PAN3_XENTR
ID PAN3_XENTR Reviewed; 787 AA.
AC A1L1C7;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=TEgg127h19.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC involved in general and miRNA-mediated mRNA turnover. PAN specifically
CC shortens poly(A) tails of RNA and the activity is stimulated by
CC poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid
CC degradation of the shortened mRNA tails by the CCR4-NOT complex.
CC Deadenylated mRNAs are then degraded by two alternative mechanisms,
CC namely exosome-mediated 3'-5' exonucleolytic degradation, or
CC deadenlyation-dependent mRNA decaping and subsequent 5'-3'
CC exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator
CC for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its
CC interaction with RNA and PABP, and to miRNA targets via its interaction
CC with GW182 family proteins. {ECO:0000255|HAMAP-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 pabpc1 (via PABC
CC domain), conferring substrate specificity of the enzyme complex.
CC Interacts with the GW182 family proteins tnrc6a, tnrc6b and tnrc6c.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- DOMAIN: The N-terminal zinc finger binds to poly(A) RNA.
CC {ECO:0000255|HAMAP-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 -!- 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
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DR EMBL; CR855590; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC128994; AAI28995.1; -; mRNA.
DR RefSeq; NP_001017301.1; NM_001017301.3.
DR AlphaFoldDB; A1L1C7; -.
DR SMR; A1L1C7; -.
DR STRING; 8364.ENSXETP00000025796; -.
DR PaxDb; A1L1C7; -.
DR DNASU; 550055; -.
DR GeneID; 550055; -.
DR KEGG; xtr:550055; -.
DR CTD; 255967; -.
DR Xenbase; XB-GENE-5731378; pan3.
DR eggNOG; KOG3741; Eukaryota.
DR HOGENOM; CLU_016423_3_0_1; -.
DR InParanoid; A1L1C7; -.
DR OMA; IGPHSQN; -.
DR OrthoDB; 1515085at2759; -.
DR PhylomeDB; A1L1C7; -.
DR TreeFam; TF105865; -.
DR Reactome; R-XTR-429947; Deadenylation of mRNA.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; ISS:UniProtKB.
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:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:UniProtKB-UniRule.
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 InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12272; PTHR12272; 1.
DR Pfam; PF18101; Pan3_PK; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Metal-binding; mRNA processing;
KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..787
FT /note="PAN2-PAN3 deadenylation complex subunit pan3"
FT /id="PRO_0000350626"
FT ZN_FING 23..51
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..650
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 690..787
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COILED 651..689
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT MOTIF 185..200
FT /note="PABPC-interacting motif-2 (PAM-2)"
FT /evidence="ECO:0000305"
FT COMPBIAS 135..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 545..546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ SEQUENCE 787 AA; 85905 MW; 9EFC212E1D4D6E44 CRC64;
MNSGLTPSPS PAVAAAGPAG VPGSKLKFCR YYAKDRTCFY GDECQFLHDD QLGGIHGNGN
SPLSLPGGGP AAVYPQPVTP VGSKKLDLAG LEAQRLAIPG LDGGAIPDTS LTDSYFSTSF
IGLNGFGSPG EATYPRMQQR MTNSSSSPSL LNDSAKPYAA HDPLGSPASA MFNDFGGLTM
SQRRKTPNPT ASEFIPKGGS TSRLSNMSQS SMSAFSQALF SHPSMGGPTG AGLAPGMSLS
AGSSPLHSPK ITPHTSPAPR RRSHTPNPAN YMVPTSASTP VTNSVSQPPS TGEIIQKATV
GGTTYFYTDT TPAPLTGMVF PNYHIYPPTA PHIAYMQPKA NAPSFFMADE LRQELINRHL
ITMAQIDQAD MPGVPAEVDS YHSLFPLEPL PPPNRIKTSN FGYITSCYKA VNSKDDLPYC
LRRIHGFRLV NTKCMSLVDT WKKIQHSNIV TLREMFTTKA FGEHSLVFAY DFHAGSETMM
SRHFNDPSAD AYFTKRKWGQ HDGPLPRQHA GLLPESLIWA YIVQLSSALR TIHTAGLACR
VMDPTKILIT GKTRLRVNCV GIFDVLTYDG SQNNPVALMP QYQQADLISL GKVVLALACN
SLAGIQRENL QKAMELVTIN YSSDLKNLIL YLLTEQNRMR SVNDIMPMIG ARFYTQLDAA
QMRNDVIEED LAKEVQNGRL FRLLAKLGTI NERPEFQKDP AWSETGDRYL LKLFRDHLFH
QVTEAGTPWI DLSHIVSCLN KLDAGVPEKI SLISRDEKSV LVVTYSDLKR CFENTFQELV
AAANGQL
