PAN3_HUMAN
ID PAN3_HUMAN Reviewed; 887 AA.
AC Q58A45; A0N0X1; A1A4Y8; A1A4Y9; B1ALF1; B7Z3W7; Q0D2P2; Q5HYG6; Q5T515;
AC Q5T516; Q5TBA0; Q76E13; Q8NBA6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
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};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 754-887 (ISOFORMS 1/2/3).
RC TISSUE=Skin fibroblast;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 147-887 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-887 (ISOFORMS 1 AND 3), FUNCTION,
RP INTERACTION WITH PAN2 AND POLYADENYLATE-BINDING PROTEIN, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=14583602; DOI=10.1074/jbc.m309125200;
RA Uchida N., Hoshino S., Katada T.;
RT "Identification of a human cytoplasmic poly(A) nuclease complex stimulated
RT by poly(A)-binding protein.";
RL J. Biol. Chem. 279:1383-1391(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 654-887 (ISOFORMS 1/2/3).
RC TISSUE=Adrenal gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP INTERACTION WITH PABPC1, AND MUTAGENESIS OF TYR-203 AND PHE-293.
RX PubMed=18056425; DOI=10.1101/gad.1597707;
RA Funakoshi Y., Doi Y., Hosoda N., Uchida N., Osawa M., Shimada I.,
RA Tsujimoto M., Suzuki T., Katada T., Hoshino S.;
RT "Mechanism of mRNA deadenylation: evidence for a molecular interplay
RT between translation termination factor eRF3 and mRNA deadenylases.";
RL Genes Dev. 21:3135-3148(2007).
RN [8]
RP INTERACTION WITH PABPC, AND MUTAGENESIS OF PHE-293.
RX PubMed=17595167; DOI=10.1074/jbc.m701256200;
RA Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B.,
RA Gehring K.;
RT "Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-
RT binding protein domain from poly(A)-binding protein.";
RL J. Biol. Chem. 282:25067-25075(2007).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18625844; DOI=10.1083/jcb.200801196;
RA Zheng D., Ezzeddine N., Chen C.Y., Zhu W., He X., Shyu A.B.;
RT "Deadenylation is prerequisite for P-body formation and mRNA decay in
RT mammalian cells.";
RL J. Cell Biol. 182:89-101(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INTERACTION WITH TNRC6A; TNRC6B AND TNRC6C.
RX PubMed=21981923; DOI=10.1016/j.molcel.2011.09.007;
RA Braun J.E., Huntzinger E., Fauser M., Izaurralde E.;
RT "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA
RT targets.";
RL Mol. Cell 44:120-133(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP FUNCTION, SUBUNIT, INTERACTION WITH PAN2, AND ATP-BINDING.
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).
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 ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:23932717}.
CC -!- SUBUNIT: Homodimer (PubMed:23932717). Forms a heterotrimer with a
CC catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation
CC complex (PubMed:14583602, PubMed:23932717). Interacts (via PAM-2 motif)
CC with poly(A)-binding protein PABPC1 (via PABC domain), conferring
CC substrate specificity of the enzyme complex (PubMed:17595167,
CC PubMed:18056425). Interacts with the GW182 family proteins TNRC6A,
CC TNRC6B and TNRC6 (PubMed:21981923). Interacts with YTHDF3 (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_03181,
CC ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:17595167,
CC ECO:0000269|PubMed:18056425, ECO:0000269|PubMed:21981923,
CC ECO:0000269|PubMed:23932717}.
CC -!- INTERACTION:
CC Q58A45; P11940: PABPC1; NbExp=4; IntAct=EBI-2513054, EBI-81531;
CC Q58A45; Q504Q3: PAN2; NbExp=6; IntAct=EBI-2513054, EBI-1058976;
CC Q58A45; Q8NDV7: TNRC6A; NbExp=2; IntAct=EBI-2513054, EBI-2269715;
CC Q58A45; Q9UPQ9: TNRC6B; NbExp=4; IntAct=EBI-2513054, EBI-947158;
CC Q58A45; Q9HCJ0: TNRC6C; NbExp=4; IntAct=EBI-2513054, EBI-6507625;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03181, ECO:0000269|PubMed:14583602,
CC ECO:0000269|PubMed:18625844}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Pan3b;
CC IsoId=Q58A45-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58A45-2; Sequence=VSP_023753, VSP_023755;
CC Name=3;
CC IsoId=Q58A45-3; Sequence=VSP_023754;
CC Name=4;
CC IsoId=Q58A45-4; Sequence=VSP_041648, VSP_041649;
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, ECO:0000269|PubMed:14583602,
CC ECO:0000269|PubMed:23932717}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI28180.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABK41888.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC03632.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/pan3/";
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DR EMBL; AK091307; BAC03632.1; ALT_INIT; mRNA.
DR EMBL; AK296435; BAH12353.1; -; mRNA.
DR EMBL; EF088216; ABK41888.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL138712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024318; AAH24318.1; -; mRNA.
DR EMBL; BC128179; AAI28180.1; ALT_INIT; mRNA.
DR EMBL; BC128180; AAI28181.1; -; mRNA.
DR EMBL; AB107584; BAD02262.1; -; mRNA.
DR EMBL; AB109552; BAD93184.1; -; mRNA.
DR EMBL; BX647740; CAI45987.2; -; mRNA.
DR CCDS; CCDS9329.2; -. [Q58A45-1]
DR RefSeq; NP_787050.6; NM_175854.7. [Q58A45-1]
DR RefSeq; XP_005266390.1; XM_005266333.3. [Q58A45-3]
DR RefSeq; XP_005266391.1; XM_005266334.1. [Q58A45-2]
DR RefSeq; XP_016876021.1; XM_017020532.1. [Q58A45-2]
DR RefSeq; XP_016876022.1; XM_017020533.1.
DR AlphaFoldDB; Q58A45; -.
DR SMR; Q58A45; -.
DR BioGRID; 129129; 64.
DR DIP; DIP-53755N; -.
DR ELM; Q58A45; -.
DR IntAct; Q58A45; 14.
DR MINT; Q58A45; -.
DR STRING; 9606.ENSP00000370345; -.
DR ChEMBL; CHEMBL4105985; -.
DR iPTMnet; Q58A45; -.
DR PhosphoSitePlus; Q58A45; -.
DR BioMuta; PAN3; -.
DR DMDM; 341942213; -.
DR EPD; Q58A45; -.
DR jPOST; Q58A45; -.
DR MassIVE; Q58A45; -.
DR MaxQB; Q58A45; -.
DR PaxDb; Q58A45; -.
DR PeptideAtlas; Q58A45; -.
DR PRIDE; Q58A45; -.
DR ProteomicsDB; 62604; -. [Q58A45-1]
DR ProteomicsDB; 62605; -. [Q58A45-2]
DR ProteomicsDB; 62606; -. [Q58A45-3]
DR ProteomicsDB; 62607; -. [Q58A45-4]
DR Antibodypedia; 22704; 145 antibodies from 21 providers.
DR DNASU; 255967; -.
DR Ensembl; ENST00000380958.8; ENSP00000370345.3; ENSG00000152520.14. [Q58A45-1]
DR GeneID; 255967; -.
DR KEGG; hsa:255967; -.
DR MANE-Select; ENST00000380958.8; ENSP00000370345.3; NM_175854.8; NP_787050.6.
DR UCSC; uc001urz.4; human. [Q58A45-1]
DR CTD; 255967; -.
DR DisGeNET; 255967; -.
DR GeneCards; PAN3; -.
DR HGNC; HGNC:29991; PAN3.
DR HPA; ENSG00000152520; Low tissue specificity.
DR MIM; 617448; gene.
DR neXtProt; NX_Q58A45; -.
DR OpenTargets; ENSG00000152520; -.
DR PharmGKB; PA144596398; -.
DR VEuPathDB; HostDB:ENSG00000152520; -.
DR eggNOG; KOG3741; Eukaryota.
DR GeneTree; ENSGT00390000001504; -.
DR InParanoid; Q58A45; -.
DR OMA; AETMYSR; -.
DR OrthoDB; 1515085at2759; -.
DR PhylomeDB; Q58A45; -.
DR TreeFam; TF105865; -.
DR PathwayCommons; Q58A45; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR SignaLink; Q58A45; -.
DR BioGRID-ORCS; 255967; 23 hits in 1077 CRISPR screens.
DR ChiTaRS; PAN3; human.
DR GenomeRNAi; 255967; -.
DR Pharos; Q58A45; Tdark.
DR PRO; PR:Q58A45; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q58A45; protein.
DR Bgee; ENSG00000152520; Expressed in pancreatic ductal cell and 192 other tissues.
DR ExpressionAtlas; Q58A45; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; IDA: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 GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IEA:GOC.
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 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Metal-binding;
KW mRNA processing; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..887
FT /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT /id="PRO_0000280525"
FT ZN_FING 43..71
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 102..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..750
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 790..887
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT COILED 751..789
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT MOTIF 284..299
FT /note="PABPC-interacting motif-2 (PAM-2)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181,
FT ECO:0000269|PubMed:17595167"
FT COMPBIAS 356..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 570..577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 644..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q640Q5"
FT VAR_SEQ 1..332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023753"
FT VAR_SEQ 231..284
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14583602,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023754"
FT VAR_SEQ 333
FT /note="P -> MKLTDSTKGWIVWAALDSSMR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023755"
FT VAR_SEQ 684..687
FT /note="QADL -> VSKN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041648"
FT VAR_SEQ 688..887
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041649"
FT MUTAGEN 203
FT /note="Y->A: Reduces interaction with polyadenylate-binding
FT protein."
FT /evidence="ECO:0000269|PubMed:18056425"
FT MUTAGEN 293
FT /note="F->A: Reduces interaction with polyadenylate-binding
FT protein."
FT /evidence="ECO:0000269|PubMed:17595167,
FT ECO:0000269|PubMed:18056425"
FT CONFLICT 229
FT /note="R -> Q (in Ref. 5; BAD02262)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="Y -> H (in Ref. 4; AAI28181)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="R -> G (in Ref. 1; BAC03632)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="D -> G (in Ref. 5; BAD02262/BAD93184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 95613 MW; 4883F859D2A642D2 CRC64;
MNSGGGLPPP SAAASPSSSS LAAAVAVVAP PGVGGVPGGA AVGVKLKYCR YYAKDKTCFY
GEECQFLHED PAAGAAPGLG LHSNSVPLAL AGAPVAGFPP GAVAGGGAGP PPGPKKPDLG
DPGTGAAAGG GGSSGGLDGP RLAIPGMDGG ALTDTSLTDS YFSTSFIGVN GFGSPVETKY
PLMQRMTNSS SSPSLLNDSA KPYSAHDPLT SPASSLFNDF GALNISQRRK PRKYRLGMLE
ERLVPMGSKA RKAKNPIGCL ADRCKSGVPI NMVWWNRVTE NNLQTPNPTA SEFIPKGGST
SRLSNVSQSN MSAFSQVFSH PSMGSPATAG LAPGMSLSAG SSPLHSPKIT PHTSPAPRRR
SHTPNPASYM VPSSASTSVN NPVSQTPSSG QVIQKETVGG TTYFYTDTTP APLTGMVFPN
YHIYPPTAPH VAYMQPKANA PSFFMADELR QELINRHLIT MAQIDQADMP AVPTEVDSYH
SLFPLEPLPP PNRIQKSSNF GYITSCYKAV NSKDDLPYCL RRIHGFRLVN TKCMVLVDMW
KKIQHSNIVT LREVFTTKAF AEPSLVFAYD FHAGGETMMS RHFNDPNADA YFTKRKWGQH
EGPLPRQHAG LLPESLIWAY IVQLSSALRT IHTAGLACRV MDPTKILITG KTRLRVNCVG
VFDVLTFDNS QNNNPLALMA QYQQADLISL GKVVLALACN SLAGIQRENL QKAMELVTIN
YSSDLKNLIL YLLTDQNRMR SVNDIMPMIG ARFYTQLDAA QMRNDVIEED LAKEVQNGRL
FRLLAKLGTI NERPEFQKDP TWSETGDRYL LKLFRDHLFH QVTEAGAPWI DLSHIISCLN
KLDAGVPEKI SLISRDEKSV LVVTYSDLKR CFENTFQELI AAANGQL
