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Centrosome-associated zinc finger protein CP190 (Protein enhancer of mod(mdg4)4-1) (dMAP190)

 CP190_DROME             Reviewed;        1096 AA.
Q24478; A4V2Y3; Q9VFA1;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
18-APR-2006, sequence version 2.
22-NOV-2017, entry version 150.
RecName: Full=Centrosome-associated zinc finger protein CP190;
AltName: Full=Protein enhancer of mod(mdg4)4-1;
AltName: Full=dMAP190;
Name=Cp190; Synonyms=E(mod)4-1; ORFNames=CG6384;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
STRAIN=Oregon-R;
PubMed=8586650;
Whitfield W.G.F., Chaplin M.A., Oegema K., Parry H., Glover D.M.;
"The 190 kDa centrosome-associated protein of Drosophila melanogaster
contains four zinc finger motifs and binds to specific sites on
polytene chromosomes.";
J. Cell Sci. 108:3377-3387(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH CP60, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=1372522; DOI=10.1091/mbc.3.1.1;
Kellogg D.R., Alberts B.M.;
"Purification of a multiprotein complex containing centrosomal
proteins from the Drosophila embryo by chromatography with low-
affinity polyclonal antibodies.";
Mol. Biol. Cell 3:1-11(1992).
[6]
INTERACTION WITH CP60 AND MICROTUBULES, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=8491775; DOI=10.1083/jcb.121.4.823;
Raff J.W., Kellogg D.R., Alberts B.M.;
"Drosophila gamma-tubulin is part of a complex containing two
previously identified centrosomal MAPs.";
J. Cell Biol. 121:823-835(1993).
[7]
INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
PubMed=8522588; DOI=10.1083/jcb.131.5.1261;
Oegema K., Whitfield W.G.F., Alberts B.M.;
"The cell cycle-dependent localization of the CP190 centrosomal
protein is determined by the coordinate action of two separable
domains.";
J. Cell Biol. 131:1261-1273(1995).
[8]
INTERACTION WITH CP60, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=8590797; DOI=10.1091/mbc.6.12.1673;
Kellogg D.R., Oegema K., Raff J., Schneider K., Alberts B.M.;
"CP60: a microtubule-associated protein that is localized to the
centrosome in a cell cycle-specific manner.";
Mol. Biol. Cell 6:1673-1684(1995).
[9]
SUBCELLULAR LOCATION.
PubMed=9247191;
Oegema K., Marshall W.F., Sedat J.W., Alberts B.M.;
"Two proteins that cycle asynchronously between centrosomes and
nuclear structures: Drosophila CP60 and CP190.";
J. Cell Sci. 110:1573-1583(1997).
[10]
TISSUE SPECIFICITY.
PubMed=9256351; DOI=10.1016/S0925-4773(97)00066-X;
Riparbelli M.G., Whitfield W.G.F., Dallai R., Callaini G.;
"Assembly of the zygotic centrosome in the fertilized Drosophila
egg.";
Mech. Dev. 65:135-144(1997).
[11]
INTERACTION WITH CP60.
PubMed=9700165; DOI=10.1083/jcb.142.3.775;
Moritz M., Zheng Y., Alberts B.M., Oegema K.;
"Recruitment of the gamma-tubulin ring complex to Drosophila salt-
stripped centrosome scaffolds.";
J. Cell Biol. 142:775-786(1998).
[12]
FUNCTION, INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
PubMed=14996941; DOI=10.1242/jcs.00979;
Butcher R.D.J., Chodagam S., Basto R., Wakefield J.G., Henderson D.S.,
Raff J.W., Whitfield W.G.F.;
"The Drosophila centrosome-associated protein CP190 is essential for
viability but not for cell division.";
J. Cell Sci. 117:1191-1199(2004).
[13]
SUBCELLULAR LOCATION.
PubMed=15479719; DOI=10.1242/jcs.01401;
Raynaud-Messina B., Mazzolini L., Moisand A., Cirinesi A.-M.,
Wright M.;
"Elongation of centriolar microtubule triplets contributes to the
formation of the mitotic spindle in gamma-tubulin-depleted cells.";
J. Cell Sci. 117:5497-5507(2004).
[14]
FUNCTION, DNA-BINDING, INTERACTION WITH MOD(MDG4) AND SU(HW), AND
SUBCELLULAR LOCATION.
PubMed=15574329; DOI=10.1016/j.molcel.2004.11.004;
Pai C.-Y., Lei E.P., Ghosh D., Corces V.G.;
"The centrosomal protein CP190 is a component of the gypsy chromatin
insulator.";
Mol. Cell 16:737-748(2004).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16051175; DOI=10.1016/j.cub.2005.06.024;
Chodagam S., Royou A., Whitfield W.G.F., Karess R., Raff J.W.;
"The centrosomal protein CP190 regulates myosin function during early
Drosophila development.";
Curr. Biol. 15:1308-1313(2005).
[16]
SUBCELLULAR LOCATION.
PubMed=16209949; DOI=10.1016/j.molcel.2005.08.031;
Capelson M., Corces V.G.;
"The ubiquitin ligase dTopors directs the nuclear organization of a
chromatin insulator.";
Mol. Cell 20:105-116(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-319; SER-920
AND SER-925, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-229; SER-233;
SER-298; THR-603; SER-610; SER-708; SER-723; THR-727; SER-745;
SER-748; SER-757; SER-760; THR-817; SER-920; SER-927; THR-936;
SER-938; SER-1071 AND SER-1074, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[19]
INTERACTION WITH INSV.
PubMed=25561495; DOI=10.1101/gad.252122.114;
Dai Q., Ren A., Westholm J.O., Duan H., Patel D.J., Lai E.C.;
"Common and distinct DNA-binding and regulatory activities of the BEN-
solo transcription factor family.";
Genes Dev. 29:48-62(2015).
-!- FUNCTION: Component of the gypsy chromatin insulator complex which
is required for the function of the gypsy chromatin insulator and
other endogenous chromatin insulators. Chromatin insulators are
regulatory elements which establish independent domains of
transcriptional activity within eukaryotic genomes. Insulators
have two defining properties; they can block the communication
between an enhancer and a promoter when placed between them and
can also buffer transgenes from position effect variegation (PEV).
Insulators are proposed to structure the chromatin fiber into
independent domains of differing transcriptional potential by
promoting the formation of distinct chromatin loops. This
chromatin looping may involve the formation of insulator bodies,
where homotypic interactions between individual subunits of the
insulator complex could promote the clustering of widely spaced
insulators at the nuclear periphery. Within the gypsy insulator
complex, this protein may directly bind to insulator DNA at sites
distinct from those recognized by su(Hw). Required during
embryogenesis for axial expansion, an actin/myosin dependent
process that distributes the dividing nuclei along the anterior-
posterior axis of the syncytial embryo. Does not appear to play a
crucial role in organizing centrosomal microtubules during
mitosis. {ECO:0000269|PubMed:14996941,
ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:16051175}.
-!- SUBUNIT: Component of the gypsy chromatin insulator complex,
composed of Cp190, mod(mdg4) and su(Hw). The gypsy chromatin
insulator complex interacts with Topors via mod(mdg4) and su(Hw).
Interacts with Cp60 and microtubules. Interacts with inv.
{ECO:0000269|PubMed:1372522, ECO:0000269|PubMed:14996941,
ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:25561495,
ECO:0000269|PubMed:8491775, ECO:0000269|PubMed:8522588,
ECO:0000269|PubMed:8590797, ECO:0000269|PubMed:9700165}.
-!- INTERACTION:
Q8TA44:CTCF; NbExp=5; IntAct=EBI-868840, EBI-466743;
Q9VHG5:Ibf1; NbExp=3; IntAct=EBI-868840, EBI-141691;
Q9VHG6:Ibf2; NbExp=3; IntAct=EBI-868840, EBI-157022;
Q86B87-1:mod(mdg4); NbExp=4; IntAct=EBI-868840, EBI-1433422;
P08970:su(Hw); NbExp=4; IntAct=EBI-868840, EBI-101373;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton.
Chromosome. Note=Nucleus in interphase. Colocalizes with other
elements of the gypsy chromatin insulator complex at multiple
sites on polytene chromosomes and at nuclear insulator bodies.
-!- TISSUE SPECIFICITY: Expressed in spermatids but not in mature
spermatozoa. Localizes within the spermatids to a sheath of
microtubules around the nucleus and to microtubules within the
tail. {ECO:0000269|PubMed:9256351}.
-!- DEVELOPMENTAL STAGE: Localizes to the centrosome throughout the
nuclear division cycle in early syncytial embryos. Localization to
the interphase nucleus is seen from nuclear cycle 9 onwards.
{ECO:0000269|PubMed:1372522, ECO:0000269|PubMed:8491775,
ECO:0000269|PubMed:8586650, ECO:0000269|PubMed:8590797}.
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EMBL; Z50021; CAA90324.1; -; mRNA.
EMBL; AE014297; AAF55159.1; -; Genomic_DNA.
EMBL; AE014297; AAN13643.1; -; Genomic_DNA.
EMBL; BT010090; AAQ22559.1; -; mRNA.
PIR; T13802; T13802.
RefSeq; NP_524359.2; NM_079635.3.
RefSeq; NP_731998.1; NM_169632.2.
UniGene; Dm.2423; -.
PDB; 4U77; X-ray; 2.03 A; A=1-134.
PDB; 5EUP; X-ray; 2.50 A; A=1-135.
PDBsum; 4U77; -.
PDBsum; 5EUP; -.
ProteinModelPortal; Q24478; -.
SMR; Q24478; -.
BioGrid; 66912; 57.
IntAct; Q24478; 15.
MINT; MINT-1899376; -.
STRING; 7227.FBpp0082580; -.
iPTMnet; Q24478; -.
PaxDb; Q24478; -.
PRIDE; Q24478; -.
EnsemblMetazoa; FBtr0083126; FBpp0082580; FBgn0000283.
EnsemblMetazoa; FBtr0083127; FBpp0082581; FBgn0000283.
GeneID; 41848; -.
KEGG; dme:Dmel_CG6384; -.
CTD; 41848; -.
FlyBase; FBgn0000283; Cp190.
eggNOG; KOG1181; Eukaryota.
eggNOG; ENOG4111M3T; LUCA.
InParanoid; Q24478; -.
OMA; INEAHTD; -.
OrthoDB; EOG091G027B; -.
PhylomeDB; Q24478; -.
SignaLink; Q24478; -.
GenomeRNAi; 41848; -.
PRO; PR:Q24478; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0000283; -.
Genevisible; Q24478; DM.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000793; C:condensed chromosome; IDA:FlyBase.
GO; GO:0005875; C:microtubule associated complex; ISS:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000242; C:pericentriolar material; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0043035; F:chromatin insulator sequence binding; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0031208; F:POZ domain binding; IDA:FlyBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0090202; P:gene looping; IMP:FlyBase.
GO; GO:0007017; P:microtubule-based process; ISS:FlyBase.
GO; GO:0035191; P:nuclear axial expansion; IMP:FlyBase.
GO; GO:0031937; P:positive regulation of chromatin silencing; IGI:FlyBase.
GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00651; BTB; 1.
SMART; SM00225; BTB; 1.
SMART; SM00355; ZnF_C2H2; 4.
SUPFAM; SSF54695; SSF54695; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS50097; BTB; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; DNA-binding; Metal-binding; Microtubule;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 1096 Centrosome-associated zinc finger protein
CP190.
/FTId=PRO_0000232629.
DOMAIN 30 97 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
ZN_FING 538 561 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 567 590 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 207 271 Nuclear localization.
REGION 385 508 Centrosomal localization and interaction
with microtubules.
MOD_RES 197 197 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 229 229 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 603 603 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 708 708 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 727 727 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 760 760 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 817 817 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 925 925 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 927 927 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 936 936 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 938 938 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1071 1071 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1074 1074 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 1061 1061 G -> D (in Ref. 1; CAA90324).
{ECO:0000305}.
HELIX 12 26 {ECO:0000244|PDB:4U77}.
STRAND 32 35 {ECO:0000244|PDB:4U77}.
STRAND 41 44 {ECO:0000244|PDB:4U77}.
HELIX 46 52 {ECO:0000244|PDB:4U77}.
HELIX 55 62 {ECO:0000244|PDB:4U77}.
STRAND 69 71 {ECO:0000244|PDB:4U77}.
HELIX 78 90 {ECO:0000244|PDB:4U77}.
HELIX 97 99 {ECO:0000244|PDB:4U77}.
HELIX 100 110 {ECO:0000244|PDB:4U77}.
HELIX 113 120 {ECO:0000244|PDB:4U77}.
SEQUENCE 1096 AA; 121679 MW; 5CD5C5492B948D39 CRC64;
MGEVKSVKVD NWGVFFLQKL QNFFNKTDYC DLTLQFRDNS QLKVHRLVLS ACTDYFNVLE
QTCEIVDDAL IMPNEFQADV VVPIVNFMYT GTLEFELKMY GKLLRTAKEM NMTVLLKLLE
AHRRTMENVN RQQRPPSPKG IRRRTVGQPS SGLPQQRVLG PSPQSRNVAT PIAQRANTQR
GSTGNTMSRT SGGSNRSPYG DSSNVKQEPT SPFEQLRKGY NNNKRPAQTS LLSPPSKKPS
LEEVKEFAEQ QRMRKQIAAE YGDNDPEYDG GMLYDDVHAG DDDDDDMPPQ PSTSKQQSPQ
GTQTQLEHGS TTIILKQDSP SQTPTIIVKD SSNAKLNHTK IIAEVLRQYP HIVKGHKNIK
LKIMPNTPAA PTEKSAPATV KPPANQSSAT TSPHKKLHVS FKADKSTPLI TAQQKAASSQ
QKSGTSQTTG NQGTGANPPA NTAAAQKRRI DSKTMHALIA QGAENTTGPW LCLRCGVNGR
PISIPSYRGF RRHLINTHKE TIDPALCEHC GWRSVNNREL HFHMYMEHQT KSLLYTFAEC
ALCNQSYRTK GELEAHINEV HTDDNKQQCI YCNKVFEQEL QLYRHMKSYH KEQALEDGII
DETDEEFLGS QDEEEEAEGD EEQEPEQTGK VRILSDISLP ATSAITVQQA QQEQLQEEDV
EQVQQEVKFV GADGNEVELT DEQRKEILSQ LNQQQAGATA GGVVMVLSEP EAEHVKQETD
EKSLAGTEEE YDDSQIYSEL GAADSVESAK KNIADESKES IDNLEWAENL IAESEEQSNK
EPKSDKPRDD ISEKLKELTG DWTEDENDDD VDDKPATAEL ASELANKDPE PTVHEEEDDI
DLALQSLHKG PEEATEEKAS EESVTSADDA VDAVPNINSQ PEKMDVDSEA ADEKASKAEV
QIKKEAELEN DQEEFIKEDS PIPHSDSVAE LREAVTASEG EDDVHLEADN IRKELLDELI
AEAEKPDQEK DIVQSEENAT TEALDRSVTD EDDLVPPTQV STEQMEIDEP AAEKAAENNE
DTRTADEKEA VEDKPNQTQD VTTAEKPTLE SAKAGDEATS GEAASVDKVK SLISEWGDDD
EDEDENGVSA AAKEEL


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