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Protein

PAN2-PAN3 deadenylation complex catalytic subunit PAN2

Gene

PAN2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded 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. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.UniRule annotation9 Publications

Miscellaneous

Present with 1510 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Exonucleolytic cleavage of poly(A) to 5'-AMP.UniRule annotation2 Publications

Cofactori

a divalent metal cationUniRule annotation1 PublicationNote: Binds 2 metal cations per subunit in the catalytic exonuclease domain.UniRule annotation1 Publication

Activity regulationi

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.UniRule annotation3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi660ZincCombined sources1 Publication1
Metal bindingi662Zinc; via pros nitrogenCombined sources1 Publication1
Metal bindingi713ZincCombined sources1 Publication1
Metal bindingi716ZincCombined sources1 Publication1
Metal bindingi910Divalent metal cation; catalyticUniRule annotationBy similarity1 Publication1
Metal bindingi912Divalent metal cation; catalyticUniRule annotationBy similarity1 Publication1
Metal bindingi1020Divalent metal cation; catalyticUniRule annotationBy similarity1
Metal bindingi1071Divalent metal cation; catalyticUniRule annotationBy similarity1 Publication1

GO - Molecular functioni

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
  • postreplication repair Source: SGD

Keywordsi

Molecular functionExonuclease, Hydrolase, Nuclease
Biological processmRNA processing
LigandMetal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30594-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
PAN2-PAN3 deadenylation complex catalytic subunit PAN2UniRule annotationCurated (EC:3.1.13.4UniRule annotation)
Alternative name(s):
PAB1P-dependent poly(A)-specific ribonucleaseUniRule annotation
Poly(A)-nuclease deadenylation complex subunit 2UniRule annotation
Short name:
PAN deadenylation complex subunit 2UniRule annotation
Gene namesi
Name:PAN2UniRule annotation
Ordered Locus Names:YGL094C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL094C
SGDiS000003062 PAN2

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi912E → A: Abolishes nuclease activity. 1 Publication1
Mutagenesisi1020D → A: Abolishes nuclease activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000582221 – 1115PAN2-PAN3 deadenylation complex catalytic subunit PAN2Add BLAST1115

Proteomic databases

MaxQBiP53010
PaxDbiP53010
PRIDEiP53010

PTM databases

iPTMnetiP53010

Interactioni

Subunit structurei

Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PAN3P361029EBI-12887,EBI-12895

Protein-protein interaction databases

BioGridi33157, 128 interactors
ComplexPortaliCPX-3294 PAN complex
DIPiDIP-2466N
IntActiP53010, 6 interactors
MINTiP53010
STRINGi4932.YGL094C

Structurei

Secondary structure

11115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP53010
SMRiP53010
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati27 – 66WD 1UniRule annotationAdd BLAST40
Repeati112 – 153WD 2UniRule annotationAdd BLAST42
Repeati155 – 194WD 3UniRule annotationAdd BLAST40
Repeati197 – 236WD 4UniRule annotationAdd BLAST40
Repeati295 – 334WD 5UniRule annotationAdd BLAST40
Domaini474 – 855USPUniRule annotation1 PublicationAdd BLAST382
Domaini907 – 1079ExonucleaseUniRule annotationAdd BLAST173

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni337 – 473LinkerUniRule annotation1 PublicationAdd BLAST137

Domaini

Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.UniRule annotation1 Publication
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the peptidase C19 family. PAN2 subfamily.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00390000013978
HOGENOMiHOG000230585
InParanoidiP53010
KOiK12571
OMAiIHLWGSP
OrthoDBiEOG092C0KHR

Family and domain databases

Gene3Di2.130.10.10, 1 hit
3.30.420.10, 1 hit
HAMAPiMF_03182 PAN2, 1 hit
InterProiView protein in InterPro
IPR013520 Exonuclease_RNaseT/DNA_pol3
IPR030843 PAN2
IPR028881 PAN2_dom
IPR038765 Papain_like_cys_pep_sf
IPR011047 Quinoprotein_ADH-like_supfam
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR028889 USP_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf
PfamiView protein in Pfam
PF00929 RNase_T, 1 hit
PF13423 UCH_1, 1 hit
SMARTiView protein in SMART
SM00479 EXOIII, 1 hit
SUPFAMiSSF50998 SSF50998, 2 hits
SSF53098 SSF53098, 1 hit
SSF54001 SSF54001, 2 hits
PROSITEiView protein in PROSITE
PS50235 USP_3, 1 hit

Sequencei

Sequence statusi: Complete.

P53010-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNNWQHFFNN PVDLSEHLKK PYFRFDNRDK EITAISFDEK ANLIWSGDSY
60 70 80 90 100
GCISSYDPTF QLYTRYRGHI GGNSVKDILS HRDGILSISE DSLHFANRRG
110 120 130 140 150
VTKLNLTSID IAAFSELNTM CYSPHSLKNN IYCGGDNTNW GIASIDLNRG
160 170 180 190 200
CLDSLLNYSS KVKLMCSNNK VLSIGRQTGT VDLLDPTSNR TIKSFNAHSA
210 220 230 240 250
SISAMDLRDN TLVTVGKSKR FYNLYADPFV NVYDLRTMRQ LPPVSFSKGT
260 270 280 290 300
TMGSGGADFV QLHPLLPTVM IVASSSGSFD FIDLSNPTLR TQYVHPCQSI
310 320 330 340 350
KKLCLSPNGD VLGILEADNH LDTWRRSSNN MGMFTNTPEM LAYPDYFNDI
360 370 380 390 400
TSDGPISVDD ETYPLSSVGM PYYLDKLLSA WPPVVFKSEG TIPQLTGKSP
410 420 430 440 450
LPSSGKLKSN LAVISSQNEK LSTQEFPLLR YDRTKYGMRN AIPDYVCLRD
460 470 480 490 500
IRKQITSGLE TSDIQTYTSI NKYEVPPAYS RLPLTSGRFG TDNFDFTPFN
510 520 530 540 550
NTEYSGLDPD VDNHYTNAII QLYRFIPEMF NFVVGCLKDE NFETTLLTDL
560 570 580 590 600
GYLFDMMERS HGKICSSSNF QASLKSLTDK RQLENGEPQE HLEEYLESLC
610 620 630 640 650
IRESIEDFNS SESIKRNMPQ KFNRFLLSQL IKEEAQTVNH NITLNQCFGL
660 670 680 690 700
ETEIRTECSC DHYDTTVKLL PSLSISGINK TVIKQLNKKS NGQNILPYIE
710 720 730 740 750
YAMKNVTQKN SICPTCGKTE TITQECTVKN LPSVLSLELS LLDTEFSNIR
760 770 780 790 800
SSKNWLTSEF YGSIIKNKAV LRSTASELKG TSHIFKYELN GYVAKITDNN
810 820 830 840 850
NETRLVTYVK KYNPKENCFK WLMFNDYLVV EITEEEALKM TYPWKTPEII
860 870 880 890 900
IYCDAEELRK PFFSVDTYSI NYDILFRDYF ANGIRDTARR EYKLLTHDEA
910 920 930 940 950
PKSGTLVAID AEFVSLQSEL CEIDHQGIRS IIRPKRTALA RISIIRGEEG
960 970 980 990 1000
ELYGVPFVDD YVVNTNHIED YLTRYSGILP GDLDPEKSTK RLVRRNVVYR
1010 1020 1030 1040 1050
KVWLLMQLGC VFVGHGLNND FKHININVPR NQIRDTAIYF LQGKRYLSLR
1060 1070 1080 1090 1100
YLAYVLLGMN IQEGNHDSIE DAHTALILYK KYLHLKEKAI FEKVLNSVYE
1110
EGRAHNFKVP ETSKG
Length:1,115
Mass (Da):127,039
Last modified:October 1, 1996 - v1
Checksum:i4F91B737F761AE5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39204 Genomic DNA Translation: AAC49152.1
Z72616 Genomic DNA Translation: CAA96800.1
BK006941 Genomic DNA Translation: DAA08012.1
PIRiS64101
RefSeqiNP_011421.1, NM_001180959.1

Genome annotation databases

EnsemblFungiiYGL094C; YGL094C; YGL094C
GeneIDi852786
KEGGisce:YGL094C

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39204 Genomic DNA Translation: AAC49152.1
Z72616 Genomic DNA Translation: CAA96800.1
BK006941 Genomic DNA Translation: DAA08012.1
PIRiS64101
RefSeqiNP_011421.1, NM_001180959.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q8GX-ray2.10A/B416-870[»]
4Q8HX-ray3.10A460-1115[»]
4XR7X-ray3.80A/D/G/J340-1115[»]
ProteinModelPortaliP53010
SMRiP53010
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33157, 128 interactors
ComplexPortaliCPX-3294 PAN complex
DIPiDIP-2466N
IntActiP53010, 6 interactors
MINTiP53010
STRINGi4932.YGL094C

PTM databases

iPTMnetiP53010

Proteomic databases

MaxQBiP53010
PaxDbiP53010
PRIDEiP53010

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL094C; YGL094C; YGL094C
GeneIDi852786
KEGGisce:YGL094C

Organism-specific databases

EuPathDBiFungiDB:YGL094C
SGDiS000003062 PAN2

Phylogenomic databases

GeneTreeiENSGT00390000013978
HOGENOMiHOG000230585
InParanoidiP53010
KOiK12571
OMAiIHLWGSP
OrthoDBiEOG092C0KHR

Enzyme and pathway databases

BioCyciYEAST:G3O-30594-MONOMER

Miscellaneous databases

PROiPR:P53010

Family and domain databases

Gene3Di2.130.10.10, 1 hit
3.30.420.10, 1 hit
HAMAPiMF_03182 PAN2, 1 hit
InterProiView protein in InterPro
IPR013520 Exonuclease_RNaseT/DNA_pol3
IPR030843 PAN2
IPR028881 PAN2_dom
IPR038765 Papain_like_cys_pep_sf
IPR011047 Quinoprotein_ADH-like_supfam
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR028889 USP_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf
PfamiView protein in Pfam
PF00929 RNase_T, 1 hit
PF13423 UCH_1, 1 hit
SMARTiView protein in SMART
SM00479 EXOIII, 1 hit
SUPFAMiSSF50998 SSF50998, 2 hits
SSF53098 SSF53098, 1 hit
SSF54001 SSF54001, 2 hits
PROSITEiView protein in PROSITE
PS50235 USP_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPAN2_YEAST
AccessioniPrimary (citable) accession number: P53010
Secondary accession number(s): D6VU51
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 10, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
  5. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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Main funding by: National Institutes of Health

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