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Mitochondrial poly(A) RNA polymerase
Known also as: PAP-associated domain-containing protein 1, Polynucleotide adenylyltransferase, Terminal uridylyltransferase 1
Known abbreviations: PAPD1, MTPAP, RP11-305E6.3, SPAX4, TUTase 1
Yeast homolog: not known
Protein
Structures Models Domains Secondary structure Disorder |
Top 3 models:
 |  |  |
| Template: 3pq1, chain A Method: hhsearch Fragment: 14-537 | Template: 2q0d, chain B Method: phyre Fragment: 163-507 | Template: 2hhp, chain A Method: hhsearch Fragment: 14-537 |
This protein has alternative isoforms:
Isoform 1:
| Sequence length: | 582 aa |
| Molecular weight: | 66.172 kDa |
| Isoelectric point: | 9.19 |
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MAVPGVGLLTRLNLCARRRTRVQRPIVRLLSCPGTVAKDLRRDEQPSGSVETGFEDKIPKRRFSEMQNERREQAQRTVLIHCPEKISENKFLKYLSQFGPINNHFFYESFGLYAVVEFCQKESIGSLQNG
THTPSTAMETAIPFRSRFFNLKLKNQTSERSRVRSSNQLPRSNKQLFELLCYAESIDDQLNTLLKEFQLTEENTKLRYLTCSLIEDMAAAYFPDCIVRPFGSSVNTFGKLGCDLDMFLDLDETRNLSAHK
ISGNFLMEFQVKNVPSERIATQKILSVLGECLDHFGPGCVGVQKILNARCPLVRFSHQASGFQCDLTTNNRIALTSSELLYIYGALDSRVRALVFSVRCWARAHSLTSSIPGAWITNFSLTMMVIFFLQR
RSPPILPTLDSLKTLADAEDKCVIEGNNCTFVRDLSRIKPSQNTETLELLLKEFFEYFGNFAFDKNSINIRQGREQNKPDSSPLYIQNPFETSLNISKNVSQSQLQKFVDLARESAWILQQEDTDRPSIS
SNRPWGLVSLLLPSAPNRKSFTKKKSNKFAIETVKNLLESLKGNRTENFTKTSGKRTISTQT
Isoform 2:
| Sequence length: | 712 aa |
| Molecular weight: | 78.833 kDa |
| Isoelectric point: | 8.14 |
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MAWAKKVGGRAGQGRSLSRCDPIILDPEWLYGPPEGEGGPEGVGGETRASIHPPLRTGRHHQKVNHNIRGPEGSAKDAAPGGGGHHQAGPGQRGDEDGALQHLCGGGGGVGVSVGRGTGTSVAAEHPSLQ
VKLLELQELVLRLAGDHNEGHGKFLAAAQNPADDPAPGAPAPQELGAADKQGGFEDKIPKRRFSEMQNERREQAQRTVLIHCPEKISENKFLKYLSQFGPINNHFFYESFGLYAVVEFCQKESIGSLQNG
THTPSTAMETAIPFRSRFFNLKLKNQTSERSRVRSSNQLPRSNKQLFELLCYAESIDDQLNTLLKEFQLTEENTKLRYLTCSLIEDMAAAYFPDCIVRPFGSSVNTFGKLGCDLDMFLDLDETRNLSAHK
ISGNFLMEFQVKNVPSERIATQKILSVLGECLDHFGPGCVGVQKILNARCPLVRFSHQASGFQCDLTTNNRIALTSSELLYIYGALDSRVRALVFSVRCWARAHSLTSSIPGAWITNFSLTMMVIFFLQR
RSPPILPTLDSLKTLADAEDKCVIEGNNCTFVRDLSRIKPSQNTETLELLLKEFFEYFGNFAFDKNSINIRQGREQNKPDSSPLYIQNPFETSLNISKNVSQSQLQKFVDLARESAWILQQEDTDRPSIS
SNRPWGLVSLLLPSAPNRKSFTKKKSNKFAIETVKNLLESLKGNRTENFTKTSGKRTISTQT
Enzyme
EC number: 2.7.7.19
Name: Polynucleotide adenylyltransferase
Reaction: ATP + RNA(n) <=> diphosphate + RNA(n+1)
Gene location: 10p11.23
Summary
PAPD1 creates the 3' poly(A) tail of mitochondrial transcripts and plays a role in replication-dependent histone mRNA degradation. It is a member of the DNA polymerase type-B-like family.
Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA.
Acts as homodimer.
Ubiquitous, with stronger expression in tissues with high energy requirements: heart, brain, and skeletal muscle.
Defects in MTPAP are the cause of spastic ataxia autosomal recessive type 4 (SPAX4).
See this protein in other databases:
Literature:
- Nagaike T, Suzuki T, Katoh T et al. Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase. J Biol Chem 2005 280(20):19721-7, doi: 10.1074/jbc.M500804200, PMID: 15769737.
- Bai Y, Srivastava SK, Chang JH et al. Structural basis for dimerization and activity of human PAPD1, a noncanonical poly(A) polymerase. Mol Cell 2011 41(3):311-20, doi: 10.1016/j.molcel.2011.01.013, PMID: 21292163.
- Chang JH, Tong L. Mitochondrial poly(A) polymerase and polyadenylation. Biochim Biophys Acta 2012 1819(9-10):992-7, doi: 10.1016/j.bbagrm.2011.10.012, PMID: 22172994.
- Thuresson AC, Astrom J, Astrom A et al. Multiple forms of poly(A) polymerases in human cells. Proc Natl Acad Sci U S A 1994 91(3):979-83, doi: , PMID: 8302877.
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