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Protein phosphatase 1B (EC 3.1.3.16) (Protein phosphatase 2C isoform beta) (PP2C-beta)

 PPM1B_HUMAN             Reviewed;         479 AA.
O75688; Q461Q2; Q4J6C1; Q4J6C2; Q658R4; Q96ER6; Q9HAY8;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
28-MAR-2018, entry version 184.
RecName: Full=Protein phosphatase 1B;
EC=3.1.3.16;
AltName: Full=Protein phosphatase 2C isoform beta;
Short=PP2C-beta;
Name=PPM1B; Synonyms=PP2CB;
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 BETA-1).
TISSUE=Liver;
PubMed=9684878; DOI=10.1016/S0014-5793(98)00708-X;
Marely A.E., Kline A., Crabtree G., Sullivan J.E., Beri R.K.;
"The cloning expression and tissue distribution of human PP2Cbeta.";
FEBS Lett. 431:121-124(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
PubMed=10934208; DOI=10.1074/jbc.M006210200;
Cheng A., Kaldis P., Solomon M.J.;
"Dephosphorylation of human cyclin-dependent kinases by protein
phosphatase type 2Calpha and beta2 isoforms.";
J. Biol. Chem. 275:34744-34749(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I.,
Smorodinsky N.I., Lavi S.;
"Protein phosphatase 1B. Cloning and characterization of two major
transcripts generated by alternative use of 3' exons.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-2; 4 AND 5).
PubMed=15913950; DOI=10.1016/j.ygeno.2005.04.001;
Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K.,
Hershkovitz E.;
"The 2p21 deletion syndrome: characterization of the transcription
content.";
Genomics 86:195-211(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
TISSUE=Stomach;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BETA-1 AND BETA-X).
TISSUE=Brain, and Urinary bladder;
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).
[10]
ISGYLATION AT LYS-12 AND LYS-142.
PubMed=16872604; DOI=10.1016/j.febslet.2006.07.032;
Takeuchi T., Kobayashi T., Tamura S., Yokosawa H.;
"Negative regulation of protein phosphatase 2Cbeta by ISG15
conjugation.";
FEBS Lett. 580:4521-4526(2006).
[11]
INTERACTION WITH PAK6.
PubMed=18642328; DOI=10.1002/pros.20787;
Kaur R., Yuan X., Lu M.L., Balk S.P.;
"Increased PAK6 expression in prostate cancer and identification of
PAK6 associated proteins.";
Prostate 68:1510-1516(2008).
[12]
FUNCTION, AND INTERACTION WITH IKBKB.
PubMed=18930133; DOI=10.1016/j.cellsig.2008.09.012;
Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K.,
Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.;
"PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-
induced IKKbeta-NF-kappaB activation.";
Cell. Signal. 21:95-102(2009).
[13]
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).
[14]
SUBCELLULAR LOCATION.
PubMed=22781750; DOI=10.1016/j.cellsig.2012.07.003;
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.;
"Protein phosphatase 5 modulates SMAD3 function in the transforming
growth factor-beta pathway.";
Cell. Signal. 24:1999-2006(2012).
[15]
FUNCTION.
PubMed=22750291; DOI=10.1016/j.cellsig.2012.06.017;
Zhao Y., Liang L., Fan Y., Sun S., An L., Shi Z., Cheng J., Jia W.,
Sun W., Mori-Akiyama Y., Zhang H., Fu S., Yang J.;
"PPM1B negatively regulates antiviral response via dephosphorylating
TBK1.";
Cell. Signal. 24:2197-2204(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[18]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297 IN COMPLEX WITH
MAGNESIUM.
PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
"Structural genomics of protein phosphatases.";
J. Struct. Funct. Genomics 8:121-140(2007).
-!- FUNCTION: Enzyme with a broad specificity. Dephosphorylates CDK2
and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits
TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-
172'. Plays an important role in the termination of TNF-alpha-
mediated NF-kappa-B activation through dephosphorylating and
inactivating IKBKB/IKKB. {ECO:0000269|PubMed:18930133,
ECO:0000269|PubMed:22750291}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- SUBUNIT: Monomer (By similarity). Interacts with PAK6. Interacts
with the phosphorylated form of IKBKB/IKKB. {ECO:0000250,
ECO:0000269|PubMed:18642328, ECO:0000269|PubMed:18930133}.
-!- INTERACTION:
P49407:ARRB1; NbExp=4; IntAct=EBI-1047039, EBI-743313;
P32121:ARRB2; NbExp=4; IntAct=EBI-1047039, EBI-714559;
P05161:ISG15; NbExp=2; IntAct=EBI-1047039, EBI-746466;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:22781750}. Membrane
{ECO:0000250|UniProtKB:P36993}; Lipid-anchor
{ECO:0000250|UniProtKB:P36993}. Note=Weakly associates at the
membrane and N-myristoylation mediates the membrane localization.
{ECO:0000250|UniProtKB:P36993}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=Beta-1; Synonyms=Beta-X, PPM1B2;
IsoId=O75688-1; Sequence=Displayed;
Name=Beta-2; Synonyms=PPM1B1;
IsoId=O75688-2; Sequence=VSP_005087, VSP_005088;
Name=Beta-X;
IsoId=O75688-3; Sequence=VSP_041085;
Name=4;
IsoId=O75688-4; Sequence=VSP_043643, VSP_043644, VSP_005088;
Name=5;
IsoId=O75688-5; Sequence=VSP_043641, VSP_043642, VSP_043644,
VSP_005088;
-!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle.
-!- PTM: Isgylation negatively regulates its activity.
{ECO:0000269|PubMed:16872604}.
-!- PTM: N-myristoylation is essential for the recognition of its
substrates for dephosphorylation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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EMBL; AJ005801; CAA06704.1; -; mRNA.
EMBL; AF294792; AAG02232.1; -; mRNA.
EMBL; AJ271832; CAC27992.1; -; mRNA.
EMBL; AJ271835; CAC27993.1; -; mRNA.
EMBL; DQ023508; AAY89639.1; -; mRNA.
EMBL; DQ023509; AAY89640.1; -; mRNA.
EMBL; DQ023510; AAY89641.1; -; mRNA.
EMBL; AF136972; AAG49433.1; -; mRNA.
EMBL; AL833035; CAH56319.1; -; mRNA.
EMBL; AC013717; AAX88954.1; -; Genomic_DNA.
EMBL; AC019129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAX00282.1; -; Genomic_DNA.
EMBL; CH471053; EAX00283.1; -; Genomic_DNA.
EMBL; BC012002; AAH12002.1; -; mRNA.
EMBL; BC064381; AAH64381.1; -; mRNA.
CCDS; CCDS1816.1; -. [O75688-2]
CCDS; CCDS1817.1; -. [O75688-1]
CCDS; CCDS1818.1; -. [O75688-3]
CCDS; CCDS46271.1; -. [O75688-4]
RefSeq; NP_001028729.1; NM_001033557.2. [O75688-4]
RefSeq; NP_002697.1; NM_002706.5. [O75688-1]
RefSeq; NP_808907.1; NM_177968.3. [O75688-2]
RefSeq; NP_808908.1; NM_177969.3. [O75688-3]
UniGene; Hs.416769; -.
PDB; 2P8E; X-ray; 1.82 A; A/B=2-297.
PDBsum; 2P8E; -.
ProteinModelPortal; O75688; -.
SMR; O75688; -.
BioGrid; 111490; 93.
IntAct; O75688; 38.
MINT; O75688; -.
STRING; 9606.ENSP00000282412; -.
BindingDB; O75688; -.
ChEMBL; CHEMBL2845; -.
DEPOD; O75688; -.
iPTMnet; O75688; -.
PhosphoSitePlus; O75688; -.
BioMuta; PPM1B; -.
EPD; O75688; -.
PaxDb; O75688; -.
PeptideAtlas; O75688; -.
PRIDE; O75688; -.
DNASU; 5495; -.
Ensembl; ENST00000282412; ENSP00000282412; ENSG00000138032. [O75688-1]
Ensembl; ENST00000345249; ENSP00000326089; ENSG00000138032. [O75688-3]
Ensembl; ENST00000378551; ENSP00000367813; ENSG00000138032. [O75688-2]
Ensembl; ENST00000409432; ENSP00000387287; ENSG00000138032. [O75688-4]
GeneID; 5495; -.
KEGG; hsa:5495; -.
UCSC; uc002rtt.4; human. [O75688-1]
CTD; 5495; -.
DisGeNET; 5495; -.
EuPathDB; HostDB:ENSG00000138032.20; -.
GeneCards; PPM1B; -.
HGNC; HGNC:9276; PPM1B.
HPA; HPA016745; -.
MalaCards; PPM1B; -.
MIM; 603770; gene.
neXtProt; NX_O75688; -.
OpenTargets; ENSG00000138032; -.
Orphanet; 163693; 2p21 microdeletion syndrome.
PharmGKB; PA33604; -.
eggNOG; KOG0697; Eukaryota.
eggNOG; COG0631; LUCA.
GeneTree; ENSGT00880000137909; -.
HOGENOM; HOG000233895; -.
HOVERGEN; HBG053647; -.
InParanoid; O75688; -.
KO; K04461; -.
OMA; ARVSAHC; -.
OrthoDB; EOG091G0AJQ; -.
PhylomeDB; O75688; -.
TreeFam; TF313590; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
SIGNOR; O75688; -.
ChiTaRS; PPM1B; human.
EvolutionaryTrace; O75688; -.
GeneWiki; PPM1B; -.
GenomeRNAi; 5495; -.
PRO; PR:O75688; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138032; -.
CleanEx; HS_PPM1B; -.
ExpressionAtlas; O75688; baseline and differential.
Genevisible; O75688; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0006499; P:N-terminal protein myristoylation; ISS:UniProtKB.
GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IMP:UniProtKB.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
CDD; cd00143; PP2Cc; 1.
Gene3D; 1.10.10.430; -; 1.
Gene3D; 3.60.40.10; -; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR000222; PP2C_BS.
InterPro; IPR012911; PP2C_C.
InterPro; IPR036580; PP2C_C_sf.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 1.
Pfam; PF07830; PP2C_C; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81601; SSF81601; 1.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS01032; PPM_1; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Isopeptide bond; Lipoprotein; Magnesium; Manganese;
Membrane; Metal-binding; Myristate; Phosphoprotein;
Protein phosphatase; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805}.
CHAIN 2 479 Protein phosphatase 1B.
/FTId=PRO_0000057746.
DOMAIN 23 295 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
METAL 60 60 Manganese 1. {ECO:0000250}.
METAL 60 60 Manganese 2. {ECO:0000244|PDB:2P8E,
ECO:0000269|PubMed:18058037}.
METAL 61 61 Manganese 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 243 243 Manganese 2. {ECO:0000244|PDB:2P8E,
ECO:0000269|PubMed:18058037}.
METAL 286 286 Manganese 2. {ECO:0000244|PDB:2P8E,
ECO:0000269|PubMed:18058037}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805}.
CROSSLNK 12 12 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
VAR_SEQ 1 287 Missing (in isoform Beta-X).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041085.
VAR_SEQ 322 327 EIMEKS -> GKTNAF (in isoform 5).
{ECO:0000303|PubMed:15913950}.
/FTId=VSP_043641.
VAR_SEQ 328 380 Missing (in isoform 5).
{ECO:0000303|PubMed:15913950}.
/FTId=VSP_043642.
VAR_SEQ 379 387 ASDEAEESG -> GAGDLEDPW (in isoform Beta-
2). {ECO:0000303|PubMed:10931946,
ECO:0000303|PubMed:10934208,
ECO:0000303|PubMed:15913950,
ECO:0000303|Ref.3}.
/FTId=VSP_005087.
VAR_SEQ 379 380 AS -> QK (in isoform 4).
{ECO:0000303|PubMed:15913950}.
/FTId=VSP_043643.
VAR_SEQ 381 387 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:15913950}.
/FTId=VSP_043644.
VAR_SEQ 388 479 Missing (in isoform Beta-2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:10931946,
ECO:0000303|PubMed:10934208,
ECO:0000303|PubMed:15913950,
ECO:0000303|Ref.3}.
/FTId=VSP_005088.
STRAND 9 19 {ECO:0000244|PDB:2P8E}.
STRAND 22 31 {ECO:0000244|PDB:2P8E}.
STRAND 33 35 {ECO:0000244|PDB:2P8E}.
STRAND 38 46 {ECO:0000244|PDB:2P8E}.
TURN 47 49 {ECO:0000244|PDB:2P8E}.
STRAND 50 63 {ECO:0000244|PDB:2P8E}.
HELIX 66 80 {ECO:0000244|PDB:2P8E}.
TURN 83 85 {ECO:0000244|PDB:2P8E}.
HELIX 99 118 {ECO:0000244|PDB:2P8E}.
TURN 121 123 {ECO:0000244|PDB:2P8E}.
STRAND 134 139 {ECO:0000244|PDB:2P8E}.
STRAND 141 151 {ECO:0000244|PDB:2P8E}.
STRAND 153 158 {ECO:0000244|PDB:2P8E}.
STRAND 161 165 {ECO:0000244|PDB:2P8E}.
HELIX 174 182 {ECO:0000244|PDB:2P8E}.
TURN 193 195 {ECO:0000244|PDB:2P8E}.
HELIX 205 207 {ECO:0000244|PDB:2P8E}.
HELIX 215 217 {ECO:0000244|PDB:2P8E}.
STRAND 218 221 {ECO:0000244|PDB:2P8E}.
STRAND 225 230 {ECO:0000244|PDB:2P8E}.
STRAND 235 241 {ECO:0000244|PDB:2P8E}.
HELIX 243 246 {ECO:0000244|PDB:2P8E}.
HELIX 251 262 {ECO:0000244|PDB:2P8E}.
HELIX 268 281 {ECO:0000244|PDB:2P8E}.
STRAND 288 294 {ECO:0000244|PDB:2P8E}.
SEQUENCE 479 AA; 52643 MW; A3A5797AD263DFBD CRC64;
MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD
GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF
SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI
QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL
ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK
VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR
NVIEAVYSRL NPHRESDGAS DEAEESGSQG KLVEALRQMR INHRGNYRQL LEEMLTSYRL
AKVEGEESPA EPAATATSSN SDAGNPVTMQ ESHTESESGL AELDSSNEDA GTKMSGEKI


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