ADRO_HUMAN
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 03-AUG-2022, entry version 209.
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/";
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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; 57.
DR IntAct; P22570; 21.
DR STRING; 9606.ENSP00000416515; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR iPTMnet; P22570; -.
DR PhosphoSitePlus; 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; P22570; -.
DR PeptideAtlas; P22570; -.
DR PRIDE; P22570; -.
DR ProteomicsDB; 17542; -.
DR ProteomicsDB; 4256; -.
DR ProteomicsDB; 4894; -.
DR ProteomicsDB; 54003; -. [P22570-1]
DR ProteomicsDB; 54004; -. [P22570-2]
DR ProteomicsDB; 6867; -.
DR Antibodypedia; 3261; 288 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 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; 1324510at2759; -.
DR PhylomeDB; P22570; -.
DR TreeFam; TF314193; -.
DR BioCyc; MetaCyc:HS08587-MON; -.
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; 452 hits in 1093 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 126 other tissues.
DR ExpressionAtlas; P22570; baseline and differential.
DR Genevisible; P22570; HS.
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:0016491; F:oxidoreductase 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; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
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
