Speckle targeted PIP5K1A-regulated poly(A) polymerase

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Q3MHT4 (STPAP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 59. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Speckle targeted PIP5K1A-regulated poly(A) polymerase
Short name=Star-PAP
EC=2.7.7.19

Alternative name(s):
RNA-binding motif protein 21
Short name=RNA-binding protein 21
U6 snRNA-specific terminal uridylyltransferase 1
Short name=U6-TUTase
EC=2.7.7.52

Gene names

Name:	Tut1
Synonyms:	Rbm21

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	866 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation By similarity.
Catalytic activity	UTP + RNA(n) = diphosphate + RNA(n+1). ATP + RNA(n) = diphosphate + RNA(n+1).
Cofactor	Magnesium or manganese By similarity.
Enzyme regulation	Adenylyltransferase activity is specifically phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) By similarity.
Subunit structure	Associates with the cleavage and polyadenylation specificity factor (CPSF) complex. Interacts with CPSF1 and CPSF3; the interaction is direct. Interacts with PIP5K1A; interaction By similarity.
Subcellular location	Nucleus › nucleolus By similarity. Nucleus speckle By similarity.
Post-translational modification	Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
Sequence similarities	Belongs to the DNA polymerase type-B-like family. Contains 1 C2H2-type zinc finger. Contains 1 PAP-associated domain. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA cleavage Inferred from sequence or structural similarity. Source: UniProtKB mRNA polyadenylation Inferred from sequence or structural similarity. Source: UniProtKB snRNA processing Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA uridylyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB mRNA 3'-UTR binding Inferred from sequence or structural similarity. Source: UniProtKB polynucleotide adenylyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 866

866

Speckle targeted PIP5K1A-regulated poly(A) polymerase

PRO_0000254188

Regions

Domain

56 – 128

RRM

Domain

492 – 550

PAP-associated

Zinc finger

16 – 40

C2H2-type

Compositional bias

229 – 311

Pro-rich

Sites

Metal binding

216

Magnesium or manganese; catalytic By similarity

Metal binding

218

Magnesium or manganese; catalytic By similarity

Amino acid modifications

Modified residue

741

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q3MHT4 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: E85DE9E051D30412
Show »

FASTA

866

94,378

        10         20         30         40         50         60 
MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR KAQGLRSVFV 

        70         80         90        100        110        120 
SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG DISAREAVLS QPKHSLGGHT 

       130        140        150        160        170        180 
LRVRPREQKE FQSPASKSPK GVDSNSHQLA QALAEAADVG AQMVKLVELR ELSEAERQLR 

       190        200        210        220        230        240 
TLVVALMQEV FTEFFPGCVV HPFGSSVNSF DVHGCDLDLF LDLGDMEEPQ PDPQTPKLPE 

       250        260        270        280        290        300 
ASSLDSTLAS SLDPQVLACT PASLDSLSPT SLQDSEALDF ETPSSLAPQT PDSALGSDTV 

       310        320        330        340        350        360 
TSPQSLPPVS PLEEDRGEGK HRKELELAEA SKDEKEEATA VLELVGSILR GCVPGVYRVQ 

       370        380        390        400        410        420 
TVPSARRPVV KFCHRPSGLH GDISLSNRLA LYNSRFLNLC SEMDSRVRPL VYTLRCWAQH 

       430        440        450        460        470        480 
NGLSGGGPLL NNYALTLLVI YFLQTRDPPV LPTVAQLTQR SGEGEQVEVD GWDCSFPKDA 

       490        500        510        520        530        540 
SRLEPSTNVE PLSSLLAQFF SCVSCWDLSG SLLSLREGQA LMVAGGLPSD LWEGLRLGPM 

       550        560        570        580        590        600 
NLQDPFDLSH NVAANVTSRV AKRLQSSCGA AASYCRSLQY QQRSSRGRDW GLLPLLQPSS 

       610        620        630        640        650        660 
PSSLLSAKLI PLPSAPFPQI ITALVSVLRE ALGCHIEQGT KRRRSEGARS KDSPLGGANK 

       670        680        690        700        710        720 
RPRLSGQEKS CEEGKEEPQG CAGDHSENEV EEMVIELRET PQDWALLHCG PPGELPLMTA 

       730        740        750        760        770        780 
KCLDKTAEQN PMEPEGAGEG SPGETEKEAS HPSSVSWRCA LWHQIWQGRR RARRRFQQQT 

       790        800        810        820        830        840 
KEEGRGGPST GAEWLAVEAR VTQELKGPKS EQQRLQGEPL LTFVASASQA EQTLTVAPLQ 

       850        860 
DPQGLFPGLH HFLQVFIPQA LKNLLK

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References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC104695 mRNA. Translation: AAI04696.1.
IPI	IPI00371444.
RefSeq	NP_001029073.1. NM_001033901.1.
UniGene	Rn.129389.
3D structure databases
ProteinModelPortal	Q3MHT4.
SMR	Q3MHT4. Positions 55-141.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q3MHT4. 1 interaction.
STRING	10116.ENSRNOP00000027187.
PTM databases
PhosphoSite	Q3MHT4.
Proteomic databases
PaxDb	Q3MHT4.
PRIDE	Q3MHT4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000027187; ENSRNOP00000027187; ENSRNOG00000020047.
GeneID	499314.
KEGG	rno:499314.
UCSC	RGD:1561043. rat.
Organism-specific databases
CTD	64852.
RGD	1561043. Tut1.
Phylogenomic databases
eggNOG	COG5260.
GeneTree	ENSGT00550000074490.
HOVERGEN	HBG079670.
InParanoid	Q3MHT4.
OMA	EQQGCAG.
OrthoDB	EOG480HWB.
Gene expression databases
Genevestigator	Q3MHT4.
GermOnline	ENSRNOG00000020047. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR002058. PAP_assoc. IPR000504. RRM_dom. IPR015880. Znf_C2H2-like. [Graphical view]
Pfam	PF03828. PAP_assoc. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. SM00355. ZnF_C2H2. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. PS00028. ZINC_FINGER_C2H2_1. False negative. PS50157. ZINC_FINGER_C2H2_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	702524.

Entry information

Entry name

STPAP_RAT

Accession

Primary (citable) accession number: Q3MHT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 25, 2005
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents