Q04609 · FOLH1_HUMAN
- ProteinGlutamate carboxypeptidase 2
- GeneFOLH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids750 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Catalytic activity
Cofactor
Activity regulation
pH Dependence
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 210 | substrate | ||||
Sequence: R | ||||||
Binding site | 257 | substrate | ||||
Sequence: N | ||||||
Binding site | 269 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 272 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 377 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 387 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 387 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 424 | Nucleophile; for NAALADase activity | ||||
Sequence: E | ||||||
Binding site | 424 | substrate | ||||
Sequence: E | ||||||
Binding site | 425 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 433 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 436 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 453 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 517-518 | substrate | ||||
Sequence: SG | ||||||
Binding site | 519 | substrate | ||||
Sequence: N | ||||||
Binding site | 534-536 | substrate | ||||
Sequence: RAR | ||||||
Binding site | 552 | substrate | ||||
Sequence: Y | ||||||
Binding site | 552-553 | substrate | ||||
Sequence: YH | ||||||
Binding site | 553 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 628 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 666 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 689 | Charge relay system | ||||
Sequence: H | ||||||
Binding site | 699-700 | substrate | ||||
Sequence: KY |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | Ac-Asp-Glu binding | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | dipeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metallocarboxypeptidase activity | |
Molecular Function | peptidase activity | |
Molecular Function | tetrahydrofolyl-poly(glutamate) polymer binding | |
Biological Process | C-terminal protein deglutamylation | |
Biological Process | folic acid-containing compound metabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlutamate carboxypeptidase 2
- 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 accessionQ04609
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform PSMA'
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-19 | Cytoplasmic | ||||
Sequence: MWNLLHETDSAVATARRPR | ||||||
Transmembrane | 20-43 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: WLCAGALVLAGGFFLLGFLFGWFI | ||||||
Topological domain | 44-750 | Extracellular | ||||
Sequence: KSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_036398 | 23 | in a colorectal cancer sample; somatic mutation | |||
Sequence: A → T | ||||||
Mutagenesis | 51 | Loss of glycosylation. Reduces enzyme activity. | ||||
Sequence: N → A | ||||||
Natural variant | VAR_024592 | 75 | in dbSNP:rs202676 | |||
Sequence: Y → H | ||||||
Mutagenesis | 76 | Loss of glycosylation. Reduces enzyme activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 121 | Loss of glycosylation. Severely reduced enzyme activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 140 | Loss of glycosylation. Severely reduced enzyme activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 153 | Loss of glycosylation. Severely reduced enzyme activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 195 | Loss of glycosylation. Severely reduced enzyme activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 336 | Loss of glycosylation. Reduces enzyme activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 377 | Complete loss of activity. | ||||
Sequence: H → A, G, or Q | ||||||
Mutagenesis | 379 | Complete loss of activity. | ||||
Sequence: D → E or N | ||||||
Mutagenesis | 387 | Complete loss of activity. | ||||
Sequence: D → E or L | ||||||
Mutagenesis | 387 | No effect on enzyme activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 388 | No effect on enzyme activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 424 | Complete loss of activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 424 | Reduces enzyme activity. | ||||
Sequence: E → D | ||||||
Mutagenesis | 424 | Reduces enzyme activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 425 | Complete loss of activity. | ||||
Sequence: E → Q or D | ||||||
Mutagenesis | 453 | Complete loss of activity. | ||||
Sequence: D → N or L | ||||||
Mutagenesis | 453 | Reduces enzyme activity. | ||||
Sequence: D → Q | ||||||
Mutagenesis | 454 | Reduces enzyme activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 459 | Loss of glycosylation. Reduces enzyme activity. | ||||
Sequence: N → A | ||||||
Natural variant | VAR_012736 | 475 | correlates with lower folate and higher homocysteine levels; dbSNP:rs61886492 | |||
Sequence: H → Y | ||||||
Mutagenesis | 476 | Loss of glycosylation. Reduces enzyme activity. | ||||
Sequence: N → A | ||||||
Natural variant | VAR_028882 | 627 | in dbSNP:rs2988342 | |||
Sequence: V → L | ||||||
Mutagenesis | 638 | Loss of glycosylation. Abolishes enzyme activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 640 | Abolishes enzyme activity. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 890 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000174117 | 1-750 | UniProt | Glutamate carboxypeptidase 2 | |||
Sequence: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA | |||||||
Modified residue | 10 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 51 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 76 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 121 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 140 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 153 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 195 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 336 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 459 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 476 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 638 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q04609-8 | TTMP Q5BVD1 | 3 | EBI-13060980, EBI-10243654 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 274-587 | NAALADase | ||||
Sequence: ANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFEL |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing.
Q04609-1
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.
- NamePSMA-1
- Length750
- Mass (Da)84,331
- Last updated1994-06-01 v1
- ChecksumAD8C0A7DBF47901A
Q04609-3
- NamePSMA-3
- Differences from canonical
- 657-750: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA → MSSMLQAATTSMQGSHSQEFMMLCLILKAKWTLPRPGEK
Q04609-4
- NamePSMA-4
Q04609-6
- NamePSMA'
- Differences from canonical
- 1-57: Missing
Q04609-7
- NamePSMA-7
- Differences from canonical
- 1-39: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF → MTAGSSYPLFLAAYACTGCLAERL
Q04609-8
- NamePSMA-8
- Differences from canonical
- 657-688: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR → K
Q04609-9
- NamePSMA-9
- SynonymsPSM-E
Q04609-10
- Name10
- Differences from canonical
- 1-308: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_038058 | 1-39 | in isoform PSMA-7 and isoform PSMA-9 | |||
Sequence: MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLF → MTAGSSYPLFLAAYACTGCLAERL | ||||||
Alternative sequence | VSP_005336 | 1-57 | in isoform PSMA' | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_044287 | 1-308 | in isoform 10 | |||
Sequence: Missing | ||||||
Sequence conflict | 194 | in Ref. 9; AAZ66619 | ||||
Sequence: I → V | ||||||
Alternative sequence | VSP_040243 | 214-243 | in isoform PSMA-4 | |||
Sequence: VKNAQLAGAKGVILYSDPADYFAPGVKSYP → NMLIGVELQRLLVFQVFLFIQLDTMMHRSS | ||||||
Alternative sequence | VSP_040244 | 244-750 | in isoform PSMA-4 | |||
Sequence: Missing | ||||||
Sequence conflict | 354 | in Ref. 1; AA sequence | ||||
Sequence: R → K | ||||||
Sequence conflict | 398 | in Ref. 8; ABO93402 | ||||
Sequence: I → N | ||||||
Alternative sequence | VSP_038059 | 657-688 | in isoform PSMA-8 and isoform PSMA-9 | |||
Sequence: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYR → K | ||||||
Alternative sequence | VSP_040245 | 657-750 | in isoform PSMA-3 | |||
Sequence: NPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA → MSSMLQAATTSMQGSHSQEFMMLCLILKAKWTLPRPGEK |
Polymorphism
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M99487 EMBL· GenBank· DDBJ | AAA60209.1 EMBL· GenBank· DDBJ | mRNA | ||
S76978 EMBL· GenBank· DDBJ | AAB33750.2 EMBL· GenBank· DDBJ | mRNA | ||
AF007544 EMBL· GenBank· DDBJ | AAC83972.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF176574 EMBL· GenBank· DDBJ | AAD51121.1 EMBL· GenBank· DDBJ | mRNA | ||
EF488811 EMBL· GenBank· DDBJ | ABO93402.2 EMBL· GenBank· DDBJ | mRNA | ||
AY101595 EMBL· GenBank· DDBJ | AAM34479.1 EMBL· GenBank· DDBJ | mRNA | ||
AF107214 EMBL· GenBank· DDBJ | AAF31167.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
DQ088979 EMBL· GenBank· DDBJ | AAZ66619.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312366 EMBL· GenBank· DDBJ | BAG35284.1 EMBL· GenBank· DDBJ | mRNA | ||
AK295368 EMBL· GenBank· DDBJ | BAH12048.1 EMBL· GenBank· DDBJ | mRNA | ||
AK295470 EMBL· GenBank· DDBJ | BAH12079.1 EMBL· GenBank· DDBJ | mRNA | ||
AC110742 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC118273 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471064 EMBL· GenBank· DDBJ | EAW67858.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW67861.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW67857.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW67859.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC025672 EMBL· GenBank· DDBJ | AAH25672.1 EMBL· GenBank· DDBJ | mRNA | ||
AF254357 EMBL· GenBank· DDBJ | AAF71357.1 EMBL· GenBank· DDBJ | mRNA | ||
AF254358 EMBL· GenBank· DDBJ | AAF71358.1 EMBL· GenBank· DDBJ | mRNA |