ID KGP2_HUMAN Reviewed; 762 AA. AC Q13237; B4DMX3; E7EPE6; O00125; O60916; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 151. DE RecName: Full=cGMP-dependent protein kinase 2; DE Short=cGK 2; DE Short=cGK2; DE EC=2.7.11.12; DE AltName: Full=cGMP-dependent protein kinase II; DE Short=cGKII; GN Name=PRKG2; Synonyms=PRKGR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8607838; DOI=10.1006/bbrc.1996.0477; RA Orstavik S., Solberg R., Taskn K., Nordahl M., Altherr M.R., RA Hansson V., Jahnsen T., Sandberg M.; RT "Molecular cloning, cDNA structure, and chromosomal localization of RT the human type II cGMP-dependent protein kinase."; RL Biochem. Biophys. Res. Commun. 220:759-765(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7498513; DOI=10.1016/0014-5793(95)01223-2; RA Fujii M., Ogata T., Takahashi E., Yamada K., Nakabayashi K., Oishi M., RA Ayusawa D.; RT "Expression of the human cGMP-dependent protein kinase II gene is lost RT upon introduction of SV40 T antigen or immortalization in human RT cells."; RL FEBS Lett. 375:263-267(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Heart; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-734. RX PubMed=9535793; DOI=10.1006/bbrc.1998.8399; RA Witczak O., Orstavik S., Natarajan V., Frengen E., Jahnsen T., RA Sandberg M.; RT "Characterization of the gene encoding the human type II cGMP- RT dependent protein kinase."; RL Biochem. Biophys. Res. Commun. 245:113-119(1998). RN [6] RP MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION. RX PubMed=8636133; DOI=10.1074/jbc.271.12.7025; RA Vaandrager A.B., Ehlert E.M., Jarchau T., Lohmann S.M., de Jonge H.R.; RT "N-terminal myristoylation is required for membrane localization of RT cGMP-dependent protein kinase type II."; RL J. Biol. Chem. 271:7025-7029(1996). RN [7] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-106 AND ARG-716. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Binding of cGMP results in enzyme activation. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:8636133}; Lipid-anchor CC {ECO:0000269|PubMed:8636133}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13237-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13237-2; Sequence=VSP_055121; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Highly concentrated in brain, lung and CC intestinal mucosa. CC -!- PTM: Myristoylation mediates membrane localization. CC {ECO:0000269|PubMed:8636133}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. cGMP subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains. CC {ECO:0000255|PROSITE-ProRule:PRU00060}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; X94612; CAA64318.1; -; mRNA. DR EMBL; D70899; BAA18934.1; -; mRNA. DR EMBL; AK297673; BAG60035.1; -; mRNA. DR EMBL; AC098819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139722; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Y16106; CAA76073.1; -; Genomic_DNA. DR EMBL; Y16107; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16108; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16109; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16110; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16111; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16112; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16113; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16114; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16115; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16116; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16117; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16118; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16119; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16120; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16121; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16122; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16123; CAA76073.1; JOINED; Genomic_DNA. DR CCDS; CCDS3589.1; -. [Q13237-1] DR CCDS; CCDS64005.1; -. [Q13237-2] DR PIR; S68217; S68217. DR RefSeq; NP_001269409.1; NM_001282480.1. DR RefSeq; NP_001269410.1; NM_001282481.1. DR RefSeq; NP_001269411.1; NM_001282482.1. DR RefSeq; NP_001269412.1; NM_001282483.1. DR RefSeq; NP_001269414.1; NM_001282485.1. [Q13237-2] DR RefSeq; NP_006250.1; NM_006259.2. [Q13237-1] DR RefSeq; XP_005263183.1; XM_005263126.2. [Q13237-1] DR RefSeq; XP_011530416.1; XM_011532114.1. [Q13237-1] DR RefSeq; XP_011530417.1; XM_011532115.1. [Q13237-1] DR UniGene; Hs.232044; -. DR UniGene; Hs.570833; -. DR UniGene; Hs.739943; -. DR PDB; 5BV6; X-ray; 1.94 A; A=269-418. DR PDB; 5C6C; X-ray; 2.05 A; A/B=137-277. DR PDB; 5C8W; X-ray; 1.80 A; A/B/C/D/E/F=137-277. DR PDBsum; 5BV6; -. DR PDBsum; 5C6C; -. DR PDBsum; 5C8W; -. DR ProteinModelPortal; Q13237; -. DR SMR; Q13237; 47-762. DR BioGrid; 111579; 7. DR IntAct; Q13237; 3. DR STRING; 9606.ENSP00000264399; -. DR BindingDB; Q13237; -. DR ChEMBL; CHEMBL2896; -. DR GuidetoPHARMACOLOGY; 1493; -. DR iPTMnet; Q13237; -. DR PhosphoSite; Q13237; -. DR DMDM; 6226833; -. DR MaxQB; Q13237; -. DR PaxDb; Q13237; -. DR PRIDE; Q13237; -. DR DNASU; 5593; -. DR Ensembl; ENST00000264399; ENSP00000264399; ENSG00000138669. [Q13237-1] DR Ensembl; ENST00000395578; ENSP00000378945; ENSG00000138669. [Q13237-1] DR Ensembl; ENST00000628926; ENSP00000486129; ENSG00000138669. [Q13237-2] DR GeneID; 5593; -. DR KEGG; hsa:5593; -. DR UCSC; uc003hmh.3; human. [Q13237-1] DR CTD; 5593; -. DR GeneCards; PRKG2; -. DR HGNC; HGNC:9416; PRKG2. DR HPA; CAB018739; -. DR HPA; HPA007386; -. DR MIM; 601591; gene. DR neXtProt; NX_Q13237; -. DR PharmGKB; PA33778; -. DR eggNOG; KOG0616; Eukaryota. DR eggNOG; ENOG410XPQQ; LUCA. DR GeneTree; ENSGT00810000125385; -. DR HOGENOM; HOG000233033; -. DR HOVERGEN; HBG006211; -. DR InParanoid; Q13237; -. DR KO; K19477; -. DR OMA; ELQSKCI; -. DR OrthoDB; EOG75B84Q; -. DR PhylomeDB; Q13237; -. DR TreeFam; TF313261; -. DR BRENDA; 2.7.11.12; 2681. DR Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation. DR Reactome; R-HSA-4086398; Ca2+ pathway. DR Reactome; R-HSA-418457; cGMP effects. DR SignaLink; Q13237; -. DR GenomeRNAi; 5593; -. DR NextBio; 21704; -. DR PRO; PR:Q13237; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; Q13237; -. DR CleanEx; HS_PRKG2; -. DR ExpressionAtlas; Q13237; baseline and differential. DR Genevisible; Q13237; HS. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW. DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0046209; P:nitric oxide metabolic process; TAS:Reactome. DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc. DR GO; GO:0072661; P:protein targeting to plasma membrane; IEA:Ensembl. DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 2.60.120.10; -; 2. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR002374; cGMP_dep_kinase. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1. DR PRINTS; PR00104; CGMPKINASE. DR SMART; SM00100; cNMP; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF51206; SSF51206; 2. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. 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; Cell membrane; cGMP; KW cGMP-binding; Complete proteome; Kinase; Lipoprotein; Membrane; KW Myristate; Nucleotide-binding; Phosphoprotein; Polymorphism; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 762 cGMP-dependent protein kinase 2. FT /FTId=PRO_0000086123. FT DOMAIN 453 711 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 712 762 AGC-kinase C-terminal. FT NP_BIND 168 285 cGMP 1. FT NP_BIND 286 417 cGMP 2. FT NP_BIND 459 467 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 576 576 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 482 482 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 110 110 Phosphoserine. FT {ECO:0000250|UniProtKB:Q64595}. FT MOD_RES 117 117 Phosphoserine. FT {ECO:0000250|UniProtKB:Q64595}. FT MOD_RES 431 431 Phosphoserine. FT {ECO:0000250|UniProtKB:Q64595}. FT MOD_RES 609 609 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q61410}. FT LIPID 2 2 N-myristoyl glycine. FT {ECO:0000269|PubMed:8636133}. FT VAR_SEQ 441 469 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055121. FT VARIANT 22 22 T -> S (in dbSNP:rs34956759). FT /FTId=VAR_051633. FT VARIANT 106 106 H -> R (in dbSNP:rs34616910). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040608. FT VARIANT 716 716 W -> R (in a colorectal adenocarcinoma FT sample; somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040609. FT CONFLICT 57 58 QL -> HG (in Ref. 2; BAA18934). FT {ECO:0000305}. FT CONFLICT 154 154 S -> I (in Ref. 5; CAA76073). FT {ECO:0000305}. FT CONFLICT 388 388 N -> D (in Ref. 3; BAG60035). FT {ECO:0000305}. FT CONFLICT 460 460 G -> A (in Ref. 2; BAA18934). FT {ECO:0000305}. FT HELIX 153 164 {ECO:0000244|PDB:5C8W}. FT HELIX 169 171 {ECO:0000244|PDB:5C8W}. FT HELIX 174 183 {ECO:0000244|PDB:5C8W}. FT STRAND 185 189 {ECO:0000244|PDB:5C8W}. FT STRAND 194 196 {ECO:0000244|PDB:5C8W}. FT STRAND 204 211 {ECO:0000244|PDB:5C8W}. FT STRAND 213 217 {ECO:0000244|PDB:5C8W}. FT STRAND 220 224 {ECO:0000244|PDB:5C8W}. FT STRAND 230 232 {ECO:0000244|PDB:5C8W}. FT HELIX 233 238 {ECO:0000244|PDB:5C8W}. FT STRAND 243 250 {ECO:0000244|PDB:5C8W}. FT STRAND 252 258 {ECO:0000244|PDB:5C8W}. FT HELIX 259 266 {ECO:0000244|PDB:5C8W}. FT HELIX 270 283 {ECO:0000244|PDB:5BV6}. FT HELIX 285 287 {ECO:0000244|PDB:5BV6}. FT HELIX 292 301 {ECO:0000244|PDB:5BV6}. FT STRAND 303 307 {ECO:0000244|PDB:5BV6}. FT STRAND 312 314 {ECO:0000244|PDB:5BV6}. FT STRAND 323 335 {ECO:0000244|PDB:5BV6}. FT STRAND 344 350 {ECO:0000244|PDB:5BV6}. FT HELIX 357 362 {ECO:0000244|PDB:5BV6}. FT STRAND 368 372 {ECO:0000244|PDB:5BV6}. FT STRAND 377 382 {ECO:0000244|PDB:5BV6}. FT HELIX 384 389 {ECO:0000244|PDB:5BV6}. FT TURN 390 393 {ECO:0000244|PDB:5BV6}. FT HELIX 395 415 {ECO:0000244|PDB:5BV6}. SQ SEQUENCE 762 AA; 87432 MW; FA7BA149906B5996 CRC64; MGNGSVKPKH SKHPDGHSGN LTTDALRNKV TELERELRRK DAEIQEREYH LKELREQLSK QTVAIAELTE ELQNKCIQLN KLQDVVHMQG GSPLQASPDK VPLEVHRKTS GLVSLHSRRG AKAGVSAEPT TRTYDLNKPP EFSFEKARVR KDSSEKKLIT DALNKNQFLK RLDPQQIKDM VECMYGRNYQ QGSYIIKQGE PGNHIFVLAE GRLEVFQGEK LLSSIPMWTT FGELAILYNC TRTASVKAIT NVKTWALDRE VFQNIMRRTA QARDEQYRNF LRSVSLLKNL PEDKLTKIID CLEVEYYDKG DYIIREGEEG STFFILAKGK VKVTQSTEGH DQPQLIKTLQ KGEYFGEKAL ISDDVRSANI IAEENDVACL VIDRETFNQT VGTFEELQKY LEGYVANLNR DDEKRHAKRS MSNWKLSKAL SLEMIQLKEK VARFSSSSPF QNLEIIATLG VGGFGRVELV KVKNENVAFA MKCIRKKHIV DTKQQEHVYS EKRILEELCS PFIVKLYRTF KDNKYVYMLL EACLGGELWS ILRDRGSFDE PTSKFCVACV TEAFDYLHRL GIIYRDLKPE NLILDAEGYL KLVDFGFAKK IGSGQKTWTF CGTPEYVAPE VILNKGHDFS VDFWSLGILV YELLTGNPPF SGVDQMMTYN LILKGIEKMD FPRKITRRPE DLIRRLCRQN PTERLGNLKN GINDIKKHRW LNGFNWEGLK ARSLPSPLQR ELKGPIDHSY FDKYPPEKGM PPDELSGWDK DF //