O00442 · RTCA_HUMAN
- ProteinRNA 3'-terminal phosphate cyclase
- GeneRTCA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids366 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA (PubMed:9184239).
The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product (PubMed:9184239).
Likely functions in some aspects of cellular RNA processing (PubMed:25961792, PubMed:9184239).
Function plays an important role in regulating axon regeneration by inhibiting central nervous system (CNS) axon regeneration following optic nerve injury (PubMed:25961792).
The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product (PubMed:9184239).
Likely functions in some aspects of cellular RNA processing (PubMed:25961792, PubMed:9184239).
Function plays an important role in regulating axon regeneration by inhibiting central nervous system (CNS) axon regeneration following optic nerve injury (PubMed:25961792).
Catalytic activity
- a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 104 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 131 | ATP (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 294 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 297 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 298 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 320 | Tele-AMP-histidine intermediate | ||||
Sequence: H | ||||||
Binding site | 320 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA-3'-phosphate cyclase activity | |
Biological Process | negative regulation of optical nerve axon regeneration | |
Biological Process | RNA processing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA 3'-terminal phosphate cyclase
- EC number
- Short namesRNA cyclase; RNA-3'-phosphate cyclase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00442
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
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The viewer provides 460 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000156410 | 1-366 | UniProt | RNA 3'-terminal phosphate cyclase | |||
Sequence: MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIRDLCDGQLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELHLKGGTNAEMAPQIDYTVMVFKPIVEKFGFIFNCDIKTRGYYPKGGGEVIVRMSPVKQLNPINLTERGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAFGNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLIVFMALANGVSRIKTGPVTLHTQTAIHFAEQIAKAKFIVKKSEDEEDAAKDTYIIECQGIGMTNPNL | |||||||
Modified residue (large scale data) | 173 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00442-2 | OTX2 P32243-2 | 3 | EBI-12886464, EBI-9087860 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O00442-1
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.
- Name1
- Length366
- Mass (Da)39,337
- Last updated1997-07-01 v1
- ChecksumD129E680FF08BAD1
O00442-2
- Name2
- Differences from canonical
- 48-48: L → LSSGGWKSKIKVLT
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A6NIC1 | A6NIC1_HUMAN | RTCA | 49 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 34 | in Ref. 4; AAH12604 | ||||
Sequence: L → S | ||||||
Alternative sequence | VSP_005915 | 48 | in isoform 2 | |||
Sequence: L → LSSGGWKSKIKVLT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y11651 EMBL· GenBank· DDBJ | CAA72364.1 EMBL· GenBank· DDBJ | mRNA | ||
Y11652 EMBL· GenBank· DDBJ | CAA72365.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445928 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL663111 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471097 EMBL· GenBank· DDBJ | EAW72961.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471097 EMBL· GenBank· DDBJ | EAW72962.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC012604 EMBL· GenBank· DDBJ | AAH12604.1 EMBL· GenBank· DDBJ | mRNA |