PAN3_DICDI
ID PAN3_DICDI Reviewed; 746 AA.
AC P0CD65;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=PAN2-PAN3 deadenylation complex subunit pan3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03181};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE Short=PAN deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN Name=pan3 {ECO:0000255|HAMAP-Rule:MF_03181}; ORFNames=DDB_G0279129;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC involved in mRNA turnover. PAN specifically shortens poly(A) tails of
CC RNA and the activity is stimulated by poly(A)-binding protein (PABP).
CC PAN deadenylation is followed by rapid degradation of the shortened
CC mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then
CC degraded by two alternative mechanisms, namely exosome-mediated 3'-5'
CC exonucleolytic degradation, or deadenlyation-dependent mRNA decaping
CC and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a
CC positive regulator for PAN activity, recruiting the catalytic subunit
CC PAN2 to mRNA via its interaction with RNA and PABP. {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit PAN2
CC to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts
CC (via PAM-2 motif) with poly(A)-binding protein (via PABC domain),
CC conferring substrate specificity of the enzyme complex.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- DOMAIN: The N-terminal zinc finger binds to poly(A) RNA.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- DOMAIN: The pseudokinase domain, the coiled-coil (CC), and C-terminal
CC knob domain (CK) form a structural unit (PKC) that forms an extensive
CC high-affinity interaction surface for pan2. {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- DOMAIN: Contains a pseudokinase domain. The protein kinase domain is
CC predicted to be catalytically inactive because some of the residues
CC important for catalytic activity are substituted and it lacks the
CC equivalent of the binding site for a peptide substrate. However, it has
CC retained an ATP-binding site and ATP-binding is required for mRNA
CC degradation, stimulating the activity of the pan2 nuclease in vitro.
CC The nucleotide-binding site is juxtaposed to the RNase active site of
CC pan2 in the complex and may actually bind nucleosides of a poly(A) RNA
CC rather than ATP, feeding the poly(A)-tail to the active site of the
CC deadenylase and thus increasing the efficiency with which this
CC distributive enzyme degrades oligo(A) RNAs. {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
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DR EMBL; AAFI02000094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFI02000095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CD65; -.
DR SMR; P0CD65; -.
DR dictyBase; DDB_G0279129; pan3.
DR InParanoid; P0CD65; -.
DR OMA; TWRNIQH; -.
DR PhylomeDB; P0CD65; -.
DR PRO; PR:P0CD65; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR HAMAP; MF_03181; PAN3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030844; PAN3.
DR InterPro; IPR041332; Pan3_PK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12272; PTHR12272; 1.
DR Pfam; PF18101; Pan3_PK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Metal-binding; mRNA processing;
KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..746
FT /note="PAN2-PAN3 deadenylation complex subunit pan3"
FT /id="PRO_0000391338"
FT ZN_FING 7..35
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 64..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..610
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 650..746
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COILED 611..649
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 509..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ SEQUENCE 746 AA; 86441 MW; ECB77446991B75CE CRC64;
MMYQQQPKNQ KQCKNIALHG YCRNSDKCEF SHELTPQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ NSNGNGSNNT ATSNNPIISP NSNIASPLKK SPIDNLTTSF QNLSTNQQTN
HHWADHFQSG IPEYIPKQQL QQLQQQQLLQ QQQQQALLLQ QQQQQNYDDD QHLYPYGDNS
VDDYEQHQYE PQPQPNNGID PNMNNQFQIN NFVAAQMRNA SPQSYQQQFQ QPNPSPQSSS
QQQQQQQQQQ QQAVYQQQQQ QQPSSQPLAQ NPSLQNNNNK LLQLQLQQHL QQIQAAQQQA
QINQSYTPYP SYSQSVIRNK PGRRNIGSFF MSESLKQDIL NQKSLLYLTL DPNDPRIKNI
PPMLNKYHSL YPLDHDASRE NQGKMFGYIT SVYKAISTLD GLPYAIRRVE GFRLSSEYAL
QAAETWRNIQ HPNIVSLKEI FVSKEFGDNS SLFFTYEFFP GSETLESKYL SQSGNPLSES
VLWSFICQIT SALKTIHSAG LVCRVIHPSK ILLTGKNRIR MNGVGIFDVV NFDTPRILAQ
YQHEDLLLFG RLILTLACRS AQSTTTTNLS KSIEYVSNQY SKELYNLIVY LLTKPVINLP
NIDEVVLMIS GRLLQENNYL HTYTDDLETE LSKEYENGRL FRLVTKLGFI NERPLYDMDP
RWSETGDRYL IKLFRDYIFH QVYDDGTPVL DFYHVVETLN KLDCGVDEKI LLMSRDEQSL
LVVSYKDLKK CIDSAFSELV SQKSHI
