P53010 (PAN2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PAB-dependent poly(A)-specific ribonuclease subunit PAN2
EC=3.1.13.4

Alternative name(s):
PAB1P-dependent poly(A)-nuclease

Gene names

Name:	PAN2
Ordered Locus Names:	YGL094C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1115 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, the minor of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by polyadenylate-binding protein PAB1. Deadenylation of the 3'-tail to a length that is too short to bind PAB1 (less than 10 adenylate residues) triggers mRNA degradation, which can be achieved by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent decaping by DCP1-DCP2 followed by 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. Ref.1 Ref.6 Ref.7 Ref.8 Ref.13 Ref.14
Catalytic activity	Exonucleolytic cleavage of poly(A) to 5'-AMP.
Enzyme regulation	Positively regulated by the regulatory subunit PAN3. Negatively regulated by PAB1-binding protein PBP1. Inhibited under stress conditions. Inhibition of deadenylation under stress increases mRNA stability, which may be a mechanism to retain the majority of the cytoplasmic pool of mRNAs for later reuse and recovery from stress. Ref.6 Ref.11 Ref.15
Subunit structure	The PAN deadenylation complex is a heterodimer of a catalytic subunit PAN2 and a regulatory subunit PAN3.
Subcellular location	Cytoplasm Ref.9 Ref.14.
Miscellaneous	Present with 1510 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the peptidase C19 family. PAN2 subfamily. Contains 1 exonuclease domain. Contains 6 WD repeats.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm
Domain	Repeat WD repeat
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA 3'-end processing Inferred from physical interaction Ref.1. Source: SGD nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC postreplication repair Inferred from physical interaction Ref.8. Source: SGD ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	PAN complex Inferred from direct assay Ref.6. Source: SGD
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro poly(A)-specific ribonuclease activity Inferred from electronic annotation. Source: EC ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAN3	P36102	3	EBI-12887,EBI-12895

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1115	1115	PAB-dependent poly(A)-specific ribonuclease subunit PAN2		PRO_0000058222
Regions
	Repeat	27 – 66	40	WD 1
	Repeat	112 – 153	42	WD 2
	Repeat	155 – 194	40	WD 3
	Repeat	197 – 236	40	WD 4
	Repeat	295 – 334	40	WD 5
	Repeat	345 – 391	47	WD 6
	Domain	906 – 1079	174	Exonuclease
Amino acid modifications
	Modified residue	404	1	Phosphoserine Ref.16

Sequences

	Sequence		Length	Mass (Da)
	P53010 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4F91B737F761AE5A	FASTA	1,115	127,039
	10 20 30 40 50 60 MNNWQHFFNN PVDLSEHLKK PYFRFDNRDK EITAISFDEK ANLIWSGDSY GCISSYDPTF 70 80 90 100 110 120 QLYTRYRGHI GGNSVKDILS HRDGILSISE DSLHFANRRG VTKLNLTSID IAAFSELNTM 130 140 150 160 170 180 CYSPHSLKNN IYCGGDNTNW GIASIDLNRG CLDSLLNYSS KVKLMCSNNK VLSIGRQTGT 190 200 210 220 230 240 VDLLDPTSNR TIKSFNAHSA SISAMDLRDN TLVTVGKSKR FYNLYADPFV NVYDLRTMRQ 250 260 270 280 290 300 LPPVSFSKGT TMGSGGADFV QLHPLLPTVM IVASSSGSFD FIDLSNPTLR TQYVHPCQSI 310 320 330 340 350 360 KKLCLSPNGD VLGILEADNH LDTWRRSSNN MGMFTNTPEM LAYPDYFNDI TSDGPISVDD 370 380 390 400 410 420 ETYPLSSVGM PYYLDKLLSA WPPVVFKSEG TIPQLTGKSP LPSSGKLKSN LAVISSQNEK 430 440 450 460 470 480 LSTQEFPLLR YDRTKYGMRN AIPDYVCLRD IRKQITSGLE TSDIQTYTSI NKYEVPPAYS 490 500 510 520 530 540 RLPLTSGRFG TDNFDFTPFN NTEYSGLDPD VDNHYTNAII QLYRFIPEMF NFVVGCLKDE 550 560 570 580 590 600 NFETTLLTDL GYLFDMMERS HGKICSSSNF QASLKSLTDK RQLENGEPQE HLEEYLESLC 610 620 630 640 650 660 IRESIEDFNS SESIKRNMPQ KFNRFLLSQL IKEEAQTVNH NITLNQCFGL ETEIRTECSC 670 680 690 700 710 720 DHYDTTVKLL PSLSISGINK TVIKQLNKKS NGQNILPYIE YAMKNVTQKN SICPTCGKTE 730 740 750 760 770 780 TITQECTVKN LPSVLSLELS LLDTEFSNIR SSKNWLTSEF YGSIIKNKAV LRSTASELKG 790 800 810 820 830 840 TSHIFKYELN GYVAKITDNN NETRLVTYVK KYNPKENCFK WLMFNDYLVV EITEEEALKM 850 860 870 880 890 900 TYPWKTPEII IYCDAEELRK PFFSVDTYSI NYDILFRDYF ANGIRDTARR EYKLLTHDEA 910 920 930 940 950 960 PKSGTLVAID AEFVSLQSEL CEIDHQGIRS IIRPKRTALA RISIIRGEEG ELYGVPFVDD 970 980 990 1000 1010 1020 YVVNTNHIED YLTRYSGILP GDLDPEKSTK RLVRRNVVYR KVWLLMQLGC VFVGHGLNND 1030 1040 1050 1060 1070 1080 FKHININVPR NQIRDTAIYF LQGKRYLSLR YLAYVLLGMN IQEGNHDSIE DAHTALILYK 1090 1100 1110 KYLHLKEKAI FEKVLNSVYE EGRAHNFKVP ETSKG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity." Boeck R., Tarun S.Z. Jr., Rieger M., Deardorff J.A., Mueller-Auer S., Sachs A.B. J. Biol. Chem. 271:432-438(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
[2]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast." Sachs A.B., Deardorff J.A. Cell 70:961-973(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 489-504.
[6]	"PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae." Brown C.E., Tarun S.Z. Jr., Boeck R., Sachs A.B. Mol. Cell. Biol. 16:5744-5753(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PAN3, ENZYME REGULATION.
[7]	"Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-specific deadenylation." Brown C.E., Sachs A.B. Mol. Cell. Biol. 18:6548-6559(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks." Hammet A., Pike B.L., Heierhorst J. J. Biol. Chem. 277:22469-22474(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"Identification of factors regulating poly(A) tail synthesis and maturation." Mangus D.A., Smith M.M., McSweeney J.M., Jacobson A. Mol. Cell. Biol. 24:4196-4206(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[12]	"Positive and negative regulation of poly(A) nuclease." Mangus D.A., Evans M.C., Agrin N.S., Smith M.M., Gongidi P., Jacobson A. Mol. Cell. Biol. 24:5521-5533(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAN3.
[13]	"Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export." Dunn E.F., Hammell C.M., Hodge C.A., Cole C.N. Genes Dev. 19:90-103(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Yeast mRNA poly(A) tail length control can be reconstituted in vitro in the absence of Pab1p-dependent poly(A) nuclease activity." Dheur S., Nykamp K.R., Viphakone N., Swanson M.S., Minvielle-Sebastia L. J. Biol. Chem. 280:24532-24538(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"Translation-independent inhibition of mRNA deadenylation during stress in Saccharomyces cerevisiae." Hilgers V., Teixeira D., Parker R. RNA 12:1835-1845(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[16]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39204 Genomic DNA. Translation: AAC49152.1. Z72616 Genomic DNA. Translation: CAA96800.1. BK006941 Genomic DNA. Translation: DAA08012.1.
PIR	S64101.
RefSeq	NP_011421.1. NM_001180959.1.
3D structure databases
ProteinModelPortal	P53010.
SMR	P53010. Positions 298-329, 906-1080.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2466N.
IntAct	P53010. 6 interactions.
MINT	MINT-637100.
STRING	4932.YGL094C.
Proteomic databases
PaxDb	P53010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL094C; YGL094C; YGL094C.
GeneID	852786.
KEGG	sce:YGL094C.
Organism-specific databases
CYGD	YGL094c.
SGD	S000003062. PAN2.
Phylogenomic databases
eggNOG	COG0847.
GeneTree	ENSGT00390000013978.
HOGENOM	HOG000230585.
KO	K12571.
OMA	SKFGIED.
OrthoDB	EOG44F9J8.
Enzyme and pathway databases
BioCyc	YEAST:G3O-30594-MONOMER.
Gene expression databases
Genevestigator	P53010.
GermOnline	YGL094C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.130.10.10. 2 hits.
InterPro	IPR006055. Exonuclease. IPR013520. Exonuclease_RNaseT/DNA_pol3. IPR001394. Peptidase_C19. IPR012337. RNaseH-like_dom. IPR015943. WD40/YVTN_repeat-like_dom. IPR017986. WD40_repeat_dom. [Graphical view]
Pfam	PF00929. RNase_T. 1 hit. [Graphical view]
SMART	SM00479. EXOIII. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit. SSF50978. WD40_like. 1 hit.
PROSITE	PS50235. UCH_2_3. 1 hit. PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	972276.

Entry information

Entry name

PAN2_YEAST

Accession

Primary (citable) accession number: P53010
Secondary accession number(s): D6VU51

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program