Q08189 · TGM3_MOUSE
- ProteinProtein-glutamine gamma-glutamyltransferase E
- GeneTgm3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids693 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity).
In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath
In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath
Catalytic activity
- L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N6-5-L-glutamyl-[protein] + NH4+
Cofactor
Note: Binds 3 Ca2+ cations per subunit. Binds 1 Ca2+ as a zymogen, and binds 2 more Ca2+ cations, or other divalent metal cations, after proteolytic processing.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 222 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 225 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 227 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 228 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 230 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 273 | |||||
Sequence: C | ||||||
Binding site | 302 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 306 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 308 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 325 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 331 | |||||
Sequence: H | ||||||
Active site | 354 | |||||
Sequence: D | ||||||
Binding site | 394 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 416 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 444 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 449 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 467-468 | Cleavage; by CTSL | ||||
Sequence: GA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | cornified envelope | |
Cellular Component | cytoplasm | |
Cellular Component | extrinsic component of cytoplasmic side of plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | calcium ion binding | |
Molecular Function | catalytic activity | |
Molecular Function | protein-glutamine gamma-glutamyltransferase activity | |
Molecular Function | structural molecule activity | |
Biological Process | epidermis development | |
Biological Process | hair cell differentiation | |
Biological Process | keratinization | |
Biological Process | keratinocyte differentiation | |
Biological Process | peptide cross-linking | |
Biological Process | skin development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-glutamine gamma-glutamyltransferase E
- EC number
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ08189
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000033654 | 1-467 | Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain | |||
Sequence: MSALQIQNVNWQVPMNRRAHHTDKFSSQDSIVRRGQPWEIILVCNRSLESGEDLNFIVSTGPQPSESARTKAVFSISGRSTGGWNAALKANSGNNLAIAIASPVSAPIGLYTLSVEISSRGRASSLKLGTFIMLFNPWLQADDVFMSNHAERQEYVEEDSGIIYVGSTNRIGMVGWNFGQFEEDILNISLSILDRSLNFRRDPVTDVARRNDPKYVCRVLSAMINGNDDNGVISGNWSGNYTGGVDPRTWNGSVEILKNWKKSGFRPVQFGQCWVFAGTLNTVLRCLGVPSRVITNFNSAHDTDRNLSVDVYYDAMGNPLEKGSDSVWNFHVWNEGWFVRTDLGPTYNGWQVLDATPQERSQGVFQCGPASVNAIKAGDVDRNFDMIFIFAEVNADRITWIYNNRNNTQKQNSVDTHSIGKYISTKAVGSNSRMDVTDKYKYPEGSSEERQVHQKALDKLKPNASFG | ||||||
Modified residue | 111 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 112 | Phosphothreonine | ||||
Sequence: T | ||||||
Chain | PRO_0000033655 | 468-693 | Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain | |||
Sequence: ATSSRNPEGEDKEPSISGKFKVTGILAVGKEVSLSLMLKNMTNDRKTVTMNMTAWTIVYNGTLVHEVWKDSATISLDPEEEIQYPVKIAYSQYERYLKADNMIRITAVCKVPDEAEVVVERDVILDNPALTLEVLEQAHVRKPVNVQMLFSNPLDQPVNNCVLLVEGSGLLRGSLKIDVPSLRPKEKSRIRFEIFPTRSGTKQLLADFSCNKFPAIKAMLPIDVSE |
Post-translational modification
Activated by proteolytic processing. In vitro activation is commonly achieved by cleavage with dispase, a neutral bacterial protease. Physiological activation may be catalyzed by CTSL and, to a lesser extent, by CTSS (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in skin and stomach and, at lower levels, in testis, kidney and spleen (at protein level). On the basis of its catalytic activity, detected in the epidermis, around the granular and spinous layers but not in the outermost cornified layers. In hair follicles, mainly located in the medulla and the hair cortex.
Developmental stage
Expression starts at 11.5 dpc in the early two-layered epidermis. From 12.5 dpc, mainly expressed in the periderm cells and weakly in the epidermal basal cells. After epidermis keratinization, at 15.5 to 17.5 dpc, detected in the granular, cornified layers and in the hair follicle. Also expressed in heart, lung, bone, muscle, testis and blood vessels at 12.5, 13.5, 14.5 and 16.5 dpc, respectively.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 457-483 | Disordered | ||||
Sequence: LDKLKPNASFGATSSRNPEGEDKEPSI |
Sequence similarities
Belongs to the transglutaminase superfamily. Transglutaminase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length693
- Mass (Da)77,309
- Last updated2011-05-31 v2
- Checksum834D86CD87AE0E9C
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 290 | in Ref. 1; AAA40421 | ||||
Sequence: P → R | ||||||
Sequence conflict | 409 | in Ref. 4; AAI29892/AAI29891 | ||||
Sequence: Q → P | ||||||
Sequence conflict | 573 | in Ref. 1; AAA40421 | ||||
Sequence: T → S | ||||||
Sequence conflict | 588 | in Ref. 1; AAA40421 | ||||
Sequence: R → W | ||||||
Sequence conflict | 616 | in Ref. 1; AAA40421 | ||||
Sequence: L → I | ||||||
Sequence conflict | 639 | in Ref. 1; AAA40421 | ||||
Sequence: R → G | ||||||
Sequence conflict | 682 | in Ref. 1; AAA40421 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L10385 EMBL· GenBank· DDBJ | AAA40421.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AL808127 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466519 EMBL· GenBank· DDBJ | EDL28248.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC129890 EMBL· GenBank· DDBJ | AAI29891.1 EMBL· GenBank· DDBJ | mRNA | ||
BC129891 EMBL· GenBank· DDBJ | AAI29892.1 EMBL· GenBank· DDBJ | mRNA |