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PAB-dependent poly(A)-specific ribonuclease subunit PAN2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-nuclease) (PAN deadenylation complex catalytic subunit 2)

 PAN2_YEAST              Reviewed;        1115 AA.
P53010; D6VU51;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 160.
RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000305};
EC=3.1.13.4 {ECO:0000255|HAMAP-Rule:MF_03182};
AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03182};
AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
Short=PAN deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
Name=PAN2 {ECO:0000255|HAMAP-Rule:MF_03182};
OrderedLocusNames=YGL094C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
FUNCTION.
PubMed=8550599; DOI=10.1074/jbc.271.1.432;
Boeck R., Tarun S.Z. Jr., Rieger M., Deardorff J.A., Mueller-Auer S.,
Sachs A.B.;
"The yeast Pan2 protein is required for poly(A)-binding protein-
stimulated poly(A)-nuclease activity.";
J. Biol. Chem. 271:432-438(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9290212;
DOI=10.1002/(SICI)1097-0061(19970915)13:11<1077::AID-YEA152>3.3.CO;2-P;
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
chromosome VII.";
Yeast 13:1077-1090(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 489-504.
PubMed=1339314; DOI=10.1016/0092-8674(92)90246-9;
Sachs A.B., Deardorff J.A.;
"Translation initiation requires the PAB-dependent poly(A)
ribonuclease in yeast.";
Cell 70:961-973(1992).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=1358757; DOI=10.1101/gad.6.11.2088;
Lowell J.E., Rudner D.Z., Sachs A.B.;
"3'-UTR-dependent deadenylation by the yeast poly(A) nuclease.";
Genes Dev. 6:2088-2099(1992).
[7]
FUNCTION, INTERACTION WITH PAN3, AND ENZYME REGULATION.
PubMed=8816488; DOI=10.1128/MCB.16.10.5744;
Brown C.E., Tarun S.Z. Jr., Boeck R., Sachs A.B.;
"PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 16:5744-5753(1996).
[8]
FUNCTION.
PubMed=9774670; DOI=10.1128/MCB.18.11.6548;
Brown C.E., Sachs A.B.;
"Poly(A) tail length control in Saccharomyces cerevisiae occurs by
message-specific deadenylation.";
Mol. Cell. Biol. 18:6548-6559(1998).
[9]
FUNCTION.
PubMed=11239395; DOI=10.1016/S0092-8674(01)00225-2;
Tucker M., Valencia-Sanchez M.A., Staples R.R., Chen J., Denis C.L.,
Parker R.;
"The transcription factor associated Ccr4 and Caf1 proteins are
components of the major cytoplasmic mRNA deadenylase in Saccharomyces
cerevisiae.";
Cell 104:377-386(2001).
[10]
FUNCTION.
PubMed=11953437; DOI=10.1074/jbc.M202473200;
Hammet A., Pike B.L., Heierhorst J.;
"Posttranscriptional regulation of the RAD5 DNA repair gene by the
Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to
survival of replication blocks.";
J. Biol. Chem. 277:22469-22474(2002).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
ENZYME REGULATION.
PubMed=15121841; DOI=10.1128/MCB.24.10.4196-4206.2004;
Mangus D.A., Smith M.M., McSweeney J.M., Jacobson A.;
"Identification of factors regulating poly(A) tail synthesis and
maturation.";
Mol. Cell. Biol. 24:4196-4206(2004).
[14]
INTERACTION WITH PAN3.
PubMed=15169912; DOI=10.1128/MCB.24.12.5521-5533.2004;
Mangus D.A., Evans M.C., Agrin N.S., Smith M.M., Gongidi P.,
Jacobson A.;
"Positive and negative regulation of poly(A) nuclease.";
Mol. Cell. Biol. 24:5521-5533(2004).
[15]
FUNCTION.
PubMed=15630021; DOI=10.1101/gad.1267005;
Dunn E.F., Hammell C.M., Hodge C.A., Cole C.N.;
"Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease
complex recruited by Pab1, connect mRNA biogenesis to export.";
Genes Dev. 19:90-103(2005).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15894541; DOI=10.1074/jbc.M504720200;
Dheur S., Nykamp K.R., Viphakone N., Swanson M.S.,
Minvielle-Sebastia L.;
"Yeast mRNA poly(A) tail length control can be reconstituted in vitro
in the absence of Pab1p-dependent poly(A) nuclease activity.";
J. Biol. Chem. 280:24532-24538(2005).
[17]
ENZYME REGULATION.
PubMed=16940550; DOI=10.1261/rna.241006;
Hilgers V., Teixeira D., Parker R.;
"Translation-independent inhibition of mRNA deadenylation during
stress in Saccharomyces cerevisiae.";
RNA 12:1835-1845(2006).
[18]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-912.
PubMed=24872509; DOI=10.15252/embj.201488373;
Wolf J., Valkov E., Allen M.D., Meineke B., Gordiyenko Y.,
McLaughlin S.H., Olsen T.M., Robinson C.V., Bycroft M., Stewart M.,
Passmore L.A.;
"Structural basis for Pan3 binding to Pan2 and its function in mRNA
recruitment and deadenylation.";
EMBO J. 33:1514-1526(2014).
[19]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 340-1115 IN COMPLEX WITH
PAN3, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF
ASP-1020.
PubMed=24880344; DOI=10.1038/nsmb.2834;
Schaefer I.B., Rode M., Bonneau F., Schuessler S., Conti E.;
"The structure of the Pan2-Pan3 core complex reveals cross-talk
between deadenylase and pseudokinase.";
Nat. Struct. Mol. Biol. 21:591-598(2014).
-!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN)
deadenylation complex, one of two cytoplasmic mRNA deadenylases
involved in mRNA turnover. PAN specifically shortens poly(A) tails
of RNA and the activity is stimulated by poly(A)-binding protein
PAB1. PAN deadenylation is followed by rapid degradation of the
shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs
are then degraded by two alternative mechanisms, namely exosome-
mediated 3'-5' exonucleolytic degradation, or deadenlyation-
dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3'
exonucleolytic degradation by XRN1. May also be involved in post-
transcriptional maturation of mRNA poly(A) tails, trimming the
tails from their synthesized length to the slightly shorter,
apparently messenger-specific length found on newly exported
mRNAs. PAN cooperates with protein kinase DUN1 in the regulation
of RAD5 mRNA levels and cell survival in response to replicational
stress. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:11239395, ECO:0000269|PubMed:11953437,
ECO:0000269|PubMed:1358757, ECO:0000269|PubMed:15630021,
ECO:0000269|PubMed:15894541, ECO:0000269|PubMed:24880344,
ECO:0000269|PubMed:8550599, ECO:0000269|PubMed:8816488,
ECO:0000269|PubMed:9774670}.
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage of poly(A) to 5'-AMP.
{ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:1358757,
ECO:0000269|PubMed:24880344}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:24880344};
Note=Binds 2 metal cations per subunit in the catalytic
exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:24880344};
-!- ENZYME REGULATION: Positively regulated by the regulatory subunit
PAN3. Negatively regulated by PAB1-binding protein PBP1. Inhibited
under stress conditions. Inhibition of deadenylation under stress
increases mRNA stability, which may be a mechanism to retain the
majority of the cytoplasmic pool of mRNAs for later reuse and
recovery from stress. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:15121841, ECO:0000269|PubMed:16940550,
ECO:0000269|PubMed:8816488}.
-!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
regulatory subunit PAN3 to form the poly(A)-nuclease (PAN)
deadenylation complex. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:15169912, ECO:0000269|PubMed:24872509,
ECO:0000269|PubMed:24880344, ECO:0000269|PubMed:8816488}.
-!- INTERACTION:
P36102:PAN3; NbExp=9; IntAct=EBI-12887, EBI-12895;
O94742:SEM1; NbExp=4; IntAct=EBI-12887, EBI-31337;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15894541}.
-!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal
hydrolase (UCH)-like or ubiquitin specific protease (USP)-like
domain is predicted to be catalytically inactive because it lacks
the active site catalytic triad characteristic of thiol proteases,
with residues at the equivalent structural positions that are
incompatible with catalysis, and it cannot bind ubiquitin. It
functions as a structural scaffold for intra- and intermolecular
interactions in the complex. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:24880344}.
-!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the
WD40 repeats and the pseudo-UCH domain mediates interaction with
PAN3. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000269|PubMed:24872509}.
-!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03182}.
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EMBL; U39204; AAC49152.1; -; Genomic_DNA.
EMBL; Z72616; CAA96800.1; -; Genomic_DNA.
EMBL; BK006941; DAA08012.1; -; Genomic_DNA.
PIR; S64101; S64101.
RefSeq; NP_011421.1; NM_001180959.1.
PDB; 4Q8G; X-ray; 2.10 A; A/B=416-870.
PDB; 4Q8H; X-ray; 3.10 A; A=460-1115.
PDB; 4XR7; X-ray; 3.80 A; A/D/G/J=340-1115.
PDBsum; 4Q8G; -.
PDBsum; 4Q8H; -.
PDBsum; 4XR7; -.
ProteinModelPortal; P53010; -.
SMR; P53010; -.
BioGrid; 33157; 119.
DIP; DIP-2466N; -.
IntAct; P53010; 11.
MINT; MINT-637100; -.
STRING; 4932.YGL094C; -.
iPTMnet; P53010; -.
MaxQB; P53010; -.
PRIDE; P53010; -.
EnsemblFungi; YGL094C; YGL094C; YGL094C.
GeneID; 852786; -.
KEGG; sce:YGL094C; -.
EuPathDB; FungiDB:YGL094C; -.
SGD; S000003062; PAN2.
GeneTree; ENSGT00390000013978; -.
HOGENOM; HOG000230585; -.
InParanoid; P53010; -.
KO; K12571; -.
OMA; MVYDLRM; -.
OrthoDB; EOG092C0KHR; -.
BioCyc; YEAST:G3O-30594-MONOMER; -.
PRO; PR:P53010; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0000932; C:P-body; IBA:GO_Central.
GO; GO:0031251; C:PAN complex; IDA:SGD.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:SGD.
GO; GO:0006301; P:postreplication repair; IGI:SGD.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_03182; PAN2; 1.
InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
InterPro; IPR030843; PAN2.
InterPro; IPR028881; PAN2_dom.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR012337; RNaseH-like_dom.
InterPro; IPR028889; USP_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
Pfam; PF00929; RNase_T; 1.
Pfam; PF13423; UCH_1; 1.
SMART; SM00479; EXOIII; 1.
SUPFAM; SSF50998; SSF50998; 2.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Exonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease;
Reference proteome; Repeat; WD repeat.
CHAIN 1 1115 PAN2-PAN3 deadenylation complex catalytic
subunit PAN2.
/FTId=PRO_0000058222.
REPEAT 27 66 WD 1. {ECO:0000255|HAMAP-Rule:MF_03182}.
REPEAT 112 153 WD 2. {ECO:0000255|HAMAP-Rule:MF_03182}.
REPEAT 155 194 WD 3. {ECO:0000255|HAMAP-Rule:MF_03182}.
REPEAT 197 236 WD 4. {ECO:0000255|HAMAP-Rule:MF_03182}.
REPEAT 295 334 WD 5. {ECO:0000255|HAMAP-Rule:MF_03182}.
DOMAIN 474 855 USP. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000305|PubMed:24880344}.
DOMAIN 907 1079 Exonuclease. {ECO:0000255|HAMAP-
Rule:MF_03182}.
REGION 337 473 Linker. {ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000305|PubMed:24880344}.
METAL 660 660 Zinc. {ECO:0000244|PDB:4Q8G,
ECO:0000269|PubMed:24880344}.
METAL 662 662 Zinc; via pros nitrogen.
{ECO:0000244|PDB:4Q8G,
ECO:0000269|PubMed:24880344}.
METAL 713 713 Zinc. {ECO:0000244|PDB:4Q8G,
ECO:0000269|PubMed:24880344}.
METAL 716 716 Zinc. {ECO:0000244|PDB:4Q8G,
ECO:0000269|PubMed:24880344}.
METAL 910 910 Divalent metal cation; catalytic.
{ECO:0000250|UniProtKB:O95453,
ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000305|PubMed:24880344}.
METAL 912 912 Divalent metal cation; catalytic.
{ECO:0000250|UniProtKB:O95453,
ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000305|PubMed:24880344}.
METAL 1020 1020 Divalent metal cation; catalytic.
{ECO:0000250|UniProtKB:O95453,
ECO:0000255|HAMAP-Rule:MF_03182}.
METAL 1071 1071 Divalent metal cation; catalytic.
{ECO:0000250|UniProtKB:O95453,
ECO:0000255|HAMAP-Rule:MF_03182,
ECO:0000305|PubMed:24880344}.
MUTAGEN 912 912 E->A: Abolishes nuclease activity.
{ECO:0000269|PubMed:24872509}.
MUTAGEN 1020 1020 D->A: Abolishes nuclease activity.
{ECO:0000269|PubMed:24880344}.
TURN 460 465 {ECO:0000244|PDB:4Q8H}.
HELIX 477 479 {ECO:0000244|PDB:4Q8G}.
HELIX 488 490 {ECO:0000244|PDB:4Q8G}.
HELIX 497 499 {ECO:0000244|PDB:4Q8G}.
STRAND 502 504 {ECO:0000244|PDB:4Q8G}.
TURN 512 515 {ECO:0000244|PDB:4Q8G}.
HELIX 516 524 {ECO:0000244|PDB:4Q8G}.
HELIX 527 536 {ECO:0000244|PDB:4Q8G}.
HELIX 546 559 {ECO:0000244|PDB:4Q8G}.
STRAND 560 562 {ECO:0000244|PDB:4Q8G}.
HELIX 568 576 {ECO:0000244|PDB:4Q8G}.
HELIX 595 600 {ECO:0000244|PDB:4Q8H}.
TURN 603 605 {ECO:0000244|PDB:4Q8H}.
STRAND 610 613 {ECO:0000244|PDB:4Q8H}.
HELIX 618 636 {ECO:0000244|PDB:4Q8G}.
STRAND 637 639 {ECO:0000244|PDB:4Q8G}.
HELIX 643 648 {ECO:0000244|PDB:4Q8G}.
STRAND 650 657 {ECO:0000244|PDB:4Q8G}.
STRAND 659 661 {ECO:0000244|PDB:4Q8G}.
STRAND 666 675 {ECO:0000244|PDB:4Q8G}.
HELIX 696 703 {ECO:0000244|PDB:4Q8G}.
STRAND 704 712 {ECO:0000244|PDB:4Q8G}.
TURN 714 716 {ECO:0000244|PDB:4Q8G}.
STRAND 719 728 {ECO:0000244|PDB:4Q8G}.
STRAND 733 739 {ECO:0000244|PDB:4Q8G}.
HELIX 743 751 {ECO:0000244|PDB:4Q8G}.
STRAND 752 754 {ECO:0000244|PDB:4Q8H}.
STRAND 758 765 {ECO:0000244|PDB:4Q8G}.
STRAND 768 774 {ECO:0000244|PDB:4Q8G}.
HELIX 775 777 {ECO:0000244|PDB:4Q8G}.
STRAND 782 797 {ECO:0000244|PDB:4Q8G}.
STRAND 803 813 {ECO:0000244|PDB:4Q8G}.
TURN 814 817 {ECO:0000244|PDB:4Q8G}.
STRAND 818 825 {ECO:0000244|PDB:4Q8G}.
STRAND 828 832 {ECO:0000244|PDB:4Q8G}.
HELIX 834 838 {ECO:0000244|PDB:4Q8G}.
STRAND 845 854 {ECO:0000244|PDB:4Q8G}.
HELIX 857 859 {ECO:0000244|PDB:4Q8G}.
HELIX 865 867 {ECO:0000244|PDB:4Q8H}.
HELIX 873 876 {ECO:0000244|PDB:4Q8H}.
HELIX 897 899 {ECO:0000244|PDB:4Q8H}.
STRAND 906 915 {ECO:0000244|PDB:4Q8H}.
STRAND 937 946 {ECO:0000244|PDB:4Q8H}.
STRAND 948 950 {ECO:0000244|PDB:4Q8H}.
TURN 951 954 {ECO:0000244|PDB:4Q8H}.
STRAND 956 962 {ECO:0000244|PDB:4Q8H}.
HELIX 973 976 {ECO:0000244|PDB:4Q8H}.
STRAND 983 986 {ECO:0000244|PDB:4Q8H}.
TURN 988 990 {ECO:0000244|PDB:4Q8H}.
TURN 994 996 {ECO:0000244|PDB:4Q8H}.
HELIX 997 1008 {ECO:0000244|PDB:4Q8H}.
STRAND 1011 1013 {ECO:0000244|PDB:4Q8H}.
HELIX 1017 1024 {ECO:0000244|PDB:4Q8H}.
HELIX 1030 1032 {ECO:0000244|PDB:4Q8H}.
HELIX 1036 1039 {ECO:0000244|PDB:4Q8H}.
HELIX 1049 1056 {ECO:0000244|PDB:4Q8H}.
HELIX 1068 1087 {ECO:0000244|PDB:4Q8H}.
HELIX 1091 1105 {ECO:0000244|PDB:4Q8H}.
SEQUENCE 1115 AA; 127039 MW; 4F91B737F761AE5A CRC64;
MNNWQHFFNN PVDLSEHLKK PYFRFDNRDK EITAISFDEK ANLIWSGDSY GCISSYDPTF
QLYTRYRGHI GGNSVKDILS HRDGILSISE DSLHFANRRG VTKLNLTSID IAAFSELNTM
CYSPHSLKNN IYCGGDNTNW GIASIDLNRG CLDSLLNYSS KVKLMCSNNK VLSIGRQTGT
VDLLDPTSNR TIKSFNAHSA SISAMDLRDN TLVTVGKSKR FYNLYADPFV NVYDLRTMRQ
LPPVSFSKGT TMGSGGADFV QLHPLLPTVM IVASSSGSFD FIDLSNPTLR TQYVHPCQSI
KKLCLSPNGD VLGILEADNH LDTWRRSSNN MGMFTNTPEM LAYPDYFNDI TSDGPISVDD
ETYPLSSVGM PYYLDKLLSA WPPVVFKSEG TIPQLTGKSP LPSSGKLKSN LAVISSQNEK
LSTQEFPLLR YDRTKYGMRN AIPDYVCLRD IRKQITSGLE TSDIQTYTSI NKYEVPPAYS
RLPLTSGRFG TDNFDFTPFN NTEYSGLDPD VDNHYTNAII QLYRFIPEMF NFVVGCLKDE
NFETTLLTDL GYLFDMMERS HGKICSSSNF QASLKSLTDK RQLENGEPQE HLEEYLESLC
IRESIEDFNS SESIKRNMPQ KFNRFLLSQL IKEEAQTVNH NITLNQCFGL ETEIRTECSC
DHYDTTVKLL PSLSISGINK TVIKQLNKKS NGQNILPYIE YAMKNVTQKN SICPTCGKTE
TITQECTVKN LPSVLSLELS LLDTEFSNIR SSKNWLTSEF YGSIIKNKAV LRSTASELKG
TSHIFKYELN GYVAKITDNN NETRLVTYVK KYNPKENCFK WLMFNDYLVV EITEEEALKM
TYPWKTPEII IYCDAEELRK PFFSVDTYSI NYDILFRDYF ANGIRDTARR EYKLLTHDEA
PKSGTLVAID AEFVSLQSEL CEIDHQGIRS IIRPKRTALA RISIIRGEEG ELYGVPFVDD
YVVNTNHIED YLTRYSGILP GDLDPEKSTK RLVRRNVVYR KVWLLMQLGC VFVGHGLNND
FKHININVPR NQIRDTAIYF LQGKRYLSLR YLAYVLLGMN IQEGNHDSIE DAHTALILYK
KYLHLKEKAI FEKVLNSVYE EGRAHNFKVP ETSKG


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