D2HS90 (STPAP_AILME) Reviewed, UniProtKB/Swiss-Prot

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
ORF Names:	PANDA_014931

Organism

Ailuropoda melanoleuca (Giant panda) [Reference proteome]

Taxonomic identifier

9646 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Ursidae › Ailuropoda

Protein attributes

Sequence length	869 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide adenylyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 869	869	Speckle targeted PIP5K1A-regulated poly(A) polymerase		PRO_0000404589
Regions
	Domain	56 – 128	73	RRM
	Domain	490 – 548	59	PAP-associated
	Zinc finger	16 – 40	25	C2H2-type
	Compositional bias	229 – 309	81	Pro-rich
Sites
	Metal binding	216	1	Magnesium or manganese; catalytic By similarity
	Metal binding	218	1	Magnesium or manganese; catalytic By similarity
Amino acid modifications
	Modified residue	748	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	D2HS90 [UniParc]. Last modified February 9, 2010. Version 1. Checksum: 01BB7E4572A16511	FASTA	869	94,063
	10 20 30 40 50 60 MAAVDLDVQS LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRATR KAQGLRSVFV 70 80 90 100 110 120 SGFPRDVDSA QLTQYFQAFG PVASVVMDKD KGVFAIVEMG DVGTREAVLS QPQHTLGGHR 130 140 150 160 170 180 LRVRPREQKE FQSPASKSPK GAAPDSHQLT KALAEAPDVG AQMVKLVGLR ELSEAERQLR 190 200 210 220 230 240 NLVVALMQEV FTEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLEESQ PAPKAPESPS 250 260 270 280 290 300 LDSALASPLD PQALACTPAS PPDSQPPSPQ DSEALDFETP SSSLAPQTPD SALASETLAS 310 320 330 340 350 360 PQSLPPASPL QEDRGEGDLG KALELAEALS GEKTEGVAML ELVGSILRGC VPGVYRVQTV 370 380 390 400 410 420 PSARRPVVKF CHRPSGLHGD VSLSNRLALH NSRFLSLCSE LDGRVRPLVY TLRCWAQGRG 430 440 450 460 470 480 LSGSGPLLSN YALTLLVIYF LQTRDPPVLP TVSQLTQKAG EGEQVEVDGW DCSFPRDASG 490 500 510 520 530 540 LEPSTNKEPL SSLLAQFFSC VSCWDLRGSL LSLREGQALP VAGDLPSNRW EGLRLGPMNL 550 560 570 580 590 600 QDPFDLSHNV AANVTSRVAG RLQNSCQAAA NYCRSLQYQR RSSRGRDWGL LPLLQPSSPS 610 620 630 640 650 660 SLLSATPIPL PPAPFTQLTA ALAQVLREAL GCHIEQGTKR LRSDRGGPEE SPQGGTSKRL 670 680 690 700 710 720 KLDGEEKSCE EGREEQQGYI RDHSEDGVEE MVVEVGEMVQ DWVQSPGRPG EPPQMLREQL 730 740 750 760 770 780 ATGEEGQSGH AALAEQGPKG PEAAREGSQG ETGRGVSLSS VSWRCALWHR VWQGRRRARR 790 800 810 820 830 840 RLQQQTKERG RGSAGTAEWL AVEAQVTREL RGLSSAAQRP EAEPLLTFVA SASQVNQTLT 850 860 VTPIQDSQGL FPDLHHFLQV FLPQALRNL

References

[1]

"The sequence and de novo assembly of the giant panda genome." Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J. , Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., Wang J. Nature 463:311-317(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	GL193267 Genomic DNA. Translation: EFB28167.1.
3D structure databases
ProteinModelPortal	D2HS90.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOGENOM	HOG000115998.
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...

Entry information

Entry name

STPAP_AILME

Accession

Primary (citable) accession number: D2HS90

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 8, 2011
Last sequence update:	February 9, 2010
Last modified:	May 29, 2013
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program