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 27-MAR-2024, entry version 234. 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}. 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; 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; 90. 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 CPTAC; CPTAC-2839; -. DR CPTAC; non-CPTAC-3114; -. DR CPTAC; non-CPTAC-5687; -. DR CPTAC; non-CPTAC-5688; -. DR EPD; P15735; -. DR jPOST; P15735; -. DR MassIVE; P15735; -. DR MaxQB; P15735; -. DR PaxDb; 9606-ENSP00000455607; -. DR PeptideAtlas; P15735; -. DR ProteomicsDB; 53208; -. [P15735-1] DR ProteomicsDB; 53209; -. [P15735-2] DR Pumba; P15735; -. DR Antibodypedia; 13792; 440 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 AGR; HGNC:8931; -. 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; 1121238at2759; -. DR PhylomeDB; P15735; -. DR TreeFam; TF320349; -. DR BioCyc; MetaCyc:HS08155-MONOMER; -. 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 1201 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 129 other cell types or tissues. DR ExpressionAtlas; P15735; baseline and differential. 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 CDD; cd14181; STKc_PhKG2; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24347:SF390; PHOSPHORYLASE B KINASE GAMMA CATALYTIC CHAIN, LIVER_TESTIS ISOFORM; 1. DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01049; PHOSPHBKNASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P15735; HS. 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 //