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Reviewed, UniProtKB/Swiss-Prot Q08188 (TGM3_HUMAN)

Last modified November 25, 2008. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-glutamine gamma-glutamyltransferase E
      Short name=TGase E
      Short name=TGE
      Short name=TG(E)
    EC=2.3.2.13
Alternative name(s):
    Transglutaminase-3
Cleaved into the following 2 chains:
    1- Recommended name:
            Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
    2- Recommended name:
            Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain
Gene names
Name: TGM3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. It is responsible for the later stages of cell envelope formation in the epidermis and the hair follicle.

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH(3).

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

This enzyme consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide.

Post-translational modification

Activated by proteolytic processing.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 470469Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
PRO_0000033652
Chain471 – 693223Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain
PRO_0000033653

Sites

Active site2731 By similarity
Active site3311 By similarity
Active site3541 By similarity
Metal binding3941Calcium By similarity
Metal binding3961Calcium By similarity
Metal binding4441Calcium By similarity
Metal binding4491Calcium By similarity

Amino acid modifications

Modified residue21N-acetylalanine

Natural variations

Natural variant131K → T: dbSNP rs214803.
VAR_040067
Natural variant1631I → L: dbSNP rs6048066.
VAR_040068
Natural variant2491S → N: dbSNP rs214814.
VAR_040069
Natural variant5621K → R: dbSNP rs1042617.
VAR_040070
Natural variant6541R → G: dbSNP rs214830.
VAR_040071

Experimental info

Sequence conflict58 – 592VS → DT in AAA61155. Ref.1
Sequence conflict2511N → G in AAA61155. Ref.1
Sequence conflict3241S → G in BAF84040. Ref.2
Sequence conflict3461S → P in AAA61155. Ref.1
Sequence conflict6741D → G in BAF84040. Ref.2

Secondary structure

.................................................................................................................. 693
Helix Strand Turn

Details...