P36102 (PAN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PAB-dependent poly(A)-specific ribonuclease subunit PAN3

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

Gene names

Name:	PAN3
Synonyms:	ECM35
Ordered Locus Names:	YKL025C

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	679 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulatory 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 induces mRNA decay, which can be achieved by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 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. PAN3 acts as a positive regulator for PAN activity, recruiting PAN2 to mRNA via its interaction with PAB1. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. Ref.1 Ref.4 Ref.8
Subunit structure	The PAN deadenylation complex is a heterodimer of a catalytic subunit PAN2 and a regulatory subunit PAN3. PAN3 interacts with PAB1, conferring substrate-specificity of the enzyme complex. Ref.1 Ref.4 Ref.7
Subcellular location	Cytoplasm Ref.5 Ref.8.
Domain	The protein kinase domain is predicted to be catalytically inactive.
Post-translational modification	Phosphorylated by the cyclin-CDK complex PCL1-PHO85. Ref.9
Miscellaneous	Present with 1600 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein kinase superfamily. Contains 1 C3H1-type zinc finger. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
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 postreplication repair Inferred from physical interaction Ref.4. Source: SGD
Cellular_component	PAN complex Inferred from direct assay Ref.1. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro protein kinase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAN2	P53010	3	EBI-12895,EBI-12887

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 679	679	PAB-dependent poly(A)-specific ribonuclease subunit PAN3		PRO_0000058223
Regions
	Domain	299 – 549	251	Protein kinase
	Zinc finger	8 – 37	30	C3H1-type
	Nucleotide binding	305 – 313	9	ATP By similarity
	Compositional bias	114 – 201	88	Asn-rich
Sites
	Binding site	325	1	ATP By similarity
Amino acid modifications
	Modified residue	39	1	Phosphothreonine Ref.10
	Modified residue	57	1	Phosphothreonine Ref.11 Ref.12
	Modified residue	59	1	Phosphothreonine Ref.12
	Modified residue	61	1	Phosphothreonine Ref.10
	Modified residue	62	1	Phosphoserine Ref.10
	Modified residue	252	1	Phosphoserine Ref.12
	Modified residue	347	1	Phosphoserine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P36102 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: DE03E15BF4A5DA7C	FASTA	679	76,455
	10 20 30 40 50 60 MDKINPDWAK DIPCRNITIY GYCKKEKEGC PFKHSDNTTA TTINDVPPPI DVGEATTPTM 70 80 90 100 110 120 TSVPKFNAKV SASFTPMTVG SDSLTTVTNT TSAATNATGN IAMAATSATA STVNPMINPI 130 140 150 160 170 180 VNSSLVNNNN NNSNISISIP TTASSSNYDP FNAPIFTPSS TSSIHTNANA HSFPFPSIAN 190 200 210 220 230 240 SGGININATD DNSNNMSMAN NVPPPMQPPP IESSNLKYPR IYPPPHSLLQ YHLYAPEQPS 250 260 270 280 290 300 SLKSLLKPNE RSADQLFIPN NIREDLTKKN LSILQVFPSS GKVIPSIVQD YFNLVPLNFN 310 320 330 340 350 360 NNDFLNKTTL FKVFSNYDGK AYVLKRLPNI DKSMNPNKIS KIYQIWSKIN CTNLIKFRDI 370 380 390 400 410 420 FQTTKFGDLS ICLVFDYYPN SLSLYDYHFV NFPKFPITNN YLWIYLVQLT NVINSIHSQN 430 440 450 460 470 480 LSIGNTLNWR KVLITGDPGR IKLSHCNFMD LLFNDDTDTV VSSGGSTIEG QQQLDYKYLG 490 500 510 520 530 540 ELLFNLSINI ENSNNNTAPK EYRLEEITPQ SIDDMRQIDD KFKDVLKYLI SDNGDSKKSI 550 560 570 580 590 600 HDLTSHFYDK MFMVLESSQT YTEYMESVLS RELENGRLFR LVNKLNCIFG RIESRIDINW 610 620 630 640 650 660 SESGTKFPII LFYDYVFHQV DSNGKPIMDL THVLRCLNKL DAGIQEKLML VTPDELNCII 670 ISYKELKDLI ESTFRSITQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 443-453 AND 517-524, FUNCTION, INTERACTION WITH PAN2.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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, INTERACTION WITH DUN1.
[5]	"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].
[6]	"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].
[7]	"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 PAN2 AND PAB1.
[8]	"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.
[9]	"Combining chemical genetics and proteomics to identify protein kinase substrates." Dephoure N., Howson R.W., Blethrow J.D., Shokat K.M., O'Shea E.K. Proc. Natl. Acad. Sci. U.S.A. 102:17940-17945(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PCL1-PHO85.
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39; THR-61 AND SER-62, MASS SPECTROMETRY. Strain: ADR376.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, MASS SPECTROMETRY.
[12]	"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 THR-57; THR-59; SER-252 AND SER-347, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z28025 Genomic DNA. Translation: CAA81860.1. BK006944 Genomic DNA. Translation: DAA09129.1.
PIR	S37842.
RefSeq	NP_012900.1. NM_001179591.1.
3D structure databases
ProteinModelPortal	P36102.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3987N.
IntAct	P36102. 6 interactions.
MINT	MINT-480456.
STRING	4932.YKL025C.
Proteomic databases
PaxDb	P36102.
PeptideAtlas	P36102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL025C; YKL025C; YKL025C.
GeneID	853843.
KEGG	sce:YKL025C.
Organism-specific databases
CYGD	YKL025c.
SGD	S000001508. PAN3.
Phylogenomic databases
eggNOG	NOG260889.
GeneTree	ENSGT00390000001504.
HOGENOM	HOG000007619.
KO	K12572.
OMA	FYDYVFH.
OrthoDB	EOG45F0Z0.
Gene expression databases
Genevestigator	P36102.
GermOnline	YKL025C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR000571. Znf_CCCH. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50011. PROTEIN_KINASE_DOM. 1 hit. PS50103. ZF_C3H1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975058.

Entry information

Entry name

PAN3_YEAST

Accession

Primary (citable) accession number: P36102
Secondary accession number(s): D6VXQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program