A1A437 · A1A437_CANLF
- ProteinProtein-arginine deiminase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids691 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
function
Catalyzes the deimination of arginine residues of proteins.
Catalytic activity
- H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4+
Cofactor
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | calcium ion binding | |
Molecular Function | protein-arginine deiminase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-arginine deiminase
- EC number
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionA1A437
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MSFQSIIHLSLDSPVRA | ||||||
Chain | PRO_5002631718 | 18-691 | Protein-arginine deiminase | |||
Sequence: LCVLGMEICLDVNGCAPERCEAFTISSSPGVSVDLHGTLPGTGQEGTAVTRWPLSNPTDVLVKMTCPSSASDGDQVLVSYYLPNEDAPVATAVLRLTGIVVSLDVDIYRSGQVEIASDKQAKKNWVWGPSGWGAILLVNCSPADKGQIIDQKTTKVFFPEEIKSLSQMTLNVTRARRHLKKYRLVLHTSEEEARKARVYRPQRDSSSTFEVLLGPGQCTYTFAPLENNLKETFYVEAIEFPSADFSGLISYSVSLVEEPQDPSIPETLVYKDTVVFRVAPCVFIPSTQMPLEVYLCRELQVQGFVNTVMELSEKSNSQVASVYEDPNRLGRWLQDEMAFCYTQAPHRTLSLVLDTPRVLTLEDFPMKYSLSPGVGYVIQCTKDHRVASMDSIGNLMVSPPVKVEGKEYPLGRILIGSCFYPSKEGRDMSKALRDFLYAQRVQAPVELFSDWLMVGHMDEFMCFIPTPDKSEGEKGFRLLLASPSSCHRLFEEKQKEGYGDMALFEEVREDQLLSNGRQANTINQLLADKNMRKQNDYVEKCINLNRDILKKELGLVERDIIDIPQLFCLEQLTNVPSSEQTGKFFARPYFPDLLQMIVMGKNLGIPKPFGPQIKGTCCLEEKICQLLEPLGFKCTFIDDFDCYLTEIGDFCACANIRRVPFAFKWWRMVPEPQA |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-114 | Protein-arginine deiminase (PAD) N-terminal | ||||
Sequence: MSFQSIIHLSLDSPVRALCVLGMEICLDVNGCAPERCEAFTISSSPGVSVDLHGTLPGTGQEGTAVTRWPLSNPTDVLVKMTCPSSASDGDQVLVSYYLPNEDAPVATAVLRLT | ||||||
Domain | 116-274 | Protein-arginine deiminase (PAD) central | ||||
Sequence: IVVSLDVDIYRSGQVEIASDKQAKKNWVWGPSGWGAILLVNCSPADKGQIIDQKTTKVFFPEEIKSLSQMTLNVTRARRHLKKYRLVLHTSEEEARKARVYRPQRDSSSTFEVLLGPGQCTYTFAPLENNLKETFYVEAIEFPSADFSGLISYSVSLVE | ||||||
Domain | 286-683 | Protein-arginine deiminase C-terminal | ||||
Sequence: VYKDTVVFRVAPCVFIPSTQMPLEVYLCRELQVQGFVNTVMELSEKSNSQVASVYEDPNRLGRWLQDEMAFCYTQAPHRTLSLVLDTPRVLTLEDFPMKYSLSPGVGYVIQCTKDHRVASMDSIGNLMVSPPVKVEGKEYPLGRILIGSCFYPSKEGRDMSKALRDFLYAQRVQAPVELFSDWLMVGHMDEFMCFIPTPDKSEGEKGFRLLLASPSSCHRLFEEKQKEGYGDMALFEEVREDQLLSNGRQANTINQLLADKNMRKQNDYVEKCINLNRDILKKELGLVERDIIDIPQLFCLEQLTNVPSSEQTGKFFARPYFPDLLQMIVMGKNLGIPKPFGPQIKGTCCLEEKICQLLEPLGFKCTFIDDFDCYLTEIGDFCACANIRRVPFAFKWW |
Sequence similarities
Belongs to the protein arginine deiminase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length691
- Mass (Da)77,683
- Last updated2007-01-23 v1
- Checksum1809008D024898C8