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PAB-dependent poly(A)-specific ribonuclease subunit PAN3 (PAB1P-dependent poly(A)-nuclease) (PAN deadenylation complex subunit 3)

 PAN3_DROME              Reviewed;         790 AA.
Q95RR8;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 148.
RecName: Full=PAN2-PAN3 deadenylation complex subunit PAN3 {ECO:0000255|HAMAP-Rule:MF_03181};
AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03181};
AltName: Full=Poly(A)-nuclease deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
Short=PAN deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
Name=PAN3 {ECO:0000255|HAMAP-Rule:MF_03181}; ORFNames=CG11486;
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 [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).
[2]
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).
[3]
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).
[4]
INTERACTION WITH GW.
PubMed=21981923; DOI=10.1016/j.molcel.2011.09.007;
Braun J.E., Huntzinger E., Fauser M., Izaurralde E.;
"GW182 proteins directly recruit cytoplasmic deadenylase complexes to
miRNA targets.";
Mol. Cell 44:120-133(2011).
[5]
FUNCTION, AND INTERACTION WITH GW.
PubMed=23172285; DOI=10.1093/nar/gks1078;
Huntzinger E., Kuzuoglu-Ozturk D., Braun J.E., Eulalio A.,
Wohlbold L., Izaurralde E.;
"The interactions of GW182 proteins with PABP and deadenylases are
required for both translational repression and degradation of miRNA
targets.";
Nucleic Acids Res. 41:978-994(2013).
[6]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 349-790 IN COMPLEX WITH AMP,
INTERACTION WITH PAN2, AND SUBUNIT.
PubMed=23932717; DOI=10.1016/j.molcel.2013.07.011;
Christie M., Boland A., Huntzinger E., Weichenrieder O.,
Izaurralde E.;
"Structure of the PAN3 pseudokinase reveals the basis for interactions
with the PAN2 deadenylase and the GW182 proteins.";
Mol. Cell 51:360-373(2013).
-!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
deadenylation complex, one of two cytoplasmic mRNA deadenylases
involved in general and miRNA-mediated mRNA turnover. PAN
specifically shortens poly(A) tails of RNA and the activity is
stimulated by poly(A)-binding protein (PABP). 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 and subsequent 5'-3' exonucleolytic degradation by XRN1.
PAN3 acts as a positive regulator for PAN activity, recruiting the
catalytic subunit PAN2 to mRNA via its interaction with RNA and
PABP, and to miRNA targets via its interaction with GW182 family
proteins. {ECO:0000255|HAMAP-Rule:MF_03181,
ECO:0000269|PubMed:23172285}.
-!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit
PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex.
Interacts (via PAM-2 motif) with poly(A)-binding protein (via PABC
domain), conferring substrate specificity of the enzyme complex
(PubMed:23932717). Interacts with the GW182 family protein gw
(PubMed:21981923, PubMed:23172285). {ECO:0000255|HAMAP-
Rule:MF_03181, ECO:0000269|PubMed:21981923,
ECO:0000269|PubMed:23172285, ECO:0000269|PubMed:23932717}.
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
Rule:MF_03181}.
-!- DOMAIN: The N-terminal zinc finger binds to poly(A) RNA.
{ECO:0000255|HAMAP-Rule:MF_03181}.
-!- DOMAIN: Contains a pseudokinase domain. The protein kinase domain
is predicted to be catalytically inactive because some of the
residues important for catalytic activity are substituted and it
lacks the equivalent of the binding site for a peptide substrate.
However, it has retained an ATP-binding site and ATP-binding is
required for mRNA degradation, stimulating the activity of the
PAN2 nuclease in vitro (PubMed:23932717). The nucleotide-binding
site is juxtaposed to the RNase active site of PAN2 in the complex
and may actually bind nucleosides of a poly(A) RNA rather than
ATP, feeding the poly(A)-tail to the active site of the
deadenylase and thus increasing the efficiency with which this
distributive enzyme degrades oligo(A) RNAs (By similarity).
{ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:23932717}.
-!- DOMAIN: The pseudokinase domain, the coiled-coil (CC), and C-
terminal knob domain (CK) form a structural unit (PKC) that forms
an extensive high-affinity interaction surface for PAN2.
{ECO:0000255|HAMAP-Rule:MF_03181}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3
family. {ECO:0000255|HAMAP-Rule:MF_03181}.
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EMBL; AE014296; AAN11527.1; -; Genomic_DNA.
EMBL; AY061183; AAL28731.1; -; mRNA.
RefSeq; NP_647767.1; NM_139510.4.
UniGene; Dm.831; -.
PDB; 4BWP; X-ray; 3.60 A; A/B=349-790.
PDBsum; 4BWP; -.
ProteinModelPortal; Q95RR8; -.
SMR; Q95RR8; -.
BioGrid; 63867; 63.
DIP; DIP-17364N; -.
IntAct; Q95RR8; 48.
MINT; MINT-337479; -.
STRING; 7227.FBpp0072861; -.
PaxDb; Q95RR8; -.
PRIDE; Q95RR8; -.
EnsemblMetazoa; FBtr0072991; FBpp0072861; FBgn0035397.
GeneID; 38369; -.
KEGG; dme:Dmel_CG11486; -.
UCSC; CG11486-RG; d. melanogaster.
FlyBase; FBgn0035397; CG11486.
eggNOG; KOG3741; Eukaryota.
eggNOG; ENOG410XQ42; LUCA.
GeneTree; ENSGT00390000001504; -.
InParanoid; Q95RR8; -.
KO; K12572; -.
OMA; GHVYPGP; -.
OrthoDB; EOG091G04WA; -.
PhylomeDB; Q95RR8; -.
GenomeRNAi; 38369; -.
PRO; PR:Q95RR8; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0035397; -.
ExpressionAtlas; Q95RR8; differential.
Genevisible; Q95RR8; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0000932; C:P-body; IBA:GO_Central.
GO; GO:0031251; C:PAN complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IBA:GO_Central.
GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IEA:GOC.
HAMAP; MF_03181; PAN3; 1.
InterPro; IPR032050; DUF4797.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR030844; PAN3.
Pfam; PF16051; DUF4797; 1.
SUPFAM; SSF56112; SSF56112; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Coiled coil; Complete proteome; Cytoplasm;
mRNA processing; Nucleotide-binding; Reference proteome.
CHAIN 1 790 PAN2-PAN3 deadenylation complex subunit
PAN3.
/FTId=PRO_0000426721.
NP_BIND 472 479 ATP. {ECO:0000255|HAMAP-Rule:MF_03181,
ECO:0000269|PubMed:23932717}.
NP_BIND 552 553 ATP. {ECO:0000255|HAMAP-Rule:MF_03181}.
REGION 369 655 Pseudokinase domain. {ECO:0000255|HAMAP-
Rule:MF_03181}.
REGION 695 790 Knob domain. {ECO:0000255|HAMAP-
Rule:MF_03181}.
COILED 656 694 {ECO:0000255|HAMAP-Rule:MF_03181}.
COMPBIAS 112 208 Ala-rich.
BINDING 423 423 ATP. {ECO:0000255|HAMAP-Rule:MF_03181,
ECO:0000269|PubMed:23932717}.
SEQUENCE 790 AA; 85391 MW; 19555B56DAA43E21 CRC64;
MCSTYGLLSF EFSDTAAMDP IFFSPTNGIP SESKLATYMN RQNVATPSGY GLNNGFSLLN
LDSPLNKKSQ VTPQSPEFIP TRLGSTPNFY APYHNAPMQL SNGLNGVNGL TAAAAAAAAA
AAAAAAAVPS STSSASSASV TISKTANGGA SMLALQKTAS IASVTIAQQQ PQHPQKQQQH
PPSVGGGAVS AASAPIAISG APPNPAAAPF VSSMSAQTPL KGRGAMMRQE SPTAAMISGA
GPGEKSPPHG MTPHGASPIP SALPTSVHQE NVGGTIYFYP TANAQNSQPV VNSMVVDGTH
PALHGVSAVA PMSAGVPAAM MYTGHVYPGP SSNVVTMQPK TLLESAFFMP DEMRAEVLAR
NEISNLIMDA AEAAQHALPL EVENYHALYP LEPPAQPLHA KLTFPATTYR ATHNTTGYKY
CLRRIHGFRL QSTKCMTLVE MWKKLQHTNV VQLREVFTTK AFGDNSLVLV YDYHPGSQTL
LAKYFTPAPE TNGYTDPFQG EARPFSHKSN MQRTSNGPLL PEATIWSIIM QLTAGLKAIH
HAGLACKVLD PTKIIVTGKR VRFSSCCISD ITQFDPNASN PLALVNMHQQ DDLTALGRLV
LALACRCLQS VQRDNVQSSI DMVTRNYSTD LRNFIVYLFT TNNRRSVTDL MPMIGARFYT
QLDALQSKID MQEDELAKEM ENGRLYRILV KLNSINERPD FNLDCTWSET GDRYMLKLFR
DYLFHSVTED GRPWLDHAHI VQCLNKLDAG SIERVQLMSR DEQSVLIVSY AELKNCLENA
FSELMSSAAN


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