PAN3_CHATD
ID PAN3_CHATD Reviewed; 640 AA.
AC G0S0Y3; A0A068EX63; A0A068F1B9;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 2.
DT 03-AUG-2022, entry version 51.
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=CTHT_0011660;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1] {ECO:0007744|PDB:4CYI, ECO:0007744|PDB:4CYJ}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), X-RAY CRYSTALLOGRAPHY (2.42
RP ANGSTROMS) OF 293-640 IN COMPLEX WITH ATP, FUNCTION, AND SUBUNIT.
RX PubMed=24872509; DOI=10.15252/embj.201488373;
RA Wolf J., Valkov E., Allen M.D., Meineke B., Gordiyenko Y., McLaughlin S.H.,
RA Olsen T.M., Robinson C.V., Bycroft M., Stewart M., Passmore L.A.;
RT "Structural basis for Pan3 binding to Pan2 and its function in mRNA
RT recruitment and deadenylation.";
RL EMBO J. 33:1514-1526(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [3] {ECO:0007744|PDB:4D0K}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 522-629.
RX PubMed=24880343; DOI=10.1038/nsmb.2837;
RA Jonas S., Christie M., Peter D., Bhandari D., Loh B., Huntzinger E.,
RA Weichenrieder O., Izaurralde E.;
RT "An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate
RT mRNA deadenylation and decay.";
RL Nat. Struct. Mol. Biol. 21:599-608(2014).
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 PAB1. PAN
CC deadenylation is followed by rapid degradation of the shortened mRNA
CC tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC 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. May also be
CC involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3
CC acts as a positive regulator for PAN activity, recruiting the catalytic
CC subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
CC {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509}.
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 PAB1 (via PABC domain),
CC conferring substrate specificity of the enzyme complex.
CC {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509}.
CC -!- INTERACTION:
CC G0S0Y3; G0SAK8: PAN2; NbExp=9; IntAct=EBI-9836608, EBI-9836534;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=G0S0Y3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G0S0Y3-2; Sequence=VSP_059086;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS22693.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ657770; AID55017.1; -; mRNA.
DR EMBL; KJ657771; AID55018.1; -; mRNA.
DR EMBL; GL988039; EGS22693.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006691685.1; XM_006691622.1.
DR PDB; 4CYI; X-ray; 2.42 A; A/B/C/D/E/F/G/H=205-640.
DR PDB; 4CYJ; X-ray; 2.59 A; A/B/C/D=205-640.
DR PDB; 4D0K; X-ray; 1.89 A; B/C=522-629.
DR PDBsum; 4CYI; -.
DR PDBsum; 4CYJ; -.
DR PDBsum; 4D0K; -.
DR AlphaFoldDB; G0S0Y3; -.
DR SMR; G0S0Y3; -.
DR DIP; DIP-61542N; -.
DR IntAct; G0S0Y3; 1.
DR MINT; G0S0Y3; -.
DR STRING; 759272.G0S0Y3; -.
DR EnsemblFungi; EGS22693; EGS22693; CTHT_0011660.
DR GeneID; 18255204; -.
DR KEGG; cthr:CTHT_0011660; -.
DR eggNOG; KOG3741; Eukaryota.
DR HOGENOM; CLU_016423_1_0_1; -.
DR OrthoDB; 1515085at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0031251; C:PAN complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; 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 PANTHER; PTHR12272; PTHR12272; 1.
DR Pfam; PF18101; Pan3_PK; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW Metal-binding; mRNA processing; Nucleotide-binding; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..640
FT /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT /id="PRO_0000441675"
FT ZN_FING 17..46
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 43..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..498
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000305|PubMed:24872509"
FT REGION 538..640
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000305|PubMed:24872509"
FT COILED 499..537
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000305|PubMed:24872509"
FT COMPBIAS 43..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24872509"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000269|PubMed:24872509"
FT BINDING 338..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000269|PubMed:24872509"
FT BINDING 397..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000269|PubMed:24872509"
FT VAR_SEQ 1..99
FT /note="MAPLDLTRGQTDACSTENKDILCRNVLIYGHCRYEDQGCTYNHDQNKNSSQP
FT EAPSKKMFNVDSPSFTPSGQSTVLPKKTTLSSQAASAAPFTPRGGGT -> MTKTRTPP
FT NQKP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:24872509"
FT /id="VSP_059086"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:4CYJ"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:4CYI"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 271..282
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 367..386
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:4CYI"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 427..447
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:4CYI"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 498..522
FT /evidence="ECO:0007829|PDB:4CYI"
FT HELIX 527..538
FT /evidence="ECO:0007829|PDB:4D0K"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:4D0K"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:4D0K"
FT HELIX 557..567
FT /evidence="ECO:0007829|PDB:4D0K"
FT HELIX 580..592
FT /evidence="ECO:0007829|PDB:4D0K"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:4D0K"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:4D0K"
FT HELIX 613..628
FT /evidence="ECO:0007829|PDB:4D0K"
SQ SEQUENCE 640 AA; 71813 MW; ABE58EFE0C199D61 CRC64;
MAPLDLTRGQ TDACSTENKD ILCRNVLIYG HCRYEDQGCT YNHDQNKNSS QPEAPSKKMF
NVDSPSFTPS GQSTVLPKKT TLSSQAASAA PFTPRGGGTP TLQTTAESTM FNPAAIREFT
PQNYDLGNNN ANGISQENGL YPDPFTMSTM GTALPTAGQY NLPLYGDHSG LAAPGAPFYP
PHAAYPTGPI QPPHYHLYQP FGPYRQELQP WQRATYDFFM PQNLREDLQK KQFATLQVIP
NSGLPQLEHW HSLVPLDTSN RKNTSCFGYP SWVYKAQNSR NGRHYALRRL EGYRLTNEKA
ILNVMKDWKK IKNASIVTIH EVFTTREFGD SSLIFAYDFH PLSKTLQEHH FQPIHGNRYR
PPPAVPENTI WGYICQIANA LKTIHSNRLA ARCLEPSKII LTDINRIRLS ACAILDVVQF
GMNSRSVVEL QQEDFVKFGK LILSLATGTL PAHLNNIPAA LETLGNKYSA NLKSAVNWLL
DTSSGETKTI EHFMTGIASQ MTTFFDLALQ DNDEKLFHLA REVENGRIAR SLMKLLTILE
RGDYDGVPSW SETGDRYQLK LFRDYVFHRV DADGKPNLSI GHMLTCMSKL EAGVDENILL
TSRDNETVFV LSYRELRQMY DRAFNELVKA SKTGAPGANT
