PHKG2_HUMAN
ID PHKG2_HUMAN Reviewed; 406 AA.
AC P15735; A8K0C7; B4DEB7; E9PEU3; P11800;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Phosphorylase b kinase gamma catalytic chain, liver/testis isoform;
DE Short=PHK-gamma-LT;
DE Short=PHK-gamma-T;
DE EC=2.7.11.19;
DE AltName: Full=PSK-C3;
DE AltName: Full=Phosphorylase kinase subunit gamma-2;
GN Name=PHKG2;
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] (ISOFORM 1).
RX PubMed=2915644; DOI=10.1210/mend-3-1-110;
RA Hanks S.K.;
RT "Messenger ribonucleic acid encoding an apparent isoform of phosphorylase
RT kinase catalytic subunit is abundant in the adult testis.";
RL Mol. Endocrinol. 3:110-116(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9384616; DOI=10.1093/hmg/7.1.149;
RA Burwinkel B., Shiomi S., Al Zaben A., Kilimann M.W.;
RT "Liver glycogenosis due to phosphorylase kinase deficiency: PHKG2 gene
RT structure and mutations associated with cirrhosis.";
RL Hum. Mol. Genet. 7:149-154(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 129-273.
RX PubMed=2948189; DOI=10.1073/pnas.84.2.388;
RA Hanks S.K.;
RT "Homology probing: identification of cDNA clones encoding members of the
RT protein-serine kinase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:388-392(1987).
RN [7]
RP INVOLVEMENT IN GSD9C.
RX PubMed=9245685; DOI=10.1006/bbrc.1997.7006;
RA van Beurden E.A., de Graaf M., Wendel U., Gitzelmann R., Berger R.,
RA van den Berg I.E.;
RT "Autosomal recessive liver phosphorylase kinase deficiency caused by a
RT novel splice-site mutation in the gene encoding the liver gamma subunit
RT (PHKG2).";
RL Biochem. Biophys. Res. Commun. 236:544-548(1997).
RN [8]
RP FUNCTION, AND STRUCTURE.
RX PubMed=10487978; DOI=10.2741/brushia;
RA Brushia R.J., Walsh D.A.;
RT "Phosphorylase kinase: the complexity of its regulation is reflected in the
RT complexity of its structure.";
RL Front. Biosci. 4:D618-D641(1999).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 6-293 IN COMPLEX WITH INHIBITOR.
RG Structural genomics consortium (SGC);
RT "Structure of human phosphorylase kinase, gamma 2.";
RL Submitted (FEB-2011) to the PDB data bank.
RN [13]
RP VARIANTS GSD9C GLU-106 AND GLU-189.
RX PubMed=8896567; DOI=10.1038/ng1196-337;
RA Maichele A.J., Burwinkel B., Maire I., Sovik O., Kilimann M.W.;
RT "Mutations in the testis/liver isoform of the phosphorylase kinase gamma
RT subunit (PHKG2) cause autosomal liver glycogenosis in the gsd rat and in
RT humans.";
RL Nat. Genet. 14:337-340(1996).
RN [14]
RP VARIANTS GSD9C LYS-157 AND ASN-215.
RX PubMed=12930917; DOI=10.1203/01.pdr.0000088069.09275.10;
RA Burwinkel B., Rootwelt T., Kvittingen E.A., Chakraborty P.K.,
RA Kilimann M.W.;
RT "Severe phenotype of phosphorylase kinase-deficient liver glycogenosis with
RT mutations in the PHKG2 gene.";
RL Pediatr. Res. 54:834-839(2003).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] THR-317.
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).
CC -!- FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which
CC mediates the neural and hormonal regulation of glycogen breakdown
CC (glycogenolysis) by phosphorylating and thereby activating glycogen
CC phosphorylase. May regulate glycogeneolysis in the testis. In vitro,
CC phosphorylates PYGM (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10487978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.;
CC EC=2.7.11.19;
CC -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC subunit, and delta is calmodulin. {ECO:0000269|Ref.12}.
CC -!- INTERACTION:
CC P15735; P43356: MAGEA2B; NbExp=3; IntAct=EBI-1383819, EBI-5650739;
CC P15735; P46019: PHKA2; NbExp=7; IntAct=EBI-1383819, EBI-1642846;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15735-2; Sequence=VSP_041858, VSP_041859;
CC -!- DISEASE: Glycogen storage disease 9C (GSD9C) [MIM:613027]: A metabolic
CC disorder manifesting in infancy with hepatomegaly, growth retardation,
CC hypotonia, liver dysfunction, and elevated plasma aminotransferases and
CC lipids. These symptoms improve with age in most cases; however, some
CC patients may develop hepatic fibrosis or cirrhosis.
CC {ECO:0000269|PubMed:12930917, ECO:0000269|PubMed:8896567,
CC ECO:0000269|PubMed:9245685}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; M31606; AAA36442.1; -; mRNA.
DR EMBL; Y11950; CAA72694.1; -; Genomic_DNA.
DR EMBL; Y11951; CAA72694.1; JOINED; Genomic_DNA.
DR EMBL; AK289492; BAF82181.1; -; mRNA.
DR EMBL; AK293551; BAG57028.1; -; mRNA.
DR EMBL; AC106886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002541; AAH02541.1; -; mRNA.
DR EMBL; M14503; AAA36518.1; -; mRNA.
DR CCDS; CCDS10690.1; -. [P15735-1]
DR CCDS; CCDS54002.1; -. [P15735-2]
DR PIR; A40069; KIHUCT.
DR RefSeq; NP_000285.1; NM_000294.2. [P15735-1]
DR RefSeq; NP_001165903.1; NM_001172432.1. [P15735-2]
DR PDB; 2Y7J; X-ray; 2.50 A; A/B/C/D=6-293.
DR PDBsum; 2Y7J; -.
DR AlphaFoldDB; P15735; -.
DR SMR; P15735; -.
DR BioGRID; 111279; 71.
DR IntAct; P15735; 53.
DR MINT; P15735; -.
DR STRING; 9606.ENSP00000455607; -.
DR BindingDB; P15735; -.
DR ChEMBL; CHEMBL2349; -.
DR DrugCentral; P15735; -.
DR GuidetoPHARMACOLOGY; 2147; -.
DR GlyGen; P15735; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P15735; -.
DR PhosphoSitePlus; P15735; -.
DR BioMuta; PHKG2; -.
DR DMDM; 125536; -.
DR EPD; P15735; -.
DR jPOST; P15735; -.
DR MassIVE; P15735; -.
DR MaxQB; P15735; -.
DR PaxDb; P15735; -.
DR PeptideAtlas; P15735; -.
DR PRIDE; P15735; -.
DR ProteomicsDB; 53208; -. [P15735-1]
DR ProteomicsDB; 53209; -. [P15735-2]
DR Antibodypedia; 13792; 387 antibodies from 30 providers.
DR DNASU; 5261; -.
DR Ensembl; ENST00000424889.7; ENSP00000388571.3; ENSG00000156873.16. [P15735-2]
DR Ensembl; ENST00000563588.6; ENSP00000455607.1; ENSG00000156873.16. [P15735-1]
DR GeneID; 5261; -.
DR KEGG; hsa:5261; -.
DR MANE-Select; ENST00000563588.6; ENSP00000455607.1; NM_000294.3; NP_000285.1.
DR UCSC; uc021tgo.3; human. [P15735-1]
DR CTD; 5261; -.
DR DisGeNET; 5261; -.
DR GeneCards; PHKG2; -.
DR GeneReviews; PHKG2; -.
DR HGNC; HGNC:8931; PHKG2.
DR HPA; ENSG00000156873; Tissue enriched (testis).
DR MalaCards; PHKG2; -.
DR MIM; 172471; gene.
DR MIM; 613027; phenotype.
DR neXtProt; NX_P15735; -.
DR OpenTargets; ENSG00000156873; -.
DR Orphanet; 264580; Glycogen storage disease due to liver phosphorylase kinase deficiency.
DR PharmGKB; PA33272; -.
DR VEuPathDB; HostDB:ENSG00000156873; -.
DR eggNOG; KOG0599; Eukaryota.
DR GeneTree; ENSGT00940000160435; -.
DR InParanoid; P15735; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P15735; -.
DR TreeFam; TF320349; -.
DR BioCyc; MetaCyc:HS08155-MON; -.
DR BRENDA; 2.7.11.19; 2681.
DR PathwayCommons; P15735; -.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P15735; -.
DR SIGNOR; P15735; -.
DR BioGRID-ORCS; 5261; 9 hits in 1114 CRISPR screens.
DR ChiTaRS; PHKG2; human.
DR GeneWiki; PHKG2; -.
DR GenomeRNAi; 5261; -.
DR Pharos; P15735; Tchem.
DR PRO; PR:P15735; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P15735; protein.
DR Bgee; ENSG00000156873; Expressed in left testis and 127 other tissues.
DR ExpressionAtlas; P15735; baseline and differential.
DR Genevisible; P15735; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005964; C:phosphorylase kinase complex; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0004689; F:phosphorylase kinase activity; TAS:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; TAS:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
DR GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
DR GO; GO:0045819; P:positive regulation of glycogen catabolic process; TAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002291; Phosph_kin_gamma.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01049; PHOSPHBKNASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Carbohydrate metabolism; Disease variant; Glycogen metabolism;
KW Glycogen storage disease; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..406
FT /note="Phosphorylase b kinase gamma catalytic chain,
FT liver/testis isoform"
FT /id="PRO_0000086512"
FT DOMAIN 24..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 306..330
FT /note="Calmodulin-binding (domain-N)"
FT /evidence="ECO:0000250"
FT REGION 346..370
FT /note="Calmodulin-binding (domain-C)"
FT /evidence="ECO:0000250"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 362..374
FT /note="VKKGEQQNRAALF -> IRKQWIGKLMACV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041858"
FT VAR_SEQ 375..406
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041859"
FT VARIANT 106
FT /note="V -> E (in GSD9C; dbSNP:rs137853589)"
FT /evidence="ECO:0000269|PubMed:8896567"
FT /id="VAR_009517"
FT VARIANT 157
FT /note="E -> K (in GSD9C; dbSNP:rs752961445)"
FT /evidence="ECO:0000269|PubMed:12930917"
FT /id="VAR_020854"
FT VARIANT 189
FT /note="G -> E (in GSD9C; dbSNP:rs137853588)"
FT /evidence="ECO:0000269|PubMed:8896567"
FT /id="VAR_009518"
FT VARIANT 215
FT /note="D -> N (in GSD9C; dbSNP:rs767427889)"
FT /evidence="ECO:0000269|PubMed:12930917"
FT /id="VAR_020855"
FT VARIANT 247
FT /note="E -> G (in dbSNP:rs34006569)"
FT /id="VAR_051658"
FT VARIANT 317
FT /note="A -> T (in dbSNP:rs759992249)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040996"
FT CONFLICT 146
FT /note="A -> P (in Ref. 6; AAA36518)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="C -> S (in Ref. 6; AAA36518)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="E -> D (in Ref. 6; AAA36518)"
FT /evidence="ECO:0000305"
FT CONFLICT 212..214
FT /note="KEV -> LVD (in Ref. 6; AAA36518)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="V -> E (in Ref. 6; AAA36518)"
FT /evidence="ECO:0000305"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2Y7J"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:2Y7J"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:2Y7J"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2Y7J"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 64..84
FT /evidence="ECO:0007829|PDB:2Y7J"
FT STRAND 93..107
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2Y7J"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2Y7J"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:2Y7J"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:2Y7J"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:2Y7J"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2Y7J"
SQ SEQUENCE 406 AA; 46442 MW; E991CFF2D3D70F60 CRC64;
MTLDVGPEDE LPDWAAAKEF YQKYDPKDVI GRGVSSVVRR CVHRATGHEF AVKIMEVTAE
RLSPEQLEEV REATRRETHI LRQVAGHPHI ITLIDSYESS SFMFLVFDLM RKGELFDYLT
EKVALSEKET RSIMRSLLEA VSFLHANNIV HRDLKPENIL LDDNMQIRLS DFGFSCHLEP
GEKLRELCGT PGYLAPEILK CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL
MLRMIMEGQY QFSSPEWDDR SSTVKDLISR LLQVDPEARL TAEQALQHPF FERCEGSQPW
NLTPRQRFRV AVWTVLAAGR VALSTHRVRP LTKNALLRDP YALRSVRHLI DNCAFRLYGH
WVKKGEQQNR AALFQHRPPG PFPIMGPEEE GDSAAITEDE AVLVLG
