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Protein

PAB-dependent poly(A)-specific ribonuclease subunit PAN3

Gene

Pan3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein (PABP), which 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 and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with PABP and to miRNA targets via its interaction with GW182 family proteins.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei467ATPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri49 – 77C3H1-typeUniRule annotationAdd BLAST29
Nucleotide bindingi516 – 521ATPUniRule annotation6
Nucleotide bindingi590 – 591ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: MGI
  • mRNA processing Source: UniProtKB-KW
  • nuclear-transcribed mRNA poly(A) tail shortening Source: GO_Central
  • positive regulation of cytoplasmic mRNA processing body assembly Source: MGI
  • protein targeting Source: MGI
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-429947. Deadenylation of mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
PAB-dependent poly(A)-specific ribonuclease subunit PAN3UniRule annotation
Alternative name(s):
PAB1P-dependent poly(A)-nucleaseUniRule annotation
PAN deadenylation complex subunit 3UniRule annotation
Gene namesi
Name:Pan3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1919837. Pan3.

Subcellular locationi

  • CytoplasmP-body UniRule annotation1 Publication

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: MGI
  • PAN complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002805261 – 837PAB-dependent poly(A)-specific ribonuclease subunit PAN3Add BLAST837

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei300PhosphoserineBy similarity1
Modified residuei307PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ640Q5.
PaxDbiQ640Q5.
PeptideAtlasiQ640Q5.
PRIDEiQ640Q5.

PTM databases

iPTMnetiQ640Q5.
PhosphoSitePlusiQ640Q5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000029647.
ExpressionAtlasiQ640Q5. baseline and differential.
GenevisibleiQ640Q5. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with the catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PABPC1 (via PABC domain), conferring substrate specificity of the enzyme complex. Interacts with the GW182 family proteins TNRC6A, TNRC6B and TNRC6C.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031651.

Structurei

3D structure databases

ProteinModelPortaliQ640Q5.
SMRiQ640Q5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini438 – 700Protein kinaseUniRule annotationAdd BLAST263

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni438 – 837Interaction with PAN2UniRule annotationAdd BLAST400

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili702 – 723UniRule annotationAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi230 – 245PABPC-interacting motif-2 (PAM-2)UniRule annotationAdd BLAST16

Domaini

The protein kinase domain is predicted to be catalytically inactive. However it still binds ATP and ATP-binding is required for mRNA degradation.UniRule annotation

Sequence similaritiesi

Belongs to the protein kinase superfamily. PAN3 family.UniRule annotation
Contains 1 C3H1-type zinc finger.UniRule annotation
Contains 1 protein kinase domain.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri49 – 77C3H1-typeUniRule annotationAdd BLAST29

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG3741. Eukaryota.
ENOG410XQ42. LUCA.
GeneTreeiENSGT00390000001504.
HOGENOMiHOG000007619.
HOVERGENiHBG058849.
InParanoidiQ640Q5.
KOiK12572.
TreeFamiTF105865.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
HAMAPiMF_03181. PAN3. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR030844. PAN3.
IPR000719. Prot_kinase_dom.
IPR000571. Znf_CCCH.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
SSF90229. SSF90229. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q640Q5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNSGGGGGLP PPSAAASPSS SSLAAAVAVA VAASSGVGGV PGGPAAAAGV
60 70 80 90 100
KLKYCRYYAK DKTCFYGEEC QFLHEDPAAG AAPGLGLHSN SVPLALAAAA
110 120 130 140 150
GAAFPPGALP GGGAGPPAGP KKPELGVPGA ATAGGGLDGP RVAIPGMDGG
160 170 180 190 200
ALTDASLTES YFSTSFIGVN GFGSPVETKY PLMQRMTSSS SSPSLLNDSA
210 220 230 240 250
KPYTGHDLLT SSASSLFNDF GALNISQRRK TPNPTASEFI PKGGSTSRLS
260 270 280 290 300
NVSQSNMSAF SQVFSHPSMG SPATAGLAPG MSLSAGSSPL HSPKITPHTS
310 320 330 340 350
PAPRRRSHTP NPASFMVPPS ASTPANNPAP QPPSSGQVIQ KETVGGTTYF
360 370 380 390 400
YTDTTPAPLT GMVFPNYHIY PPTAPHVAYM QPKANAPSFF MADELRQELI
410 420 430 440 450
NRHLITMAQI DQADMPAVPT EVDSYHSLFP LEPLPPPNRI QKSSNFGYIT
460 470 480 490 500
SCYKAVNSKD DLPYCLRRIH GFRLVNTKCM VLVDMWKKIQ HSNIVTLREV
510 520 530 540 550
FTTKAFAEPS LVFAYDFHAG GETMMSRHFN DPNSDAYFTK RKWGQHDGPL
560 570 580 590 600
PRQHAGLLPE SLIWAYIVQL SSALRTIHTA GLACRVMDPT KILITSKTRL
610 620 630 640 650
RVNCVGVFDV LTFDNSQNNN PLALMAQYQQ ADLISLGKVV LALACNSLAG
660 670 680 690 700
IQRENLQKAM ELVTINYSSD LKNLILYLLT DQNRMRSVND IMPMIGARFY
710 720 730 740 750
TQLDAAQMRN DVIEEDLAKE VQNGRLFRLL AKLGTINERP EFQKDPTWSE
760 770 780 790 800
TGDRYLLKLF RDHLFHQVTE AGAPWIDLSH IISCLNKLDA GVPEKISLIS
810 820 830
RDEKSVLVVT YSDLKRCFEN TFQELIAAAN GNDRNSN
Length:837
Mass (Da):89,745
Last modified:July 27, 2011 - v3
Checksum:i323CACB0F32E745A
GO
Isoform 2 (identifier: Q640Q5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     281-301: MSLSAGSSPLHSPKITPHTSP → NKLPSESALDLKINPTVHETD
     302-837: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:301
Mass (Da):29,592
Checksum:i92A49BF5ECFF5FEE
GO

Sequence cautioni

The sequence AAH82547 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated
The sequence BAB28221 differs from that shown. Intron retention.Curated
The sequence BAE32127 differs from that shown. Several sequencing errors.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041650281 – 301MSLSA…PHTSP → NKLPSESALDLKINPTVHET D in isoform 2. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_041651302 – 837Missing in isoform 2. 1 PublicationAdd BLAST536

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012409 mRNA. Translation: BAB28221.1. Sequence problems.
AK028869 mRNA. Translation: BAC26161.1.
AK153632 mRNA. Translation: BAE32127.1. Sequence problems.
AC131730 Genomic DNA. No translation available.
AC134441 Genomic DNA. No translation available.
BC082547 mRNA. Translation: AAH82547.1. Sequence problems.
CCDSiCCDS39401.2. [Q640Q5-1]
RefSeqiNP_082567.3. NM_028291.4. [Q640Q5-1]
UniGeneiMm.320469.
Mm.491496.

Genome annotation databases

EnsembliENSMUST00000031651; ENSMUSP00000031651; ENSMUSG00000029647. [Q640Q5-1]
GeneIDi72587.
KEGGimmu:72587.
UCSCiuc009aod.2. mouse. [Q640Q5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012409 mRNA. Translation: BAB28221.1. Sequence problems.
AK028869 mRNA. Translation: BAC26161.1.
AK153632 mRNA. Translation: BAE32127.1. Sequence problems.
AC131730 Genomic DNA. No translation available.
AC134441 Genomic DNA. No translation available.
BC082547 mRNA. Translation: AAH82547.1. Sequence problems.
CCDSiCCDS39401.2. [Q640Q5-1]
RefSeqiNP_082567.3. NM_028291.4. [Q640Q5-1]
UniGeneiMm.320469.
Mm.491496.

3D structure databases

ProteinModelPortaliQ640Q5.
SMRiQ640Q5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031651.

PTM databases

iPTMnetiQ640Q5.
PhosphoSitePlusiQ640Q5.

Proteomic databases

EPDiQ640Q5.
PaxDbiQ640Q5.
PeptideAtlasiQ640Q5.
PRIDEiQ640Q5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031651; ENSMUSP00000031651; ENSMUSG00000029647. [Q640Q5-1]
GeneIDi72587.
KEGGimmu:72587.
UCSCiuc009aod.2. mouse. [Q640Q5-1]

Organism-specific databases

CTDi255967.
MGIiMGI:1919837. Pan3.

Phylogenomic databases

eggNOGiKOG3741. Eukaryota.
ENOG410XQ42. LUCA.
GeneTreeiENSGT00390000001504.
HOGENOMiHOG000007619.
HOVERGENiHBG058849.
InParanoidiQ640Q5.
KOiK12572.
TreeFamiTF105865.

Enzyme and pathway databases

ReactomeiR-MMU-429947. Deadenylation of mRNA.

Miscellaneous databases

ChiTaRSiPan3. mouse.
PROiQ640Q5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029647.
ExpressionAtlasiQ640Q5. baseline and differential.
GenevisibleiQ640Q5. MM.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
HAMAPiMF_03181. PAN3. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR030844. PAN3.
IPR000719. Prot_kinase_dom.
IPR000571. Znf_CCCH.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
SSF90229. SSF90229. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAN3_MOUSE
AccessioniPrimary (citable) accession number: Q640Q5
Secondary accession number(s): Q3U5F2, Q8CE75, Q9CZM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.