COQ8B_HUMAN
ID COQ8B_HUMAN Reviewed; 544 AA.
AC Q96D53; Q8TAJ1; Q9HA52;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Atypical kinase COQ8B, mitochondrial {ECO:0000305};
DE EC=2.7.-.- {ECO:0000250|UniProtKB:Q8NI60};
DE AltName: Full=AarF domain-containing protein kinase 4 {ECO:0000312|HGNC:HGNC:19041};
DE AltName: Full=Coenzyme Q protein 8B {ECO:0000305};
GN Name=COQ8B {ECO:0000312|HGNC:HGNC:19041};
GN Synonyms=ADCK4 {ECO:0000312|HGNC:HGNC:19041};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-166 (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [3]
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 [4]
RP SUBUNIT.
RX PubMed=25216398; DOI=10.1021/ja505017f;
RA Khadria A.S., Mueller B.K., Stefely J.A., Tan C.H., Pagliarini D.J.,
RA Senes A.;
RT "A Gly-zipper motif mediates homodimerization of the transmembrane domain
RT of the mitochondrial kinase ADCK3.";
RL J. Am. Chem. Soc. 136:14068-14077(2014).
RN [5]
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 [6]
RP INTERACTION WITH THE COQ ENZYME COMPLEX.
RX PubMed=27499296; DOI=10.1016/j.molcel.2016.06.033;
RA Floyd B.J., Wilkerson E.M., Veling M.T., Minogue C.E., Xia C., Beebe E.T.,
RA Wrobel R.L., Cho H., Kremer L.S., Alston C.L., Gromek K.A., Dolan B.K.,
RA Ulbrich A., Stefely J.A., Bohl S.L., Werner K.M., Jochem A.,
RA Westphall M.S., Rensvold J.W., Taylor R.W., Prokisch H., Kim J.J.,
RA Coon J.J., Pagliarini D.J.;
RT "Mitochondrial protein interaction mapping identifies regulators of
RT respiratory chain function.";
RL Mol. Cell 63:621-632(2016).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-78; ARG-174; MET-318; ARG-352 AND
RP MET-462.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [8]
RP VARIANTS NPHS9 TRP-178; GLY-286; TRP-320; TRP-343 AND GLN-477, FUNCTION,
RP INTERACTION WITH COQ6 AND COQ7, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24270420; DOI=10.1172/jci69000;
RA Ashraf S., Gee H.Y., Woerner S., Xie L.X., Vega-Warner V., Lovric S.,
RA Fang H., Song X., Cattran D.C., Avila-Casado C., Paterson A.D.,
RA Nitschke P., Bole-Feysot C., Cochat P., Esteve-Rudd J., Haberberger B.,
RA Allen S.J., Zhou W., Airik R., Otto E.A., Barua M., Al-Hamed M.H.,
RA Kari J.A., Evans J., Bierzynska A., Saleem M.A., Bockenhauer D., Kleta R.,
RA El Desoky S., Hacihamdioglu D.O., Gok F., Washburn J., Wiggins R.C.,
RA Choi M., Lifton R.P., Levy S., Han Z., Salviati L., Prokisch H.,
RA Williams D.S., Pollak M., Clarke C.F., Pei Y., Antignac C., Hildebrandt F.;
RT "ADCK4 mutations promote steroid-resistant nephrotic syndrome through CoQ10
RT biosynthesis disruption.";
RL J. Clin. Invest. 123:5179-5189(2013).
RN [9]
RP VARIANTS NPHS9 ARG-98; TRP-178; LEU-310 AND GLU-498.
RX PubMed=25967120; DOI=10.1681/asn.2014121240;
RG PodoNet Consortium;
RA Korkmaz E., Lipska-Zietkiewicz B.S., Boyer O., Gribouval O., Fourrage C.,
RA Tabatabaei M., Schnaidt S., Gucer S., Kaymaz F., Arici M., Dinckan A.,
RA Mir S., Bayazit A.K., Emre S., Balat A., Rees L., Shroff R., Bergmann C.,
RA Mourani C., Antignac C., Ozaltin F., Schaefer F.;
RT "ADCK4-associated glomerulopathy causes adolescence-onset FSGS.";
RL J. Am. Soc. Nephrol. 27:63-68(2016).
CC -!- FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q,
CC also named ubiquinone, an essential lipid-soluble electron transporter
CC for aerobic cellular respiration (PubMed:24270420). Its substrate
CC specificity is unclear: does not show any protein kinase activity.
CC Probably acts as a small molecule kinase, possibly a lipid kinase that
CC phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway.
CC Required for podocyte migration (PubMed:24270420).
CC {ECO:0000250|UniProtKB:Q8NI60, ECO:0000269|PubMed:24270420}.
CC -!- ACTIVITY REGULATION: Autoinhibited by the N-terminal domain, containing
CC the KxGQ motif, that completely occludes the typical substrate binding
CC pocket. Nucleotide-binding relieves inhibition.
CC {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- SUBUNIT: Homodimer; homodimerizes via its transmembrane region
CC (PubMed:25216398). Interacts with COQ6 and COQ7 (PubMed:24270420).
CC Interacts with the multi-subunit COQ enzyme complex, composed of at
CC least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 (PubMed:27499296).
CC {ECO:0000269|PubMed:24270420, ECO:0000269|PubMed:25216398,
CC ECO:0000269|PubMed:27499296}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:24270420}; Single-pass membrane protein
CC {ECO:0000269|PubMed:24270420}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:24270420}. Cell membrane
CC {ECO:0000269|PubMed:24270420}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96D53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96D53-2; Sequence=VSP_022357;
CC -!- TISSUE SPECIFICITY: Widely expressed, including renal podocytes.
CC {ECO:0000269|PubMed:24270420}.
CC -!- DOMAIN: Adopts an atypical protein kinase-like fold: while it adopts a
CC core fold similar to that of well-characterized protein kinase-like
CC domains. The KxGQ motif completely occludes the typical substrate
CC binding pocket. Nucleotide-binding opens the substrate binding pocket
CC and flips the active site from inside the hydrophobic core into a
CC catalytically competent, solvent-exposed posture.
CC {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- DISEASE: Nephrotic syndrome 9 (NPHS9) [MIM:615573]: A form of nephrotic
CC syndrome, a renal disease clinically characterized by progressive renal
CC failure, severe proteinuria, hypoalbuminemia, hyperlipidemia and edema.
CC Kidney biopsies show focal segmental glomerulosclerosis.
CC {ECO:0000269|PubMed:24270420, ECO:0000269|PubMed:25967120}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; BC013114; AAH13114.2; -; mRNA.
DR EMBL; BC027473; AAH27473.1; -; mRNA.
DR EMBL; AK022291; BAB14004.1; -; mRNA.
DR CCDS; CCDS12562.1; -. [Q96D53-1]
DR CCDS; CCDS46081.1; -. [Q96D53-2]
DR RefSeq; NP_001136027.1; NM_001142555.2. [Q96D53-2]
DR RefSeq; NP_079152.3; NM_024876.3. [Q96D53-1]
DR AlphaFoldDB; Q96D53; -.
DR SMR; Q96D53; -.
DR BioGRID; 123009; 130.
DR IntAct; Q96D53; 64.
DR MINT; Q96D53; -.
DR STRING; 9606.ENSP00000315118; -.
DR BindingDB; Q96D53; -.
DR ChEMBL; CHEMBL5753; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q96D53; -.
DR iPTMnet; Q96D53; -.
DR PhosphoSitePlus; Q96D53; -.
DR BioMuta; COQ8B; -.
DR DMDM; 74731415; -.
DR EPD; Q96D53; -.
DR jPOST; Q96D53; -.
DR MassIVE; Q96D53; -.
DR MaxQB; Q96D53; -.
DR PaxDb; Q96D53; -.
DR PeptideAtlas; Q96D53; -.
DR PRIDE; Q96D53; -.
DR ProteomicsDB; 76252; -. [Q96D53-1]
DR ProteomicsDB; 76253; -. [Q96D53-2]
DR Antibodypedia; 30619; 239 antibodies from 29 providers.
DR DNASU; 79934; -.
DR Ensembl; ENST00000243583.10; ENSP00000243583.5; ENSG00000123815.13. [Q96D53-2]
DR Ensembl; ENST00000324464.8; ENSP00000315118.3; ENSG00000123815.13. [Q96D53-1]
DR Ensembl; ENST00000594720.6; ENSP00000470876.2; ENSG00000123815.13. [Q96D53-1]
DR Ensembl; ENST00000601967.6; ENSP00000470916.2; ENSG00000123815.13. [Q96D53-1]
DR Ensembl; ENST00000677018.1; ENSP00000503480.1; ENSG00000123815.13. [Q96D53-1]
DR Ensembl; ENST00000678404.1; ENSP00000503944.1; ENSG00000123815.13. [Q96D53-1]
DR Ensembl; ENST00000678419.1; ENSP00000504085.1; ENSG00000123815.13. [Q96D53-1]
DR Ensembl; ENST00000678467.1; ENSP00000504072.1; ENSG00000123815.13. [Q96D53-1]
DR Ensembl; ENST00000679130.1; ENSP00000504845.1; ENSG00000123815.13. [Q96D53-1]
DR GeneID; 79934; -.
DR KEGG; hsa:79934; -.
DR MANE-Select; ENST00000324464.8; ENSP00000315118.3; NM_024876.4; NP_079152.3.
DR UCSC; uc002ooq.3; human. [Q96D53-1]
DR CTD; 79934; -.
DR DisGeNET; 79934; -.
DR GeneCards; COQ8B; -.
DR GeneReviews; COQ8B; -.
DR HGNC; HGNC:19041; COQ8B.
DR HPA; ENSG00000123815; Low tissue specificity.
DR MalaCards; COQ8B; -.
DR MIM; 615567; gene.
DR MIM; 615573; phenotype.
DR neXtProt; NX_Q96D53; -.
DR OpenTargets; ENSG00000123815; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA134988974; -.
DR VEuPathDB; HostDB:ENSG00000123815; -.
DR eggNOG; KOG1234; Eukaryota.
DR GeneTree; ENSGT00940000158965; -.
DR HOGENOM; CLU_006533_9_0_1; -.
DR InParanoid; Q96D53; -.
DR OMA; KFHQDGP; -.
DR OrthoDB; 525494at2759; -.
DR PhylomeDB; Q96D53; -.
DR TreeFam; TF300630; -.
DR BioCyc; MetaCyc:ENSG00000123815-MON; -.
DR PathwayCommons; Q96D53; -.
DR SignaLink; Q96D53; -.
DR BioGRID-ORCS; 79934; 18 hits in 1110 CRISPR screens.
DR ChiTaRS; COQ8B; human.
DR GenomeRNAi; 79934; -.
DR Pharos; Q96D53; Tchem.
DR PRO; PR:Q96D53; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96D53; protein.
DR Bgee; ENSG00000123815; Expressed in right uterine tube and 151 other tissues.
DR ExpressionAtlas; Q96D53; baseline and differential.
DR Genevisible; Q96D53; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:FlyBase.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; ISS:FlyBase.
DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:UniProtKB.
DR CDD; cd13970; ABC1_ADCK3; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR034646; ADCK3_dom.
DR InterPro; IPR034638; COQ8B.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR43851:SF4; PTHR43851:SF4; 1.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm;
KW Disease variant; Kinase; Membrane; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..544
FT /note="Atypical kinase COQ8B, mitochondrial"
FT /id="PRO_0000271797"
FT TRANSMEM 92..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 191..423
FT /note="Protein kinase"
FT REGION 45..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..158
FT /note="KxGQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MOTIF 216..219
FT /note="AAAS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT COMPBIAS 51..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 324..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT VAR_SEQ 123..163
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022357"
FT VARIANT 78
FT /note="R -> C (in dbSNP:rs11538384)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041420"
FT VARIANT 98
FT /note="L -> R (in NPHS9)"
FT /evidence="ECO:0000269|PubMed:25967120"
FT /id="VAR_076861"
FT VARIANT 174
FT /note="H -> R (in dbSNP:rs3865452)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_029995"
FT VARIANT 178
FT /note="R -> W (in NPHS9; dbSNP:rs398122978)"
FT /evidence="ECO:0000269|PubMed:24270420,
FT ECO:0000269|PubMed:25967120"
FT /id="VAR_070552"
FT VARIANT 286
FT /note="D -> G (in NPHS9; dbSNP:rs398122979)"
FT /evidence="ECO:0000269|PubMed:24270420"
FT /id="VAR_070553"
FT VARIANT 310
FT /note="P -> L (in NPHS9)"
FT /evidence="ECO:0000269|PubMed:25967120"
FT /id="VAR_076862"
FT VARIANT 318
FT /note="T -> M (in dbSNP:rs55899516)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041421"
FT VARIANT 320
FT /note="R -> W (in NPHS9; dbSNP:rs369573693)"
FT /evidence="ECO:0000269|PubMed:24270420"
FT /id="VAR_070554"
FT VARIANT 343
FT /note="R -> W (in NPHS9; dbSNP:rs398122981)"
FT /evidence="ECO:0000269|PubMed:24270420"
FT /id="VAR_070555"
FT VARIANT 352
FT /note="T -> R (in dbSNP:rs36012476)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041422"
FT VARIANT 462
FT /note="T -> M (in dbSNP:rs56083906)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041423"
FT VARIANT 477
FT /note="R -> Q (in NPHS9; dbSNP:rs1057519347)"
FT /evidence="ECO:0000269|PubMed:24270420"
FT /id="VAR_070556"
FT VARIANT 498
FT /note="A -> E (in NPHS9)"
FT /evidence="ECO:0000269|PubMed:25967120"
FT /id="VAR_076863"
FT CONFLICT 164..166
FT /note="DNS -> GTA (in Ref. 2; BAB14004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 60069 MW; 4645DF579B9DFA4B CRC64;
MWLKVGGLLR GTGGQLGQTV GWPCGALGPG PHRWGPCGGS WAQKFYQDGP GRGLGEEDIR
RAREARPRKT PRPQLSDRSR ERKVPASRIS RLANFGGLAV GLGLGVLAEM AKKSMPGGRL
QSEGGSGLDS SPFLSEANAE RIVQTLCTVR GAALKVGQML SIQDNSFISP QLQHIFERVR
QSADFMPRWQ MLRVLEEELG RDWQAKVASL EEVPFAAASI GQVHQGLLRD GTEVAVKIQY
PGIAQSIQSD VQNLLAVLKM SAALPAGLFA EQSLQALQQE LAWECDYRRE AACAQNFRQL
LANDPFFRVP AVVKELCTTR VLGMELAGGV PLDQCQGLSQ DLRNQICFQL LTLCLRELFE
FRFMQTDPNW ANFLYDASSH QVTLLDFGAS REFGTEFTDH YIEVVKAAAD GDRDCVLQKS
RDLKFLTGFE TKAFSDAHVE AVMILGEPFA TQGPYDFGSG ETARRIQDLI PVLLRHRLCP
PPEETYALHR KLAGAFLACA HLRAHIACRD LFQDTYHRYW ASRQPDAATA GSLPTKGDSW
VDPS
