Q68EN5 · MACA1_HUMAN
- ProteinMicrotubule-associated tyrosine carboxypeptidase 1
- GeneMATCAP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids471 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:35482892).
Also able to remove the C-terminal phenylalanine residue of alpha-tubulin TUBA8 (PubMed:35482892).
Recognizes adjacent tubulin dimers along the same protofilament (PubMed:35482892).
Also able to remove the C-terminal phenylalanine residue of alpha-tubulin TUBA8 (PubMed:35482892).
Recognizes adjacent tubulin dimers along the same protofilament (PubMed:35482892).
Catalytic activity
- C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + L-tyrosineThis reaction proceeds in the forward direction.
- C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-phenylalanyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + L-phenylalanineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Molecular Function | metallocarboxypeptidase activity | |
Molecular Function | tubulin-tyrosine carboxypeptidase | |
Biological Process | brain development | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-associated tyrosine carboxypeptidase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ68EN5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associates with microtubules.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 219 | Reduced binding to microtubules. | ||||
Sequence: K → E | ||||||
Mutagenesis | 223 | Reduced binding to microtubules. | ||||
Sequence: W → A | ||||||
Mutagenesis | 227 | Reduced binding to microtubules. | ||||
Sequence: R → A | ||||||
Mutagenesis | 280 | Abolished tyrosine carboxypeptidase activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 281 | Abolished tyrosine carboxypeptidase activity. | ||||
Sequence: E → A or Q | ||||||
Mutagenesis | 285 | Abolished tyrosine carboxypeptidase activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 316 | Abolished tyrosine carboxypeptidase activity. | ||||
Sequence: E → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 547 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000320619 | 1-471 | Microtubule-associated tyrosine carboxypeptidase 1 | |||
Sequence: MVLDSGAQAYDQAPPSPPTSPPSLRHRLKPSDRDGPPLYPWSQSLALPLALAVPPALQPQPEQQPFSQMLLGHRGHMRRSESTYSVNSTGRRGRGTLGRPPPGRGRNPGGGTLRPAASLPHIAKTQRDAGHIASKSPCMLVALRPTNMDRERDKFFQSHYTYNPQFEYQEPMPTAVLEKYCEASGQFIHQAVGIIEAVLEKFGTYEHFEAATGGQLLTKCQIWSIVRKYMQKEGCAGEVVVQLSEDLLSQAVMMVENSRPTLAINLTGARQYWLEGMLRHEIGTHYLRGVNNARQPWHNAEGRLRYGLRPANPTEEGLASLHSVLFRKQPFLWRAALLYYTIHRAARMSFRQLFQDLERYVQDADVRWEYCVRAKRGQTDTSLPGCFSKDQVYLDGIVRILRHRQTIDFPLLTSLGKVSYEDVDHLRPHGVLDNTRVPHFMQDLARYRQQLEHIMATNRLDEAELGRLLPD |
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q68EN5 | ZBTB8B Q8NAP8 | 3 | EBI-17494528, EBI-17494306 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-40 | Disordered | ||||
Sequence: MVLDSGAQAYDQAPPSPPTSPPSLRHRLKPSDRDGPPLYP | ||||||
Region | 76-116 | Disordered | ||||
Sequence: HMRRSESTYSVNSTGRRGRGTLGRPPPGRGRNPGGGTLRPA |
Domain
Metalloprotease with an atypical HExxxH zinc-binding motif instead of HExxH, which interrupts the active site-containing helix without affecting the integrity of the catalytic site arrangement.
The N-terminal disordered region enhances its anchoring on microtubules, while dampening processivity on the polymerized substrate.
Sequence similarities
Belongs to the peptidase MATCAP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q68EN5-1
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
- Length471
- Mass (Da)53,446
- Last updated2004-10-11 v1
- ChecksumC60BC58B867DB156
Q68EN5-2
- Name2
Q68EN5-3
- Name3
- Differences from canonical
- 1-282: MVLDSGAQAYDQAPPSPPTSPPSLRHRLKPSDRDGPPLYPWSQSLALPLALAVPPALQPQPEQQPFSQMLLGHRGHMRRSESTYSVNSTGRRGRGTLGRPPPGRGRNPGGGTLRPAASLPHIAKTQRDAGHIASKSPCMLVALRPTNMDRERDKFFQSHYTYNPQFEYQEPMPTAVLEKYCEASGQFIHQAVGIIEAVLEKFGTYEHFEAATGGQLLTKCQIWSIVRKYMQKEGCAGEVVVQLSEDLLSQAVMMVENSRPTLAINLTGARQYWLEGMLRHEI → MTVQDDMGTQDVGQGGICILVPRRAGGNVSLGEFVHVCGCVGVGWGADGWERIHVCEPLWILGCESTGGGASRCLGLGEPVCEPEFRSMRMEVSRPEPRPDGTGPGLGSQAGPRTPRPAPPPLAFPA
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
I3L230 | I3L230_HUMAN | MATCAP1 | 205 |
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_031689 | 1-282 | in isoform 3 | |||
Sequence: MVLDSGAQAYDQAPPSPPTSPPSLRHRLKPSDRDGPPLYPWSQSLALPLALAVPPALQPQPEQQPFSQMLLGHRGHMRRSESTYSVNSTGRRGRGTLGRPPPGRGRNPGGGTLRPAASLPHIAKTQRDAGHIASKSPCMLVALRPTNMDRERDKFFQSHYTYNPQFEYQEPMPTAVLEKYCEASGQFIHQAVGIIEAVLEKFGTYEHFEAATGGQLLTKCQIWSIVRKYMQKEGCAGEVVVQLSEDLLSQAVMMVENSRPTLAINLTGARQYWLEGMLRHEI → MTVQDDMGTQDVGQGGICILVPRRAGGNVSLGEFVHVCGCVGVGWGADGWERIHVCEPLWILGCESTGGGASRCLGLGEPVCEPEFRSMRMEVSRPEPRPDGTGPGLGSQAGPRTPRPAPPPLAFPA | ||||||
Alternative sequence | VSP_031690 | 385-408 | in isoform 2 | |||
Sequence: GCFSKDQVYLDGIVRILRHRQTID → ARTRCTWTASCAFCDIARPSISRC | ||||||
Alternative sequence | VSP_031691 | 409-471 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK092303 EMBL· GenBank· DDBJ | BAC03856.1 EMBL· GenBank· DDBJ | mRNA | ||
AL834156 EMBL· GenBank· DDBJ | CAD38862.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
CH471092 EMBL· GenBank· DDBJ | EAW83091.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007594 EMBL· GenBank· DDBJ | AAH07594.1 EMBL· GenBank· DDBJ | mRNA | ||
BC080183 EMBL· GenBank· DDBJ | AAH80183.1 EMBL· GenBank· DDBJ | mRNA | ||
BC128539 EMBL· GenBank· DDBJ | AAI28540.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |