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   27-MAR-2024, entry version 164.
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   SUBCELLULAR LOCATION.
RX   PubMed=33988507; DOI=10.7554/elife.64943;
RA   Zhang H., Cao X., Tang M., Zhong G., Si Y., Li H., Zhu F., Liao Q., Li L.,
RA   Zhao J., Feng J., Li S., Wang C., Kaulich M., Wang F., Chen L., Li L.,
RA   Xia Z., Liang T., Lu H., Feng X.H., Zhao B.;
RT   "A subcellular map of the human kinome.";
RL   Elife 10:0-0(2021).
RN   [8]
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   [9]
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   [10]
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, ECO:0000269|PubMed:33988507}; Single-pass
CC       membrane protein {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; 147.
DR   IntAct; Q96D53; 67.
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   SwissPalm; Q96D53; -.
DR   BioMuta; COQ8B; -.
DR   DMDM; 74731415; -.
DR   EPD; Q96D53; -.
DR   jPOST; Q96D53; -.
DR   MassIVE; Q96D53; -.
DR   MaxQB; Q96D53; -.
DR   PaxDb; 9606-ENSP00000315118; -.
DR   PeptideAtlas; Q96D53; -.
DR   ProteomicsDB; 76252; -. [Q96D53-1]
DR   ProteomicsDB; 76253; -. [Q96D53-2]
DR   Pumba; Q96D53; -.
DR   Antibodypedia; 30619; 281 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   AGR; HGNC:19041; -.
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; 668390at2759; -.
DR   PhylomeDB; Q96D53; -.
DR   TreeFam; TF300630; -.
DR   BioCyc; MetaCyc:ENSG00000123815-MONOMER; -.
DR   PathwayCommons; Q96D53; -.
DR   SignaLink; Q96D53; -.
DR   BioGRID-ORCS; 79934; 18 hits in 1189 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 153 other cell types or tissues.
DR   ExpressionAtlas; Q96D53; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR43851; -; 1.
DR   PANTHER; PTHR43851:SF4; ATYPICAL KINASE COQ8B, MITOCHONDRIAL; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   Genevisible; Q96D53; HS.
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
//