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cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE)

 PDE2A_MOUSE             Reviewed;         939 AA.
Q922S4; Q3TCR8; Q3TXZ6; Q8K2U1;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 4.
07-NOV-2018, entry version 144.
RecName: Full=cGMP-dependent 3',5'-cyclic phosphodiesterase;
EC=3.1.4.17;
AltName: Full=Cyclic GMP-stimulated phosphodiesterase;
Short=CGS-PDE;
Short=cGSPDE;
Name=Pde2a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:BAE34768.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PDE2A2 AND PDE2A3).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34768.1};
TISSUE=Visual cortex {ECO:0000312|EMBL:BAE34768.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE2A1).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 828-837, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
FUNCTION (ISOFORM PDE2A2), SUBCELLULAR LOCATION (ISOFORM PDE2A2), AND
TISSUE SPECIFICITY (ISOFORM PDE2A2).
PubMed=21724846; DOI=10.1074/jbc.M111.266379;
Acin-Perez R., Russwurm M., Gunnewig K., Gertz M., Zoidl G., Ramos L.,
Buck J., Levin L.R., Rassow J., Manfredi G., Steegborn C.;
"A phosphodiesterase 2A isoform localized to mitochondria regulates
respiration.";
J. Biol. Chem. 286:30423-30432(2011).
[6]
FUNCTION (ISOFORM PDE2A2), DISRUPTION PHENOTYPE, AND ACTIVITY
REGULATION.
TISSUE=Embryonic fibroblast;
PubMed=28463107; DOI=10.7554/eLife.21374;
Monterisi S., Lobo M.J., Livie C., Castle J.C., Weinberger M.,
Baillie G., Surdo N.C., Musheshe N., Stangherlin A., Gottlieb E.,
Maizels R., Bortolozzi M., Micaroni M., Zaccolo M.;
"PDE2A2 regulates mitochondria morphology and apoptotic cell death via
local modulation of cAMP/PKA signalling.";
Elife 6:0-0(2017).
[7]
X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 217-561 IN COMPLEX WITH
CGMP, DOMAIN GAF 1, AND SUBUNIT.
PubMed=12271124; DOI=10.1073/pnas.192374899;
Martinez S.E., Wu A.Y., Glavas N.A., Tang X.-B., Turley S.,
Hol W.G.J., Beavo J.A.;
"The two GAF domains in phosphodiesterase 2A have distinct roles in
dimerization and in cGMP binding.";
Proc. Natl. Acad. Sci. U.S.A. 99:13260-13265(2002).
-!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
specificity for the second messengers cAMP and cGMP, which are key
regulators of many important physiological processes.
{ECO:0000250}.
-!- FUNCTION: Isoform PDE2A2: Regulates mitochondrial cAMP levels and
respiration (PubMed:21724846). Involved in the regulation of
mitochondria morphology/dynamics and apoptotic cell death via
local modulation of cAMP/PKA signaling in the mitochondrion,
including the monitoring of local cAMP levels at the outer
mitochondrial membrane and of PKA-dependent phosphorylation of
DNM1L (PubMed:28463107). {ECO:0000269|PubMed:21724846,
ECO:0000269|PubMed:28463107}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000250};
-!- ACTIVITY REGULATION: Specifically inhibited by Bay 60-7550.
{ECO:0000269|PubMed:28463107}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12271124}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A1: Cytoplasm
{ECO:0000250|UniProtKB:O00408}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A2: Mitochondrion matrix
{ECO:0000269|PubMed:21724846}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:O00408}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:O00408}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A3: Cell membrane
{ECO:0000250|UniProtKB:O00408}; Lipid-anchor
{ECO:0000250|UniProtKB:O00408}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=PDE2A3 {ECO:0000305};
IsoId=Q922S4-1; Sequence=Displayed;
Name=PDE2A1 {ECO:0000305};
IsoId=Q922S4-2; Sequence=VSP_059396, VSP_059397;
Name=PDE2A2 {ECO:0000303|PubMed:21724846};
IsoId=Q922S4-3; Sequence=VSP_059395, VSP_059397;
Note=Contains a transit peptide at positions 1-17.
{ECO:0000269|PubMed:21724846};
-!- TISSUE SPECIFICITY: Isoform PDE2A2: Expressed in brain and liver
(at protein level). {ECO:0000269|PubMed:21724846}.
-!- DOMAIN: GAF 1 functions as a dimerization domain, whereas GAF 2
binds cGMP, which causes activation of the catalytic activity of
the enzyme. {ECO:0000269|PubMed:12271124}.
-!- DISRUPTION PHENOTYPE: Abnormally elongated mitochondria. This
phenotype is reversed by treatment with the PKA inhibitor H89.
Protected from ionomycin- but not staurosporin-induced cell death.
{ECO:0000269|PubMed:28463107}.
-!- MISCELLANEOUS: cGMP binds at an allosteric activator site.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE2 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BC057029; Type=Frameshift; Positions=560; Evidence={ECO:0000305};
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EMBL; AK159012; BAE34768.1; -; mRNA.
EMBL; AK170573; BAE41887.1; -; mRNA.
EMBL; AC129079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC129609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006845; AAH06845.1; -; mRNA.
EMBL; BC029810; AAH29810.1; -; mRNA.
EMBL; BC057029; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS52330.1; -. [Q922S4-1]
RefSeq; NP_001137320.1; NM_001143848.2. [Q922S4-1]
RefSeq; NP_001137321.1; NM_001143849.2. [Q922S4-3]
RefSeq; XP_006507590.1; XM_006507527.3.
UniGene; Mm.247564; -.
PDB; 1MC0; X-ray; 2.86 A; A=217-561.
PDBsum; 1MC0; -.
ProteinModelPortal; Q922S4; -.
SMR; Q922S4; -.
IntAct; Q922S4; 4.
STRING; 10090.ENSMUSP00000131553; -.
iPTMnet; Q922S4; -.
PhosphoSitePlus; Q922S4; -.
SwissPalm; Q922S4; -.
MaxQB; Q922S4; -.
PaxDb; Q922S4; -.
PeptideAtlas; Q922S4; -.
PRIDE; Q922S4; -.
Ensembl; ENSMUST00000163751; ENSMUSP00000131553; ENSMUSG00000110195. [Q922S4-1]
GeneID; 207728; -.
KEGG; mmu:207728; -.
UCSC; uc009ioq.3; mouse. [Q922S4-1]
UCSC; uc012fqk.2; mouse.
CTD; 5138; -.
MGI; MGI:2446107; Pde2a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG053540; -.
InParanoid; Q922S4; -.
KO; K18283; -.
OrthoDB; EOG091G0L2F; -.
TreeFam; TF316499; -.
Reactome; R-MMU-418457; cGMP effects.
Reactome; R-MMU-418555; G alpha (s) signalling events.
EvolutionaryTrace; Q922S4; -.
PRO; PR:Q922S4; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030653; Expressed in 251 organ(s), highest expression level in striatum.
CleanEx; MM_PDE2A; -.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0097457; C:hippocampal mossy fiber; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0097060; C:synaptic membrane; ISO:MGI.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IMP:UniProtKB.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IMP:UniProtKB.
GO; GO:0030552; F:cAMP binding; IMP:UniProtKB.
GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0036004; F:GAF domain binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030911; F:TPR domain binding; ISO:MGI.
GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0003279; P:cardiac septum development; IMP:MGI.
GO; GO:1904613; P:cellular response to 2,3,7,8-tetrachlorodibenzodioxine; ISO:MGI.
GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
GO; GO:0071321; P:cellular response to cGMP; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
GO; GO:0046069; P:cGMP catabolic process; IMP:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; IDA:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0003170; P:heart valve development; IMP:MGI.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IMP:UniProtKB.
GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IMP:UniProtKB.
GO; GO:0033159; P:negative regulation of protein import into nucleus, translocation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0043117; P:positive regulation of vascular permeability; ISS:UniProtKB.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB.
GO; GO:0010749; P:regulation of nitric oxide mediated signal transduction; IGI:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 2.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF01590; GAF; 1.
Pfam; PF13185; GAF_2; 1.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; cAMP; Cell membrane; cGMP;
cGMP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Lipoprotein; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Mitochondrion outer membrane; Myristate;
Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O00408}.
CHAIN 2 939 cGMP-dependent 3',5'-cyclic
phosphodiesterase.
/FTId=PRO_0000198797.
DOMAIN 236 373 GAF 1. {ECO:0000255}.
DOMAIN 408 547 GAF 2. {ECO:0000255}.
DOMAIN 577 901 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
REGION 655 659 Substrate binding. {ECO:0000250}.
ACT_SITE 655 655 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
METAL 659 659 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 695 695 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 696 696 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 696 696 Divalent metal cation 2.
{ECO:0000250|UniProtKB:O00408}.
METAL 807 807 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
BINDING 430 430 cGMP. {ECO:0000244|PDB:1MC0,
ECO:0000269|PubMed:12271124}.
BINDING 445 445 cGMP. {ECO:0000244|PDB:1MC0,
ECO:0000269|PubMed:12271124}.
BINDING 498 498 cGMP. {ECO:0000244|PDB:1MC0,
ECO:0000269|PubMed:12271124}.
BINDING 696 696 Substrate. {ECO:0000250}.
BINDING 807 807 Substrate. {ECO:0000250}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000250|UniProtKB:Q01062}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:O00408}.
LIPID 5 5 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:O00408}.
LIPID 11 11 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:O00408}.
VAR_SEQ 1 46 MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPQPC
ADSLQ -> MRRQPAASQDPLAQKPEPPGSRDDRLE (in
isoform PDE2A1). {ECO:0000305}.
/FTId=VSP_059396.
VAR_SEQ 1 24 MGQACGHSILCRSQQYPAARPAEP -> MVLVLHHILIAVV
QFLR (in isoform PDE2A2). {ECO:0000305}.
/FTId=VSP_059395.
VAR_SEQ 353 356 Missing (in isoform PDE2A1 and isoform
PDE2A2). {ECO:0000305}.
/FTId=VSP_059397.
CONFLICT 596 596 D -> G (in Ref. 1; BAE41887).
{ECO:0000305}.
HELIX 218 229 {ECO:0000244|PDB:1MC0}.
HELIX 236 250 {ECO:0000244|PDB:1MC0}.
STRAND 253 261 {ECO:0000244|PDB:1MC0}.
STRAND 263 265 {ECO:0000244|PDB:1MC0}.
STRAND 267 273 {ECO:0000244|PDB:1MC0}.
STRAND 276 290 {ECO:0000244|PDB:1MC0}.
HELIX 291 297 {ECO:0000244|PDB:1MC0}.
HELIX 303 305 {ECO:0000244|PDB:1MC0}.
HELIX 308 318 {ECO:0000244|PDB:1MC0}.
STRAND 325 331 {ECO:0000244|PDB:1MC0}.
TURN 333 335 {ECO:0000244|PDB:1MC0}.
STRAND 337 349 {ECO:0000244|PDB:1MC0}.
HELIX 360 404 {ECO:0000244|PDB:1MC0}.
TURN 405 407 {ECO:0000244|PDB:1MC0}.
TURN 409 411 {ECO:0000244|PDB:1MC0}.
HELIX 412 424 {ECO:0000244|PDB:1MC0}.
STRAND 426 434 {ECO:0000244|PDB:1MC0}.
STRAND 436 444 {ECO:0000244|PDB:1MC0}.
HELIX 463 471 {ECO:0000244|PDB:1MC0}.
STRAND 475 478 {ECO:0000244|PDB:1MC0}.
HELIX 491 494 {ECO:0000244|PDB:1MC0}.
STRAND 501 507 {ECO:0000244|PDB:1MC0}.
STRAND 513 522 {ECO:0000244|PDB:1MC0}.
STRAND 525 527 {ECO:0000244|PDB:1MC0}.
HELIX 530 558 {ECO:0000244|PDB:1MC0}.
SEQUENCE 939 AA; 105619 MW; 1DD7BD9DBCF806E3 CRC64;
MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPQP CADSLQDALL SLGAVIDIAG
LRQAARDALS AVLPKVETVY TYLLDGESRL VCEDPPHELP QEGKIREAVI SQKRLSCNGL
GPSDLLGKPL ARLVAPLAPD MQVLVIPLLD KETGSVAAVI LVHCGQLSDS EEQSLQVVEK
HALVALRRVQ ALQQRRPEAV QNTSVDASED QKDEKGYTDH DRKILQLCGE LFDLDATSLQ
LKVLQYLQQE TQATHCCLLL VSEDNLQLSC KVIGDKVLGE EVSFPLTMGR LGQVVEDKQC
IQLKDLTSDD VQQLQNMLGC ELQAMLCVPV ISRATDQVVA LACAFNKLGG DFPTSSFTDE
DEHVIQHCFH YTGTVLTSTL AFQKEQKLKC ECQALLQVAK NLFTHLDDVS VLLQEIITEA
RNLSNAEICS VFLLDQNELV AKVFDGGVVD DESYEIRIPA DQGIAGHVAT TGQILNIPDA
YAHPLFYRGV DDSTGFRTRN ILCFPIKNEN QEVIGVAELV NKINGPWFSK FDEDLATAFS
IYCGISIAHS LLYKKVNEAQ YRSHLANEMM MYHMKVSDDE YTKLLHDGIQ PVAAIDSNFA
NFTYTPRSLP EDDTSMAILS MLQDMNFINN YKIDCPTLAR FCLMVKKGYR DPPYHNWMHA
FSVSHFCYLL YKNLELSNYL EDIEIFALFI SCMCHDLDHR GTNNSFQVAS KSVLAALYSS
EGSVMERHHF AQAIAILNTH GCNIFDHFSR KDYQRMLDLM RDIILATDLA HHLRIFKDLQ
KMAEVGYDRN NRQHHRLLLC LLMTSCDLSD QTKGWKTTRK IAELIYKEFF SQGDLEKAMG
NRPMEMMDRE KAYIPELQIS FMEHIAMPIY KLLQDLFPKA AELYERVASN REHWTKVSHK
FTIRGLPSNN SLDFLDEEYE VPDLDGTRAP VNGCCSLEG


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