PAN3_NEUCR
ID PAN3_NEUCR Reviewed; 656 AA.
AC Q7SDP4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=par-2; Synonyms=pan3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN ORFNames=NCU01929;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2] {ECO:0007744|PDB:4BWK, ECO:0007744|PDB:4BWX}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 234-656 IN COMPLEX WITH ATP, AND
RP SUBUNIT.
RX PubMed=23932717; DOI=10.1016/j.molcel.2013.07.011;
RA Christie M., Boland A., Huntzinger E., Weichenrieder O., Izaurralde E.;
RT "Structure of the PAN3 pseudokinase reveals the basis for interactions with
RT the PAN2 deadenylase and the GW182 proteins.";
RL Mol. Cell 51:360-373(2013).
RN [3] {ECO:0007744|PDB:4CZX, ECO:0007744|PDB:4CZY}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 234-656 IN COMPLEX WITH ATP, AND
RP SUBUNIT.
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 pabp-1.
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 rgb-30/xrn1. May
CC also be involved in post-transcriptional maturation of mRNA poly(A)
CC tails. par-2/pan3 acts as a positive regulator for PAN activity,
CC recruiting the catalytic subunit par-1/pan2 to mRNA via its interaction
CC with RNA and with pabp-1. {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit par-
CC 1/pan2 to form the poly(A)-nuclease (PAN) deadenylation complex.
CC Interacts (via PAM-2 motif) with poly(A)-binding protein pabp-1 (via
CC PABC domain), conferring substrate specificity of the enzyme complex.
CC {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:23932717,
CC ECO:0000269|PubMed:24880343}.
CC -!- INTERACTION:
CC Q7SDP4; P0C581: par-1; NbExp=6; IntAct=EBI-16108116, EBI-16108085;
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 (PubMed:23932717). The nucleotide-binding site is juxtaposed to the
CC RNase active site of par-1/pan2 in the complex and may actually bind
CC nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail
CC to the active site of the deadenylase and thus increasing the
CC efficiency with which this distributive enzyme degrades oligo(A) RNAs
CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_03181,
CC ECO:0000305|PubMed:23932717}.
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 par-1/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; CM002236; EAA34877.3; -; Genomic_DNA.
DR RefSeq; XP_964113.3; XM_959020.3.
DR PDB; 4BWK; X-ray; 3.30 A; A/B=234-656.
DR PDB; 4BWX; X-ray; 2.85 A; A/B=234-656.
DR PDB; 4CZX; X-ray; 1.85 A; B=538-656.
DR PDB; 4CZY; X-ray; 3.40 A; B/D=234-656.
DR PDBsum; 4BWK; -.
DR PDBsum; 4BWX; -.
DR PDBsum; 4CZX; -.
DR PDBsum; 4CZY; -.
DR AlphaFoldDB; Q7SDP4; -.
DR SMR; Q7SDP4; -.
DR DIP; DIP-61540N; -.
DR IntAct; Q7SDP4; 1.
DR STRING; 367110.Q7SDP4; -.
DR EnsemblFungi; EAA34877; EAA34877; NCU01929.
DR GeneID; 3880262; -.
DR KEGG; ncr:NCU01929; -.
DR VEuPathDB; FungiDB:NCU01929; -.
DR HOGENOM; CLU_016423_0_1_1; -.
DR InParanoid; Q7SDP4; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR HAMAP; MF_03181; PAN3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030844; PAN3.
DR InterPro; IPR041332; Pan3_PK.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12272; PTHR12272; 1.
DR Pfam; PF18101; Pan3_PK; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Cytoplasm; Metal-binding;
KW mRNA processing; Nucleotide-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..656
FT /note="PAN2-PAN3 deadenylation complex subunit pan3"
FT /id="PRO_0000295373"
FT ZN_FING 24..53
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..514
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000305|PubMed:24880343"
FT REGION 554..656
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000305|PubMed:24880343"
FT COILED 515..553
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000305|PubMed:24880343"
FT MOTIF 63..83
FT /note="PABPC-interacting motif-2 (PAM-2)"
FT /evidence="ECO:0000305"
FT BINDING 275..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23932717,
FT ECO:0000269|PubMed:24880343"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000269|PubMed:23932717, ECO:0000269|PubMed:24880343"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000269|PubMed:23932717, ECO:0000269|PubMed:24880343"
FT BINDING 412..413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000269|PubMed:23932717, ECO:0000269|PubMed:24880343"
FT HELIX 236..250
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:4BWX"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:4BWX"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 382..400
FT /evidence="ECO:0007829|PDB:4BWX"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:4BWX"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 442..461
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:4BWX"
FT TURN 472..477
FT /evidence="ECO:0007829|PDB:4BWX"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 485..495
FT /evidence="ECO:0007829|PDB:4BWX"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 540..554
FT /evidence="ECO:0007829|PDB:4CZX"
FT HELIX 566..583
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:4BWX"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:4CZY"
FT STRAND 624..628
FT /evidence="ECO:0007829|PDB:4CZX"
FT HELIX 629..643
FT /evidence="ECO:0007829|PDB:4CZX"
SQ SEQUENCE 656 AA; 74011 MW; 5E0D563A3B07451B CRC64;
MAATRYNSGD LRRQVGSPRA KNRDTKETLC RNVVIYGHCR WEDSGCTFNH DQNKASVSQT
DLNSNRRVFN VESPSFTPAN QQQSAGKKST FSSQAASAAP FTPRGVGTST PTLQQANDST
IFNPAAIREF TPQNYDVGNT ISQNGAQHVT QDGGLYSDPF SISSLGQTMP PQGQYNPYAN
DPNNLAGAGA GLYQPAGFGN GLVHPPNYHL YQPPSELYRP SLQPYQRTTY DFFIPKDRRE
NLQKKLFHMQ QLLPNSGLPN LDRWHSLFPL DTKATRNSTC FGYPSWMYKA QNNKNGRHFA
LRRIEGYRLT NEKAILNVTK EWKKIINANI VTVHEAFTTE FFGDSSLIFV YDFHPLSETL
YDHHFPPNNS HNRLRNTNKI PENLLWSYVC QIANALLAIH NAKLAARCLE LSKIIWENNR
IRLAACSILD VLHHDSPNRK TIEELQQEDF VKFGRIILAL ATNTPTLNFN NIDAALATIV
PRYSTQLRGV LEWLIKPSAP GETKTVETLL GGITTHLANF ANFVMQESDE KEFHLMRELE
NGRIARLMFK LSVVNERGDS CGVHNWSETG ERLLLKLFRD YVFHQVDADG KARLDTNHYL
NCLSKLDASS EEQILLTSRD NATVFVVSYR SIRQMLDRAY GELGKESKPS ATGATI
