PAN3_CRYNJ
ID PAN3_CRYNJ Reviewed; 684 AA.
AC P0CP50; Q55L85; Q5KA98;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
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}; OrderedLocusNames=CNJ02470;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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 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; AE017350; AAW46022.1; -; Genomic_DNA.
DR RefSeq; XP_567539.1; XM_567539.1.
DR AlphaFoldDB; P0CP50; -.
DR SMR; P0CP50; -.
DR STRING; 5207.AAW46022; -.
DR PaxDb; P0CP50; -.
DR PRIDE; P0CP50; -.
DR EnsemblFungi; AAW46022; AAW46022; CNJ02470.
DR GeneID; 3254153; -.
DR KEGG; cne:CNJ02470; -.
DR VEuPathDB; FungiDB:CNJ02470; -.
DR eggNOG; KOG3741; Eukaryota.
DR HOGENOM; CLU_016423_2_0_1; -.
DR InParanoid; P0CP50; -.
DR OMA; IGPHSQN; -.
DR OrthoDB; 1515085at2759; -.
DR Proteomes; UP000002149; Chromosome 10.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; IBA:GO_Central.
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 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..684
FT /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT /id="PRO_0000295366"
FT ZN_FING 36..65
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..544
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 387..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..684
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COILED 545..583
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COMPBIAS 19..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 444..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ SEQUENCE 684 AA; 75082 MW; C278F58E2770A483 CRC64;
MLPPPKSAAV QIVRPPSPSS EKAKEKEKKH SPEKRETAQR ICRNVMIYGY CKYQDQGCIY
YHPPAGADPS TPQNSSPVAH APTPSAPTPL AGTPAREKPT LSIEHLAAPV FVPKGLDSSP
RASTPSVPTP SAPTPPVWPS LPSTGLLPRQ DVQVSAQPSH AQLSATASPM AYDDPSHIAL
SAAHAHAQAQ ALTHGILDPH AHAPPVDQSM YLPPRQPLDY NLYAAPLPSI GGNPLYPTHP
HAFFVSDDLR RAIQAKQEAV YAGANGASAP GLPQELGVYH SLIPLPLPAP TAQCPPTQSQ
PSKVYGLPSP VYRATSEVDG NTYCLRRVEG FKLVNQLAFA SMDTWRRMRH PNIVGLKEAF
TTKTFGDNSL IMVYDYHPLS TTLYDEYLSP NPPEPSPASA LANQPPKRRS SPPERILWSY
VTQIANALKA IHSSGLAVRN LDASKILLTG KNRIRLNGCG VWDVLAFDNK TPVQAFQQED
LLSFGKLIIS LTCDFFQPTL PFSLPLEHIS RHYSSDLSNL ILYLISKPAQ GQIKSIDEVV
KMMGPRILNE LDAVQSYADV LENELGAEVE NGRIVRLLTK LGFINERAEF ELDPRWSDTG
DRYILKLFRD YVFHSVGVDG KPILDLSHVL VCLNKLDAGL DERVMLVSRD DQSCLVVSYR
EIKHCIEAAF NELKNAGNNH RVHR
