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mRNA-capping enzyme (HCAP1) (HCE) [Includes: Polynucleotide 5'-triphosphatase (EC 3.1.3.33) (mRNA 5'-triphosphatase) (TPase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase)]

 MCE1_HUMAN              Reviewed;         597 AA.
O60942; E1P513; E1P514; O43483; O60257; O60351; Q5TCW8; Q8WUM8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 172.
RecName: Full=mRNA-capping enzyme;
AltName: Full=HCAP1;
AltName: Full=HCE;
Includes:
RecName: Full=Polynucleotide 5'-triphosphatase;
EC=3.1.3.33;
AltName: Full=mRNA 5'-triphosphatase;
Short=TPase;
Includes:
RecName: Full=mRNA guanylyltransferase;
EC=2.7.7.50;
AltName: Full=GTP--RNA guanylyltransferase;
Short=GTase;
Name=RNGTT; Synonyms=CAP1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9371772; DOI=10.1073/pnas.94.24.12898;
Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J.;
"Mammalian capping enzyme complements mutant Saccharomyces cerevisiae
lacking mRNA guanylyltransferase and selectively binds the elongating
form of RNA polymerase II.";
Proc. Natl. Acad. Sci. U.S.A. 94:12898-12903(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), MUTAGENESIS OF
LYS-294; ARG-299; GLU-345; LYS-458 AND LYS-460, AND FUNCTION.
PubMed=9512541; DOI=10.1093/nar/26.7.1700;
Yamada-Okabe T., Doi R., Shimmi O., Arisawa M., Yamada-Okabe H.;
"Isolation and characterization of a human cDNA for mRNA 5'-capping
enzyme.";
Nucleic Acids Res. 26:1700-1706(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), FUNCTION, AND CATALYTIC
ACTIVITY.
TISSUE=Colon adenocarcinoma;
PubMed=9473487; DOI=10.1006/bbrc.1997.8038;
Tsukamoto T., Shibagaki Y., Murakoshi T., Suzuki M., Nakamura A.,
Gotoh H., Mizumoto K.;
"Cloning and characterization of two human cDNAs encoding the mRNA
capping enzyme.";
Biochem. Biophys. Res. Commun. 243:101-108(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-594.
TISSUE=Skin;
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).
[7]
INTERACTION WITH RNMT.
PubMed=9705270; DOI=10.1074/jbc.273.34.21443;
Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J.;
"Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA
polymerase IIo complexes.";
J. Biol. Chem. 273:21443-21446(1998).
[8]
INTERACTION WITH SUPT5H.
PubMed=10421630; DOI=10.1101/gad.13.14.1774;
Wen Y., Shatkin A.J.;
"Transcription elongation factor hSPT5 stimulates mRNA capping.";
Genes Dev. 13:1774-1779(1999).
[9]
INTERACTION WITH HIV-1 TAT.
PubMed=11278368; DOI=10.1074/jbc.M007901200;
Chiu Y.-L., Coronel E., Ho C.K., Shuman S., Rana T.M.;
"HIV-1 Tat protein interacts with mammalian capping enzyme and
stimulates capping of TAR RNA.";
J. Biol. Chem. 276:12959-12966(2001).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 229-567, CATALYTIC ACTIVITY,
FUNCTION, MUTAGENESIS OF GLU-234; LYS-458; LYS-460; ARG-528; ARG-530;
ASP-532 AND LYS-533, AND ACTIVE SITE.
PubMed=21636784; DOI=10.1073/pnas.1106610108;
Chu C., Das K., Tyminski J.R., Bauman J.D., Guan R., Qiu W.,
Montelione G.T., Arnold E., Shatkin A.J.;
"Structure of the guanylyltransferase domain of human mRNA capping
enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 108:10104-10108(2011).
-!- FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-
triphosphatase activity in the N-terminal part and mRNA
guanylyltransferase activity in the C-terminal part. Catalyzes the
first two steps of cap formation: by removing the gamma-phosphate
from the 5'-triphosphate end of nascent mRNA to yield a
diphosphate end, and by transferring the gmp moiety of GTP to the
5'-diphosphate terminus. {ECO:0000269|PubMed:21636784,
ECO:0000269|PubMed:9473487, ECO:0000269|PubMed:9512541}.
-!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a
polynucleotide + phosphate.
-!- CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate +
G(5')ppp-Pur-mRNA.
-!- SUBUNIT: Interacts with POLR2A (via C-terminus); this enhances
guanylyltransferase activity. Binds (via GTase domain) to the
elongating phosphorylated form of RNA polymerase II; can form
direct interactions with the phosphorylated POLR2A C-terminal
domain and indirect interactions via bound RNA (By similarity).
Interacts with SUPT5H and RNMT. Interacts with HIV-1 Tat.
{ECO:0000250, ECO:0000269|PubMed:10421630,
ECO:0000269|PubMed:11278368, ECO:0000269|PubMed:9705270}.
-!- INTERACTION:
P16333-1:NCK1; NbExp=2; IntAct=EBI-1237132, EBI-15578122;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=HCE1, HCAP1A;
IsoId=O60942-1; Sequence=Displayed;
Name=2; Synonyms=HCE1A;
IsoId=O60942-2; Sequence=VSP_003202;
Name=3; Synonyms=HCE1B;
IsoId=O60942-3; Sequence=VSP_003202, VSP_003203;
Name=4; Synonyms=HCAP1B;
IsoId=O60942-4; Sequence=VSP_003204;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 4 (at a lesser extent)
are expressed in cerebrum, cerebellum, thyroid, lung, heart,
liver, kidney, spleen, large intestine, testis, skin and muscle.
-!- MISCELLANEOUS: Isoform 2 to isoform 4 lack mRNA 5'-
guanylyltransferase activity due to disruptions of the GTase
domain.
-!- SIMILARITY: In the N-terminal section; belongs to the non-receptor
class of the protein-tyrosine phosphatase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
GTase family. {ECO:0000305}.
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EMBL; AF025654; AAB91559.1; -; mRNA.
EMBL; AB009022; BAA25894.1; -; mRNA.
EMBL; AB009023; BAA25895.1; -; mRNA.
EMBL; AB009024; BAA25896.1; -; mRNA.
EMBL; AB012142; BAA25198.1; -; mRNA.
EMBL; AB012143; BAA25199.1; -; mRNA.
EMBL; AL079342; CAI22537.1; -; Genomic_DNA.
EMBL; AL096868; CAI22537.1; JOINED; Genomic_DNA.
EMBL; AL133408; CAI22537.1; JOINED; Genomic_DNA.
EMBL; AL445530; CAI22537.1; JOINED; Genomic_DNA.
EMBL; AL096868; CAI21547.1; -; Genomic_DNA.
EMBL; AL079342; CAI21547.1; JOINED; Genomic_DNA.
EMBL; AL133408; CAI21547.1; JOINED; Genomic_DNA.
EMBL; AL445530; CAI21547.1; JOINED; Genomic_DNA.
EMBL; AL133408; CAI21542.1; -; Genomic_DNA.
EMBL; AL079342; CAI21542.1; JOINED; Genomic_DNA.
EMBL; AL096868; CAI21542.1; JOINED; Genomic_DNA.
EMBL; AL445530; CAI21542.1; JOINED; Genomic_DNA.
EMBL; AL445530; CAI22048.1; -; Genomic_DNA.
EMBL; AL079342; CAI22048.1; JOINED; Genomic_DNA.
EMBL; AL096868; CAI22048.1; JOINED; Genomic_DNA.
EMBL; AL133408; CAI22048.1; JOINED; Genomic_DNA.
EMBL; CH471051; EAW48566.1; -; Genomic_DNA.
EMBL; CH471051; EAW48567.1; -; Genomic_DNA.
EMBL; CH471051; EAW48569.1; -; Genomic_DNA.
EMBL; CH471051; EAW48570.1; -; Genomic_DNA.
EMBL; BC019954; AAH19954.1; -; mRNA.
CCDS; CCDS5017.1; -. [O60942-1]
CCDS; CCDS69153.1; -. [O60942-2]
PIR; JC5936; JC5936.
PIR; JC5937; JC5937.
RefSeq; NP_001273355.1; NM_001286426.1. [O60942-2]
RefSeq; NP_001273357.1; NM_001286428.1.
RefSeq; NP_003791.3; NM_003800.4. [O60942-1]
UniGene; Hs.567378; -.
UniGene; Hs.627135; -.
PDB; 2C46; X-ray; 1.60 A; A/B/C/D=1-219.
PDB; 3S24; X-ray; 3.01 A; A/B/C/D/E/F/G=229-567.
PDBsum; 2C46; -.
PDBsum; 3S24; -.
ProteinModelPortal; O60942; -.
SMR; O60942; -.
BioGrid; 114270; 45.
DIP; DIP-61014N; -.
IntAct; O60942; 5.
STRING; 9606.ENSP00000358497; -.
DrugBank; DB02325; Isopropyl Alcohol.
DEPOD; O60942; -.
iPTMnet; O60942; -.
PhosphoSitePlus; O60942; -.
BioMuta; RNGTT; -.
EPD; O60942; -.
MaxQB; O60942; -.
PaxDb; O60942; -.
PeptideAtlas; O60942; -.
PRIDE; O60942; -.
DNASU; 8732; -.
Ensembl; ENST00000369475; ENSP00000358487; ENSG00000111880. [O60942-2]
Ensembl; ENST00000369485; ENSP00000358497; ENSG00000111880. [O60942-1]
Ensembl; ENST00000538899; ENSP00000442609; ENSG00000111880. [O60942-3]
GeneID; 8732; -.
KEGG; hsa:8732; -.
UCSC; uc003pmr.4; human. [O60942-1]
CTD; 8732; -.
DisGeNET; 8732; -.
EuPathDB; HostDB:ENSG00000111880.15; -.
GeneCards; RNGTT; -.
HGNC; HGNC:10073; RNGTT.
HPA; HPA003750; -.
MIM; 603512; gene.
neXtProt; NX_O60942; -.
OpenTargets; ENSG00000111880; -.
PharmGKB; PA34446; -.
eggNOG; KOG2386; Eukaryota.
eggNOG; COG5226; LUCA.
GeneTree; ENSGT00530000063473; -.
HOVERGEN; HBG006332; -.
InParanoid; O60942; -.
KO; K13917; -.
OMA; KIIECTF; -.
OrthoDB; EOG091G063D; -.
PhylomeDB; O60942; -.
TreeFam; TF314914; -.
BioCyc; MetaCyc:HS03479-MONOMER; -.
BRENDA; 2.7.7.50; 2681.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
ChiTaRS; RNGTT; human.
EvolutionaryTrace; O60942; -.
GeneWiki; RNGTT; -.
GenomeRNAi; 8732; -.
PRO; PR:O60942; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000111880; -.
CleanEx; HS_RNGTT; -.
Genevisible; O60942; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004484; F:mRNA guanylyltransferase activity; IDA:UniProtKB.
GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; TAS:Reactome.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0008192; F:RNA guanylyltransferase activity; IDA:UniProtKB.
GO; GO:0050355; F:triphosphatase activity; IDA:UniProtKB.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
GO; GO:0006396; P:RNA processing; IDA:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR017074; mRNA_cap_enz_bifunc.
InterPro; IPR001339; mRNA_cap_enzyme.
InterPro; IPR013846; mRNA_cap_enzyme_C.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00782; DSPc; 1.
Pfam; PF03919; mRNA_cap_C; 1.
Pfam; PF01331; mRNA_cap_enzyme; 1.
PIRSF; PIRSF036958; mRNA_capping_HCE; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; GTP-binding;
Host-virus interaction; Hydrolase; mRNA capping; mRNA processing;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Nucleus; Polymorphism; Reference proteome; Transferase.
CHAIN 1 597 mRNA-capping enzyme.
/FTId=PRO_0000210108.
NP_BIND 343 345 GTP. {ECO:0000255}.
NP_BIND 458 460 GTP. {ECO:0000255}.
NP_BIND 528 533 GTP. {ECO:0000255}.
REGION 1 212 TPase.
REGION 229 597 GTase.
REGION 330 386 Interaction with POLR2A. {ECO:0000250}.
COMPBIAS 195 205 Asp/Glu-rich.
ACT_SITE 126 126 For RNA 5'-triphosphatase activity.
{ECO:0000250}.
ACT_SITE 294 294 N6-GMP-lysine intermediate.
{ECO:0000269|PubMed:21636784}.
BINDING 299 299 GTP. {ECO:0000250}.
BINDING 315 315 GTP. {ECO:0000255}.
VAR_SEQ 424 446 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:9512541}.
/FTId=VSP_003202.
VAR_SEQ 481 597 Missing (in isoform 3).
{ECO:0000303|PubMed:9512541}.
/FTId=VSP_003203.
VAR_SEQ 504 597 TKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYNTAMA
VCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTELM
PPPPPKRPRPLT -> CLFIFSVLFLDVLLSGIHQNLANNN
QHIKISCSSTLGG (in isoform 4).
{ECO:0000303|PubMed:9473487}.
/FTId=VSP_003204.
VARIANT 594 594 R -> H (in dbSNP:rs17856595).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_046481.
MUTAGEN 234 234 E->A: No effect on GTase activity.
{ECO:0000269|PubMed:21636784}.
MUTAGEN 294 294 K->A: Loss of GTase activity.
{ECO:0000269|PubMed:9512541}.
MUTAGEN 299 299 R->A: Loss of GTase activity.
{ECO:0000269|PubMed:9512541}.
MUTAGEN 345 345 E->A: Loss of GTase activity.
{ECO:0000269|PubMed:9512541}.
MUTAGEN 458 458 K->A: Loss of GTase activity.
{ECO:0000269|PubMed:21636784,
ECO:0000269|PubMed:9512541}.
MUTAGEN 460 460 K->A: Loss of GTase activity.
{ECO:0000269|PubMed:21636784,
ECO:0000269|PubMed:9512541}.
MUTAGEN 528 528 R->A: Strongly reduced GTase activity.
{ECO:0000269|PubMed:21636784}.
MUTAGEN 530 530 R->A: Loss of GTase activity.
{ECO:0000269|PubMed:21636784}.
MUTAGEN 532 532 D->A: Loss of GTase activity.
{ECO:0000269|PubMed:21636784}.
MUTAGEN 533 533 K->A: Loss of GTase activity.
{ECO:0000269|PubMed:21636784}.
CONFLICT 30 30 M -> I (in Ref. 1; AAB91559).
{ECO:0000305}.
CONFLICT 212 212 P -> T (in Ref. 6; AAH19954).
{ECO:0000305}.
CONFLICT 484 484 Q -> P (in Ref. 1; AAB91559).
{ECO:0000305}.
TURN 21 23 {ECO:0000244|PDB:2C46}.
STRAND 24 27 {ECO:0000244|PDB:2C46}.
HELIX 33 38 {ECO:0000244|PDB:2C46}.
HELIX 41 43 {ECO:0000244|PDB:2C46}.
HELIX 47 57 {ECO:0000244|PDB:2C46}.
STRAND 60 66 {ECO:0000244|PDB:2C46}.
HELIX 77 80 {ECO:0000244|PDB:2C46}.
TURN 81 83 {ECO:0000244|PDB:2C46}.
STRAND 85 88 {ECO:0000244|PDB:2C46}.
HELIX 100 110 {ECO:0000244|PDB:2C46}.
STRAND 120 125 {ECO:0000244|PDB:2C46}.
STRAND 127 130 {ECO:0000244|PDB:2C46}.
HELIX 131 143 {ECO:0000244|PDB:2C46}.
HELIX 149 159 {ECO:0000244|PDB:2C46}.
HELIX 167 177 {ECO:0000244|PDB:2C46}.
HELIX 180 182 {ECO:0000244|PDB:2C46}.
STRAND 232 235 {ECO:0000244|PDB:3S24}.
STRAND 241 243 {ECO:0000244|PDB:3S24}.
HELIX 247 261 {ECO:0000244|PDB:3S24}.
STRAND 265 267 {ECO:0000244|PDB:3S24}.
STRAND 270 275 {ECO:0000244|PDB:3S24}.
TURN 278 280 {ECO:0000244|PDB:3S24}.
HELIX 281 285 {ECO:0000244|PDB:3S24}.
STRAND 289 295 {ECO:0000244|PDB:3S24}.
STRAND 298 304 {ECO:0000244|PDB:3S24}.
STRAND 306 308 {ECO:0000244|PDB:3S24}.
STRAND 310 314 {ECO:0000244|PDB:3S24}.
STRAND 319 324 {ECO:0000244|PDB:3S24}.
STRAND 339 351 {ECO:0000244|PDB:3S24}.
STRAND 354 367 {ECO:0000244|PDB:3S24}.
HELIX 372 374 {ECO:0000244|PDB:3S24}.
HELIX 377 387 {ECO:0000244|PDB:3S24}.
HELIX 389 394 {ECO:0000244|PDB:3S24}.
TURN 395 397 {ECO:0000244|PDB:3S24}.
STRAND 398 401 {ECO:0000244|PDB:3S24}.
TURN 403 405 {ECO:0000244|PDB:3S24}.
STRAND 406 412 {ECO:0000244|PDB:3S24}.
HELIX 418 424 {ECO:0000244|PDB:3S24}.
STRAND 437 446 {ECO:0000244|PDB:3S24}.
STRAND 451 459 {ECO:0000244|PDB:3S24}.
HELIX 462 464 {ECO:0000244|PDB:3S24}.
STRAND 466 476 {ECO:0000244|PDB:3S24}.
STRAND 484 490 {ECO:0000244|PDB:3S24}.
STRAND 498 501 {ECO:0000244|PDB:3S24}.
HELIX 507 509 {ECO:0000244|PDB:3S24}.
STRAND 512 520 {ECO:0000244|PDB:3S24}.
STRAND 523 529 {ECO:0000244|PDB:3S24}.
HELIX 539 550 {ECO:0000244|PDB:3S24}.
HELIX 555 563 {ECO:0000244|PDB:3S24}.
SEQUENCE 597 AA; 68557 MW; 51CEEC1B190603DE CRC64;
MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK
MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE
LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI
EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG
VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL
IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT
SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG
LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR TDKSFPNAYN
TAMAVCNSIS NPVTKEMLFE FIDRCTAASQ GQKRKHHLDP DTELMPPPPP KRPRPLT


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