMed:18544534. Instead, PubMed:18544534 found that it acts as a CC repressor of DAO. Conversely, PubMed:17684499 reported that DAOA does CC not activate, interact, or colocalize with DAO, whereas PubMed:21679769 CC suggested that they may colocalize prior to the peroxisomal import of CC DAO. The mitochondrial activity is also disputed with PubMed:18544534 CC reporting its absence and PubMed:17684499 and PubMed:25078755 its CC presence in the mitochondrion. {ECO:0000269|PubMed:12364586, CC ECO:0000269|PubMed:17684499, ECO:0000269|PubMed:18544534, CC ECO:0000269|PubMed:21679769, ECO:0000269|PubMed:24362575, CC ECO:0000269|PubMed:25078755, ECO:0000269|PubMed:29114206}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014294; AAN16027.1; -; Genomic_DNA. DR EMBL; AE014294; AAN16028.1; -; Genomic_DNA. DR EMBL; AY138546; AAN08432.1; -; mRNA. DR EMBL; AY138547; AAN08433.1; -; mRNA. DR EMBL; AY170469; AAO12727.1; -; mRNA. DR EMBL; AY223901; AAO73604.1; -; mRNA. DR EMBL; DQ343761; ABC59904.1; -; mRNA. DR EMBL; DQ357223; ABC86111.1; -; mRNA. DR EMBL; AL359751; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471085; EAX09080.1; -; Genomic_DNA. DR EMBL; BC121091; AAI21092.1; -; mRNA. DR CCDS; CCDS41905.1; -. [P59103-1] DR CCDS; CCDS53880.1; -. [P59103-3] DR CCDS; CCDS91834.1; -. [P59103-4] DR RefSeq; NP_001155284.1; NM_001161812.1. DR RefSeq; NP_001155286.1; NM_001161814.1. [P59103-3] DR RefSeq; NP_758958.3; NM_172370.4. [P59103-1] DR RefSeq; XP_005254099.1; XM_005254042.1. DR AlphaFoldDB; P59103; -. DR BioGRID; 129363; 5. DR IntAct; P59103; 1. DR MINT; P59103; -. DR STRING; 9606.ENSP00000483757; -. DR BioMuta; DAOA; -. DR DMDM; 84028201; -. DR PaxDb; 9606-ENSP00000483757; -. DR Antibodypedia; 54191; 96 antibodies from 16 providers. DR DNASU; 267012; -. DR Ensembl; ENST00000329625.9; ENSP00000329951.5; ENSG00000182346.22. [P59103-3] DR Ensembl; ENST00000375936.9; ENSP00000365103.3; ENSG00000182346.22. [P59103-1] DR Ensembl; ENST00000473269.5; ENSP00000470244.1; ENSG00000182346.22. [P59103-4] DR Ensembl; ENST00000559369.5; ENSP00000453831.1; ENSG00000182346.22. [P59103-3] DR Ensembl; ENST00000600388.5; ENSP00000472260.1; ENSG00000182346.22. [P59103-3] DR Ensembl; ENST00000618629.1; ENSP00000483757.1; ENSG00000182346.22. [P59103-1] DR GeneID; 267012; -. DR KEGG; hsa:267012; -. DR MANE-Select; ENST00000375936.9; ENSP00000365103.3; NM_172370.5; NP_758958.3. DR UCSC; uc001vqb.5; human. [P59103-1] DR AGR; HGNC:21191; -. DR CTD; 267012; -. DR DisGeNET; 267012; -. DR GeneCards; DAOA; -. DR HGNC; HGNC:21191; DAOA. DR HPA; ENSG00000182346; Not detected. DR MalaCards; DAOA; -. DR MIM; 181500; phenotype. DR MIM; 607408; gene. DR neXtProt; NX_P59103; -. DR OpenTargets; ENSG00000182346; -. DR PharmGKB; PA134924986; -. DR VEuPathDB; HostDB:ENSG00000182346; -. DR eggNOG; ENOG502T4XP; Eukaryota. DR GeneTree; ENSGT00410000028557; -. DR HOGENOM; CLU_2557651_0_0_1; -. DR InParanoid; P59103; -. DR OMA; QASKDCR; -. DR OrthoDB; 4700083at2759; -. DR PhylomeDB; P59103; -. DR TreeFam; TF354179; -. DR PathwayCommons; P59103; -. DR SignaLink; P59103; -. DR BioGRID-ORCS; 267012; 14 hits in 1142 CRISPR screens. DR GenomeRNAi; 267012; -. DR Pharos; P59103; Tbio. DR PRO; PR:P59103; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P59103; Protein. DR Bgee; ENSG00000182346; Expressed in ganglionic eminence. DR ExpressionAtlas; P59103; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0046416; P:D-amino acid metabolic process; IDA:UniProtKB. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB. DR InterPro; IPR027929; DAOA. DR Pfam; PF15199; DAOA; 1. DR Genevisible; P59103; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Golgi apparatus; Mitochondrion; KW Reference proteome; Schizophrenia. FT CHAIN 1..153 FT /note="D-amino acid oxidase regulator" FT /id="PRO_0000079781" FT REGION 1..25 FT /note="Involved in targeting to the mitochondrion" FT /evidence="ECO:0000269|PubMed:17684499" FT REGION 138..153 FT /note="Interaction with DAO" FT /evidence="ECO:0000269|PubMed:24362575" FT VAR_SEQ 1..71 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12647258, ECO:0000303|Ref.4" FT /id="VSP_044292" FT VAR_SEQ 16 FT /note="S -> V (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_004053" FT VAR_SEQ 17..153 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_004054" FT VAR_SEQ 95..153 FT /note="LEEVSSHVGKVFMARNYEFLAYEASKDRRQPLERMWTCNYNQQKDQSCNHKE FT ITSTKAE -> HSKVILNGNLHCHFKRISQIFAGHFMEGDTEA (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12647258" FT /id="VSP_044293" FT VARIANT 30 FT /note="R -> K (in dbSNP:rs2391191)" FT /evidence="ECO:0000269|PubMed:12364586" FT /id="VAR_014313" FT VARIANT 62 FT /note="K -> E (in dbSNP:rs9558562)" FT /id="VAR_050943" FT MUTAGEN 30 FT /note="R->K: Does not affect interaction with DDO." FT /evidence="ECO:0000269|PubMed:37805834" SQ SEQUENCE 153 AA; 18108 MW; 597E2DE432A48EAE CRC64; MLEKLMGADS LQLFRSRYTL GKIYFIGFQR SILLSKSENS LNSIAKETEE GRETVTRKEG WKRRHEDGYL EMAQRHLQRS LCPWVSYLPQ PYAELEEVSS HVGKVFMARN YEFLAYEASK DRRQPLERMW TCNYNQQKDQ SCNHKEITST KAE //