ID ADRO_HUMAN Reviewed; 491 AA. AC P22570; B4DDI7; B4DHX5; B4DQQ4; B4DX24; B7Z7G2; E7EQC1; Q13716; Q4PJI0; AC Q9BU12; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 3. DT 27-MAR-2024, entry version 218. DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial; DE Short=AR; DE Short=Adrenodoxin reductase {ECO:0000303|PubMed:2845396}; DE EC=1.18.1.6 {ECO:0000250|UniProtKB:P08165}; DE AltName: Full=Ferredoxin--NADP(+) reductase; DE Short=Ferredoxin reductase; DE Flags: Precursor; GN Name=FDXR {ECO:0000312|HGNC:HGNC:3642}; Synonyms=ADXR; 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 [MRNA] (ISOFORMS SHORT AND LONG), AND VARIANT GLN-123. RX PubMed=2845396; DOI=10.1073/pnas.85.19.7104; RA Solish S.B., Picado-Leonard J., Morel Y., Kuhn R.W., Mohandas T.K., RA Hanukoglu I., Miller W.L.; RT "Human adrenodoxin reductase: two mRNAs encoded by a single gene on RT chromosome 17cen-->q25 are expressed in steroidogenic tissues."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7104-7108(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2236061; DOI=10.1073/pnas.87.21.8516; RA Lin D., Shi Y., Miller W.L.; RT "Cloning and sequence of the human adrenodoxin reductase gene."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8516-8520(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-7; GLN-123; VAL-213; RP LEU-248; TRP-251; CYS-301; MET-345; SER-352 AND ALA-472. RG NIEHS SNPs program; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), AND RP VARIANT GLN-123. RC TISSUE=Adrenal gland, Caudate nucleus, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RC TISSUE=Lung; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-317, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [11] RP INVOLVEMENT IN ANOA, AND VARIANTS ANOA VAL-215; TRP-242; CYS-306; SER-327 RP AND 419-GLN--HIS-491 DEL. RX PubMed=28965846; DOI=10.1016/j.ajhg.2017.09.007; RA Paul A., Drecourt A., Petit F., Deguine D.D., Vasnier C., Oufadem M., RA Masson C., Bonnet C., Masmoudi S., Mosnier I., Mahieu L., Bouccara D., RA Kaplan J., Challe G., Domange C., Mochel F., Sterkers O., Gerber S., RA Nitschke P., Bole-Feysot C., Jonard L., Gherbi S., Mercati O., RA Ben Aissa I., Lyonnet S., Roetig A., Delahodde A., Marlin S.; RT "FDXR Mutations Cause Sensorial Neuropathies and Expand the Spectrum of RT Mitochondrial Fe-S-Synthesis Diseases."; RL Am. J. Hum. Genet. 101:630-637(2017). CC -!- FUNCTION: Serves as the first electron transfer protein in all the CC mitochondrial P450 systems including cholesterol side chain cleavage in CC all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal CC cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C- CC 27 hydroxylation in the liver. {ECO:0000250|UniProtKB:P08165}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized CC [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA- CC COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6; CC Evidence={ECO:0000250|UniProtKB:P08165}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P08165}; CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism. CC {ECO:0000250|UniProtKB:P08165}. CC -!- SUBUNIT: Monomer. Interacts directly with FDX1. CC {ECO:0000250|UniProtKB:P08165}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=Short; CC IsoId=P22570-1; Sequence=Displayed; CC Name=Long; CC IsoId=P22570-2; Sequence=VSP_003416; CC Name=3; CC IsoId=P22570-3; Sequence=VSP_045135; CC Name=4; CC IsoId=P22570-4; Sequence=VSP_046669; CC Name=5; CC IsoId=P22570-5; Sequence=VSP_046673; CC Name=6; CC IsoId=P22570-6; Sequence=VSP_046671, VSP_046672; CC Name=7; CC IsoId=P22570-7; Sequence=VSP_046670; CC -!- DISEASE: Auditory neuropathy and optic atrophy (ANOA) [MIM:617717]: An CC autosomal recessive disease characterized by hearing loss, visual CC impairment and optic atrophy, with onset in the first or second decades CC of life. Optic atrophy is caused by degeneration of nerve fibers which CC arise in the retina and converge to form the optic disk, optic nerve, CC optic chiasm and optic tracts. {ECO:0000269|PubMed:28965846}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform Long]: Represents 10-20% of all adrenodoxin CC reductase mRNAs and seems to be inactive. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/fdxr/"; 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; J03826; AAB59498.1; -; mRNA. DR EMBL; J03826; AAB59497.1; -; mRNA. DR EMBL; M58509; AAA51668.1; -; Genomic_DNA. DR EMBL; M58508; AAA51668.1; JOINED; Genomic_DNA. DR EMBL; M58509; AAA51669.1; -; Genomic_DNA. DR EMBL; M58508; AAA51669.1; JOINED; Genomic_DNA. DR EMBL; DQ085780; AAY68215.1; -; Genomic_DNA. DR EMBL; AK293208; BAG56748.1; -; mRNA. DR EMBL; AK295307; BAG58287.1; -; mRNA. DR EMBL; AK298908; BAG61016.1; -; mRNA. DR EMBL; AK301779; BAG63236.1; -; mRNA. DR EMBL; AK301977; BAH13598.1; -; mRNA. DR EMBL; AC068874; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002960; AAH02960.1; -; mRNA. DR CCDS; CCDS11707.1; -. [P22570-2] DR CCDS; CCDS58591.1; -. [P22570-4] DR CCDS; CCDS58592.1; -. [P22570-5] DR CCDS; CCDS58593.1; -. [P22570-1] DR CCDS; CCDS58594.1; -. [P22570-6] DR CCDS; CCDS58595.1; -. [P22570-3] DR CCDS; CCDS58596.1; -. [P22570-7] DR PIR; A40487; A40487. DR RefSeq; NP_001244941.2; NM_001258012.3. DR RefSeq; NP_001244942.2; NM_001258013.3. DR RefSeq; NP_001244943.2; NM_001258014.3. DR RefSeq; NP_001244944.1; NM_001258015.2. [P22570-6] DR RefSeq; NP_001244945.2; NM_001258016.3. DR RefSeq; NP_004101.3; NM_004110.5. DR RefSeq; NP_077728.3; NM_024417.4. DR AlphaFoldDB; P22570; -. DR SMR; P22570; -. DR BioGRID; 108523; 72. DR IntAct; P22570; 22. DR STRING; 9606.ENSP00000416515; -. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate. DR GlyGen; P22570; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P22570; -. DR PhosphoSitePlus; P22570; -. DR SwissPalm; P22570; -. DR BioMuta; FDXR; -. DR DMDM; 85681283; -. DR REPRODUCTION-2DPAGE; IPI00026958; -. DR EPD; P22570; -. DR jPOST; P22570; -. DR MassIVE; P22570; -. DR MaxQB; P22570; -. DR PaxDb; 9606-ENSP00000416515; -. DR PeptideAtlas; P22570; -. DR ProteomicsDB; 17542; -. DR ProteomicsDB; 4256; -. DR ProteomicsDB; 4894; -. DR ProteomicsDB; 54003; -. [P22570-1] DR ProteomicsDB; 54004; -. [P22570-2] DR ProteomicsDB; 6867; -. DR Pumba; P22570; -. DR Antibodypedia; 3261; 330 antibodies from 29 providers. DR DNASU; 2232; -. DR Ensembl; ENST00000420580.6; ENSP00000414172.2; ENSG00000161513.12. [P22570-6] DR GeneID; 2232; -. DR KEGG; hsa:2232; -. DR UCSC; uc002jlx.4; human. [P22570-1] DR AGR; HGNC:3642; -. DR CTD; 2232; -. DR DisGeNET; 2232; -. DR GeneCards; FDXR; -. DR HGNC; HGNC:3642; FDXR. DR HPA; ENSG00000161513; Tissue enriched (adrenal). DR MalaCards; FDXR; -. DR MIM; 103270; gene. DR MIM; 617717; phenotype. DR neXtProt; NX_P22570; -. DR OpenTargets; ENSG00000161513; -. DR Orphanet; 542585; Auditory neuropathy-optic atrophy syndrome. DR Orphanet; 543470; Optic atrophy-ataxia-peripheral neuropathy-global developmental delay syndrome. DR PharmGKB; PA28086; -. DR VEuPathDB; HostDB:ENSG00000161513; -. DR eggNOG; KOG1800; Eukaryota. DR GeneTree; ENSGT00390000013574; -. DR HOGENOM; CLU_024722_3_1_1; -. DR InParanoid; P22570; -. DR OrthoDB; 5764at2759; -. DR PhylomeDB; P22570; -. DR TreeFam; TF314193; -. DR BioCyc; MetaCyc:HS08587-MONOMER; -. DR PathwayCommons; P22570; -. DR Reactome; R-HSA-196108; Pregnenolone biosynthesis. DR Reactome; R-HSA-211976; Endogenous sterols. DR Reactome; R-HSA-2395516; Electron transport from NADPH to Ferredoxin. DR Reactome; R-HSA-5579026; Defective CYP11A1 causes AICSR. DR SignaLink; P22570; -. DR UniPathway; UPA00296; -. DR BioGRID-ORCS; 2232; 485 hits in 1175 CRISPR screens. DR GeneWiki; Adrenodoxin_reductase; -. DR GenomeRNAi; 2232; -. DR Pharos; P22570; Tbio. DR PRO; PR:P22570; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P22570; Protein. DR Bgee; ENSG00000161513; Expressed in right adrenal gland cortex and 128 other cell types or tissues. DR ExpressionAtlas; P22570; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; TAS:ProtInc. DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IBA:GO_Central. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc. DR GO; GO:0006694; P:steroid biosynthetic process; TAS:ProtInc. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR021163; Ferredox_Rdtase_adrenod. DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1. DR PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PIRSF; PIRSF000362; FNR; 1. DR PRINTS; PR00419; ADXRDTASE. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF51971; Nucleotide-binding domain; 2. DR Genevisible; P22570; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cholesterol metabolism; Deafness; Disease variant; KW Electron transport; FAD; Flavoprotein; Lipid metabolism; Membrane; KW Mitochondrion; Mitochondrion inner membrane; NADP; Neuropathy; KW Oxidoreductase; Phosphoprotein; Reference proteome; Steroid metabolism; KW Sterol metabolism; Transit peptide; Transport. FT TRANSIT 1..32 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:P08165" FT CHAIN 33..491 FT /note="NADPH:adrenodoxin oxidoreductase, mitochondrial" FT /id="PRO_0000019420" FT BINDING 49 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 69 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 77 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 113 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 184..187 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 228..229 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 240 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 398 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 405..407 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P08165" FT BINDING 405 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P08165" FT MOD_RES 310 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 317 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..59 FT /note="MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFY FT TAQHLLK -> MEDKDRE (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046669" FT VAR_SEQ 27..34 FT /note="SFCHHFST -> TFGGSDEVRDPANAKALRNKRRRMQVRVKLGKFQLLLDI FT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046670" FT VAR_SEQ 59 FT /note="K -> KRVEALCSQPRVLNSPALSGEGEDLGASQPLSLDPTSCHPVPQQ FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045135" FT VAR_SEQ 59 FT /note="K -> KQ (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046671" FT VAR_SEQ 91..131 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046672" FT VAR_SEQ 91..98 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046673" FT VAR_SEQ 203 FT /note="E -> EALLLCQ (in isoform Long)" FT /evidence="ECO:0000303|PubMed:2845396" FT /id="VSP_003416" FT VARIANT 7 FT /note="R -> L (in dbSNP:rs28365947)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025192" FT VARIANT 123 FT /note="R -> Q (in dbSNP:rs690514)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:2845396, ECO:0000269|Ref.3" FT /id="VAR_004624" FT VARIANT 213 FT /note="G -> V (in dbSNP:rs35692345)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025193" FT VARIANT 215 FT /note="L -> V (in ANOA)" FT /evidence="ECO:0000269|PubMed:28965846" FT /id="VAR_080376" FT VARIANT 242 FT /note="R -> W (in ANOA)" FT /evidence="ECO:0000269|PubMed:28965846" FT /id="VAR_080377" FT VARIANT 248 FT /note="P -> L (in dbSNP:rs35072974)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025194" FT VARIANT 251 FT /note="R -> W (in dbSNP:rs34038065)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025195" FT VARIANT 301 FT /note="R -> C (in dbSNP:rs34118765)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025196" FT VARIANT 306 FT /note="R -> C (in ANOA)" FT /evidence="ECO:0000269|PubMed:28965846" FT /id="VAR_080378" FT VARIANT 327 FT /note="R -> S (in ANOA)" FT /evidence="ECO:0000269|PubMed:28965846" FT /id="VAR_080379" FT VARIANT 345 FT /note="T -> M (in dbSNP:rs35660143)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025197" FT VARIANT 352 FT /note="P -> S (in dbSNP:rs35696549)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025198" FT VARIANT 419..491 FT /note="Missing (in ANOA)" FT /evidence="ECO:0000269|PubMed:28965846" FT /id="VAR_080380" FT VARIANT 472 FT /note="T -> A (in dbSNP:rs35769464)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025199" FT CONFLICT 223 FT /note="V -> G (in Ref. 4; BAG56748)" FT /evidence="ECO:0000305" SQ SEQUENCE 491 AA; 53837 MW; 15D07E714F592C9D CRC64; MASRCWRWWG WSAWPRTRLP PAGSTPSFCH HFSTQEKTPQ ICVVGSGPAG FYTAQHLLKH PQAHVDIYEK QPVPFGLVRF GVAPDHPEVK NVINTFTQTA HSGRCAFWGN VEVGRDVTVP ELREAYHAVV LSYGAEDHRA LEIPGEELPG VCSARAFVGW YNGLPENQEL EPDLSCDTAV ILGQGNVALD VARILLTPPE HLERTDITKA ALGVLRQSRV KTVWLVGRRG PLQVAFTIKE LREMIQLPGA RPILDPVDFL GLQDKIKEVP RPRKRLTELL LRTATEKPGP AEAARQASAS RAWGLRFFRS PQQVLPSPDG RRAAGVRLAV TRLEGVDEAT RAVPTGDMED LPCGLVLSSI GYKSRPVDPS VPFDSKLGVI PNVEGRVMDV PGLYCSGWVK RGPTGVIATT MTDSFLTGQM LLQDLKAGLL PSGPRPGYAA IQALLSSRGV RPVSFSDWEK LDAEEVARGQ GTGKPREKLV DPQEMLRLLG H //