PAN3_PICGU
ID PAN3_PICGU Reviewed; 620 AA.
AC A5DCP8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 74.
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=PGUG_01053;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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}.
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: 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; CH408155; EDK36955.2; -; Genomic_DNA.
DR RefSeq; XP_001487676.1; XM_001487626.1.
DR AlphaFoldDB; A5DCP8; -.
DR SMR; A5DCP8; -.
DR STRING; 4929.XP_001487676.1; -.
DR PRIDE; A5DCP8; -.
DR EnsemblFungi; EDK36955; EDK36955; PGUG_01053.
DR GeneID; 5128905; -.
DR KEGG; pgu:PGUG_01053; -.
DR VEuPathDB; FungiDB:PGUG_01053; -.
DR eggNOG; KOG3741; Eukaryota.
DR HOGENOM; CLU_016423_1_0_1; -.
DR InParanoid; A5DCP8; -.
DR OMA; IGPHSQN; -.
DR OrthoDB; 1515085at2759; -.
DR Proteomes; UP000001997; 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 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..620
FT /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT /id="PRO_0000295375"
FT ZN_FING 7..36
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 39..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..482
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 522..620
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COILED 483..521
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COMPBIAS 101..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 323..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 380..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ SEQUENCE 620 AA; 68973 MW; DAC0DC3D19186E95 CRC64;
MNINLDSAKG TLCKNILIYG YCKYENKGCA FSHRRNNNAN SGPGATPAKS VATTPTSDKR
KFNVNTPSFQ PSTAPVQGLA NKFAGLSPKV KDIPVFVPSG TPASPAQSTP STGNQEQPMP
TSTVSNVPER KFNTSTPSFT PSQPIPAPPP QNTSSPPTNP YLMNQPGPPT DMYYQSAYPL
QYHLYAPAPP PRLAITHSSH QVDAHSLFID SELRETLQKR NEATLQSYPG GPEIVDVYHT
VVPIAAEGVS KIWKVSSSVY KGVSNVDGNV YALRKIEDFK IINETPFRTI KRWHGLQSAN
IVKIQDAFTT VAFGSPSLVV AYDYYPNAST LLEQHVNRRL GGRLEPLTED ILWLYLTQLV
NAVRTVHKKK LAARSSLDLS KIIVTTNRIR LAAIGMSDIL NWEADDAEIA RVGLPTYMEN
LQQEDIRNMA RLMVDLTTVM NPVVQNDIFK LKSSGLSTDF VAAVQDLSNT DDLESYIRKH
LAIRLLDVVD MLEDSNDYLE SQLSTELENA RLVRLMTKIN FIVDRPEWDN EATAAAAGWT
ENGPKYLLKL FRDFVFFQTD EMGKPVTDLS RVLVTLNKLD AGIDEKFLLV SRDEKTCIVV
SYKEIRDLLE SVFRTITRGK
