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Protein cup (Oskar ribonucleoprotein complex 147 kDa subunit)

 CUP_DROME               Reviewed;        1117 AA.
Q9VMA3; O02432;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 3.
12-SEP-2018, entry version 143.
RecName: Full=Protein cup;
AltName: Full=Oskar ribonucleoprotein complex 147 kDa subunit;
Name=cup; Synonyms=fs(2)cup; ORFNames=CG11181;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Ovary;
PubMed=9118812;
Keyes L.N., Spradling A.C.;
"The Drosophila gene fs(2)cup interacts with otu to define a
cytoplasmic pathway required for the structure and function of germ-
line chromosomes.";
Development 124:1419-1431(1997).
[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;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
INTERACTION WITH NOS.
PubMed=11060247;
Verrotti A.C., Wharton R.P.;
"Nanos interacts with cup in the female germline of Drosophila.";
Development 127:5225-5232(2000).
[6]
IDENTIFICATION IN THE OSK RNP COMPLEX.
PubMed=10662770; DOI=10.1083/jcb.148.3.427;
Wilhelm J.E., Mansfield J., Hom-Booher N., Wang S., Turck C.W.,
Hazelrigg T., Vale R.D.;
"Isolation of a ribonucleoprotein complex involved in mRNA
localization in Drosophila oocytes.";
J. Cell Biol. 148:427-440(2000).
[7]
FUNCTION, AND INTERACTION WITH BTZ AND EIF-4E.
PubMed=14691132; DOI=10.1083/jcb.200309088;
Wilhelm J.E., Hilton M., Amos Q., Henzel W.J.;
"Cup is an eIF4E binding protein required for both the translational
repression of oskar and the recruitment of Barentsz.";
J. Cell Biol. 163:1197-1204(2003).
[8]
FUNCTION, INTERACTION WITH ARET AND EIF-4E, AND MUTAGENESIS OF TYR-327
AND 332-LEU-MET-333.
PubMed=14723848; DOI=10.1016/S1534-5807(03)00400-3;
Nakamura A., Sato K., Hanyu-Nakamura K.;
"Drosophila Cup is an eIF4E binding protein that associates with Bruno
and regulates oskar mRNA translation in oogenesis.";
Dev. Cell 6:69-78(2004).
[9]
FUNCTION, INTERACTION WITH SMG AND EIF-4E, AND MUTAGENESIS OF TYR-327;
LEU-364 AND LEU-368.
PubMed=14685270; DOI=10.1038/sj.emboj.7600026;
Nelson M.R., Leidal A.M., Smibert C.A.;
"Drosophila Cup is an eIF4E-binding protein that functions in Smaug-
mediated translational repression.";
EMBO J. 23:150-159(2004).
[10]
FUNCTION, INTERACTION WITH EIF-4E, AND SUBCELLULAR LOCATION.
PubMed=15465908; DOI=10.1073/pnas.0406451101;
Zappavigna V., Piccioni F., Villaescusa J.C., Verrotti A.C.;
"Cup is a nucleocytoplasmic shuttling protein that interacts with the
eukaryotic translation initiation factor 4E to modulate Drosophila
ovary development.";
Proc. Natl. Acad. Sci. U.S.A. 101:14800-14805(2004).
[11]
FUNCTION, INTERACTION WITH NUP154, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=17277377; DOI=10.1534/genetics.106.062844;
Grimaldi M.R., Cozzolino L., Malva C., Graziani F., Gigliotti S.;
"nup154 genetically interacts with cup and plays a cell-type-specific
function during Drosophila melanogaster egg-chamber development.";
Genetics 175:1751-1759(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-270; SER-347;
SER-350; THR-503; SER-509; SER-513; SER-520; SER-523 AND SER-524, 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).
[13]
FUNCTION, AND IDENTIFICATION IN THE NOS RNP COMPLEX.
PubMed=21081899; DOI=10.1038/emboj.2010.283;
Jeske M., Moritz B., Anders A., Wahle E.;
"Smaug assembles an ATP-dependent stable complex repressing nanos mRNA
translation at multiple levels.";
EMBO J. 30:90-103(2011).
[14]
FUNCTION, AND INTERACTION WITH EIF-4E; ME31B AND TRAL.
PubMed=21937713; DOI=10.1101/gad.17136311;
Igreja C., Izaurralde E.;
"CUP promotes deadenylation and inhibits decapping of mRNA targets.";
Genes Dev. 25:1955-1967(2011).
[15]
FUNCTION, INTERACTION WITH ORB, AND DISRUPTION PHENOTYPE.
PubMed=22164257; DOI=10.1371/journal.pone.0028261;
Wong L.C., Schedl P.;
"Cup blocks the precocious activation of the orb autoregulatory
loop.";
PLoS ONE 6:E28261-E28261(2011).
[16]
FUNCTION, INTERACTION WITH OSK; VAS AND CCR4-NOT COMPLEX, SUBCELLULAR
LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=22454519; DOI=10.1242/jcs.095208;
Ottone C., Gigliotti S., Giangrande A., Graziani F.,
Verrotti di Pianella A.;
"The translational repressor Cup is required for germ cell development
in Drosophila.";
J. Cell Sci. 125:3114-3123(2012).
-!- FUNCTION: Adapter protein that plays a central role in
localization of transcripts in the oocyte and in young embryos
(PubMed:9118812). Maintains RNA targets in a repressed state by
promoting their deadenylation and protects deadenylated mRNAs from
further degradation (PubMed:21937713). Binds to and recruits eIF-
4E to the 3'-UTR of some mRNA targets which prevents interaction
between eIF4E1 and eIF4G (PubMed:14685270, PubMed:15465908,
PubMed:21081899). This may contribute to translational repression
but does not appear to be necessary for it to occur
(PubMed:21081899). Can promote translational repression
independently of deadenylation and eIF4E1 binding
(PubMed:21937713). Required for correct localization of eIF4E1 in
the developing oocyte (PubMed:15465908). Required for
translational repression of oskar (osk) mRNA (PubMed:14691132,
PubMed:14723848). Also required for the translational repression
of nanos (nos) mRNA (PubMed:21081899). Promotes the accumulation
of the germ plasm components osk, vas and stau at the posterior
pole of the oocyte and is required for germ cell development
(PubMed:22454519, PubMed:17277377). Represses orb positive
autoregulatory activity which prevents premature activation of orb
and ensures its accumulation specifically in the developing oocyte
(PubMed:22164257). {ECO:0000269|PubMed:14685270,
ECO:0000269|PubMed:14691132, ECO:0000269|PubMed:14723848,
ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:21081899,
ECO:0000269|PubMed:21937713, ECO:0000269|PubMed:22164257,
ECO:0000269|PubMed:22454519, ECO:0000269|PubMed:9118812,
ECO:0000303|PubMed:21937713}.
-!- SUBUNIT: Interacts with nos (PubMed:11060247). Interacts with smg
(PubMed:14685270). Interacts with eIF4E1; the interaction promotes
retention of cup in the cytoplasm (PubMed:14723848,
PubMed:14685270, PubMed:15465908, PubMed:21937713). Component of
the osk RNP complex, which is composed of at least exu, yps,
aret/bruno, cup, and the mRNA of osk (PubMed:10662770). Interacts
with the decapping activators me31B and tral (PubMed:21937713).
Component of the nos RNP complex, which is composed of at least
smg, cup, tral, me31B, the CCR4-NOT complex members Rga/NOT2 and
Caf1, and the mRNA of nos (PubMed:21081899). Interacts with btz
(PubMed:14691132, PubMed:14723848). Recruited to the 3'-UTR of nos
and osk mRNAs by smg and btz, respectively (PubMed:14685270,
PubMed:14691132). Interacts with orb; the interaction represses
the orb positive autoregulatory loop (PubMed:22164257). Interacts
with osk and vas (PubMed:22454519). Interacts with Pop2,
twin/CCR4, Rga, Not3 and Not1 which are all core components of the
CCR4-NOT deadenylase complex; interaction with the complex is
required for cup deadenylation activity (PubMed:21937713).
Interacts with Nup154 (PubMed:17277377).
{ECO:0000269|PubMed:10662770, ECO:0000269|PubMed:11060247,
ECO:0000269|PubMed:14685270, ECO:0000269|PubMed:14691132,
ECO:0000269|PubMed:14723848, ECO:0000269|PubMed:17277377,
ECO:0000269|PubMed:21081899, ECO:0000269|PubMed:21937713,
ECO:0000269|PubMed:22164257, ECO:0000269|PubMed:22454519}.
-!- INTERACTION:
P48598:eIF4E1; NbExp=6; IntAct=EBI-95398, EBI-198574;
P23128:me31B; NbExp=3; IntAct=EBI-95398, EBI-300281;
Q23972:smg; NbExp=4; IntAct=EBI-95398, EBI-108638;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465908,
ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:9118812}. Nucleus
{ECO:0000269|PubMed:15465908}. Note=Retained in the cytoplasm by
interaction with eIF4E1. Located throughout the cytoplasm of all
germline cells and is excluded from the nucleus of nurse cells,
oocytes and follicular cells (PubMed:15465908). During oogenesis,
accumulates in the cytoplasm at the posterior end of the forming
oocyte (PubMed:15465908). Component of the germ plasm in
developing oocytes (PubMed:22454519).
{ECO:0000269|PubMed:15465908, ECO:0000269|PubMed:22454519}.
-!- TISSUE SPECIFICITY: Predominantly expressed in ovaries and in 0-2
hours old embryos. Weakly expressed in testis. Expressed in young
embryos through stage 9, then it decreases throughout the rest of
embryogenesis. In ovaries, it is expressed in germ cells
throughout pre-vitellogenic development, but is not expressed in
the somatic follicle cells. In germarial cysts, the protein (and
not the transcripts) is transported selectively into the oocyte.
{ECO:0000269|PubMed:9118812}.
-!- DEVELOPMENTAL STAGE: Expressed in the egg chamber and more
specifically in nurse cells (at protein level) (PubMed:17277377).
Expressed both maternally and zygotically (PubMed:9118812).
Expressed throughout embryogenesis (PubMed:22454519). In stage 2,
uniformly distributed throughout the whole embryo
(PubMed:22454519). During blastoderm formation, concentrated at
the posterior pole to become incorporated into newly formed germ
cells (PubMed:22454519). Subsequently accumulates specifically in
the pole cells at stage 10, when they migrate through the
posterior midgut primordium, and during stage 14, when the germ
cells reach their final destination (PubMed:22454519).
{ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:22454519,
ECO:0000269|PubMed:9118812}.
-!- DISRUPTION PHENOTYPE: Mislocalization and precocious expression of
orb in the ovary, accumulation of high levels of orb in nurse
cells, elongation of orb poly-A tails, hyperphosphorylation of orb
and reduced osk mRNA levels (PubMed:22164257). Reduced number of
germ cells (PubMed:22454519). {ECO:0000269|PubMed:22164257,
ECO:0000269|PubMed:22454519}.
-!- SEQUENCE CAUTION:
Sequence=AAB64427.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAL39852.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF004917; AAB64427.1; ALT_INIT; mRNA.
EMBL; AE014134; AAF52418.3; -; Genomic_DNA.
EMBL; AY069707; AAL39852.1; ALT_INIT; mRNA.
RefSeq; NP_001285687.1; NM_001298758.1.
RefSeq; NP_523493.3; NM_078769.3.
UniGene; Dm.333; -.
PDB; 4AXG; X-ray; 2.80 A; C/D=296-425.
PDBsum; 4AXG; -.
ProteinModelPortal; Q9VMA3; -.
SMR; Q9VMA3; -.
BioGrid; 60088; 58.
ComplexPortal; CPX-3177; eIF4E-cup complex.
DIP; DIP-17920N; -.
ELM; Q9VMA3; -.
IntAct; Q9VMA3; 10.
MINT; Q9VMA3; -.
STRING; 7227.FBpp0288761; -.
iPTMnet; Q9VMA3; -.
PaxDb; Q9VMA3; -.
PRIDE; Q9VMA3; -.
EnsemblMetazoa; FBtr0290322; FBpp0288761; FBgn0000392.
EnsemblMetazoa; FBtr0346452; FBpp0312102; FBgn0000392.
GeneID; 33934; -.
KEGG; dme:Dmel_CG11181; -.
UCSC; CG11181-RB; d. melanogaster.
CTD; 33934; -.
FlyBase; FBgn0000392; cup.
eggNOG; ENOG410JI9T; Eukaryota.
eggNOG; ENOG4111A0F; LUCA.
InParanoid; Q9VMA3; -.
KO; K18746; -.
OMA; QTEFQDP; -.
OrthoDB; EOG091G01M2; -.
PhylomeDB; Q9VMA3; -.
ChiTaRS; cup; fly.
GenomeRNAi; 33934; -.
PRO; PR:Q9VMA3; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0000392; Expressed in 7 organ(s), highest expression level in adult organism.
Genevisible; Q9VMA3; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; HDA:FlyBase.
GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0000932; C:P-body; IDA:FlyBase.
GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
GO; GO:0003723; F:RNA binding; IDA:FlyBase.
GO; GO:0045182; F:translation regulator activity; IDA:UniProtKB.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
GO; GO:0007143; P:female meiotic nuclear division; IGI:UniProtKB.
GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
GO; GO:0045132; P:meiotic chromosome segregation; IDA:UniProtKB.
GO; GO:0007319; P:negative regulation of oskar mRNA translation; IDA:FlyBase.
GO; GO:0017148; P:negative regulation of translation; IMP:FlyBase.
GO; GO:0030715; P:oocyte growth in germarium-derived egg chamber; IGI:UniProtKB.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0007297; P:ovarian follicle cell migration; HMP:FlyBase.
GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR018862; eIF4E-T.
PANTHER; PTHR12269; PTHR12269; 1.
Pfam; PF10477; EIF4E-T; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; Nucleus; Oogenesis; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation.
CHAIN 1 1117 Protein cup.
/FTId=PRO_0000079561.
MOTIF 327 333 eIF-4E-binding 1.
MOTIF 363 369 eIF-4E-binding 2.
MOD_RES 263 263 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 503 503 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 327 327 Y->A: Strong reduction in interaction
with eIF4E1. Strong reduction in
interaction with eIF4E1; when associated
with A-332 and A-348. Complete loss of
interaction with eIF4E1; when associated
with A-364 and A-368.
{ECO:0000269|PubMed:14685270,
ECO:0000269|PubMed:14723848}.
MUTAGEN 332 333 LM->AA: Reduction in interaction with
eIF4E1. Strong reduction in interaction
with eIF4E1; when associated with A-327.
{ECO:0000269|PubMed:14723848}.
MUTAGEN 364 364 L->A: Mild reduction in interaction with
eIF4E1. Complete loss of interaction with
eIF4E1; when associated with A-327 and A-
368. {ECO:0000269|PubMed:14685270}.
MUTAGEN 368 368 L->A: Mild reduction in interaction with
eIF4E1. Complete loss of interaction with
eIF4E1; when associated with A-327 and A-
364. {ECO:0000269|PubMed:14685270}.
CONFLICT 836 836 H -> Q (in Ref. 1; AAB64427).
{ECO:0000305}.
CONFLICT 1030 1030 N -> K (in Ref. 1; AAB64427).
{ECO:0000305}.
CONFLICT 1035 1035 K -> Q (in Ref. 1; AAB64427).
{ECO:0000305}.
HELIX 329 337 {ECO:0000244|PDB:4AXG}.
HELIX 364 370 {ECO:0000244|PDB:4AXG}.
SEQUENCE 1117 AA; 125672 MW; 91274997F199EFD3 CRC64;
MQMAEAEQEN GAGALKIATN AGATDRPAHQ QLPLPVEDQQ DEVLTPAEKG KFEYPPPPPP
PTPVQAPLAT KATALNASQE HDDDEANSEK WEDPCAPPPP PPLPTSAFLA TGLGYLKLPA
FKLKDALEKA ITKLEANKRT LKASPESSRS IKNKNVVALE MLPRRSNPET IGDGSMLAST
STAVMLQTKK PAVIVEMERR CKIINLLAKQ NQILESISGE AIPMHGPSKH LHEDEGLTLQ
VLSARASTPY TQPSSMLSCT AVSCDLEHDS PRKQVASKEA VPEQQSSQVQ QKRPPSTGIH
KPGSLRAPKA VRPTTAPVVS SKPVKSYTRS RLMDIRNGMF NALMHRSKES FVMPRIATCD
DIELEGRLRR MNIWRTSDGT RFRTRSTTAN LNMNNNNNNE CMPAFFKNKN KPNLISDESI
IQSQPPQPQT EFQDPAIVNQ RRIGSGRLNH SKWGYNDEDY HSYHNGKSQH MEEVNSKNSK
NMTVLQFFDN GEISSQPQRR PNTPVMGMSI NRSENDTLHS NESSEDLSRA NENYVKRVMS
GFLVVSKPKS RDVEDRHHRR YRNQNEEPEW FSCGPTSRLD TIELCGFDED EEKMLKEGNK
NHGLGETERE TSKQKMDHKY KWTHAEPMGR SKYMPKHDTN NNHNVENMNN VMATEHQQQK
EEKRPGSGRS FQFDKFNQSQ QNYESSSYVN HQQPPQTQPQ QMQQQSNTNT NNSKFMSFFA
NEGNSSSSSL NEFFKQAINQ GHGNNPEQPK SLGHIGQMPS VDQLEAKWRR NSLNNVGETA
NKQTDNFQKL IGSLSSAKPQ SQAVGYDAIS NFIMQQQQYQ QQQQKQHLII QQQQQHTAFL
ASLQLKAILG RADTQLLLLR LTKGEISKHG LLVQLANPRL TDMDREAITA VLQFTNTQQQ
QQQHKQQLDM LSSTVIASQL QNLHNLAIVQ QTLAARQQPQ HNPQTQAPHQ LSQEDLQAHA
NVIMRNAVMK RKIEEQTSKL INGGAKHQAQ QQYLNRGQQR QARPDANSNA LLHALISGGG
NNHASGYPMN GQPQKHHSNL RFGDNQNFQS FESNQPHFAT QYKQQYQQSQ QQHPHQQPQQ
LNSLHQNNAG AVNSFNKAQM QAQSAISMLP NSGDEFH


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