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D4A5U3 (TGM3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase E
EC=2.3.2.13
Alternative name(s):
Transglutaminase E
Short name=TG(E)
Short name=TGE
Short name=TGase E
Transglutaminase-3
Short name=TGase-3

Cleaved into the following 2 chains:

  1. Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain
  2. Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain
Gene names
Name:Tgm3
Synonyms:Tgase3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

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

General annotation (Comments)

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 and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold. In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath By similarity.

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide By similarity.

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.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 467466Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain
PRO_0000408951
Chain468 – 693226Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain
PRO_0000408952

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
Site467 – 4682Cleavage; by CTSL By similarity

Amino acid modifications

Modified residue1111Phosphotyrosine By similarity
Modified residue1121Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
D4A5U3 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: CFE4D1B46960D4C2

FASTA69377,230
        10         20         30         40         50         60 
MSALEVQNIN WQMPMNRRAH HTDKFSSQDF IVRRGQPWEV ILLCNRSLES GDNLNFIVST 

        70         80         90        100        110        120 
GPQPSESART KAVFSISGRN TSGWSAALKA SNGNNLFIAI ASPVSAPIGL YTLNVEVSSK 

       130        140        150        160        170        180 
GRVSSVKLGT FTVLFNPWQQ GDDVFMSNHA ERQEYVEEDS GIIYVGSTNR IGMVGWNFGQ 

       190        200        210        220        230        240 
FEEDILSISL SILDRSLNFR RDPATDVARR NDPKYVCRVL SAMINANDDS GVLSGNWSGN 

       250        260        270        280        290        300 
YSGGVDPRTW NGSVEILKNW KKSGFRPVQF GQCWVFAGTL NTVLRCLGVP SRVITNFNSA 

       310        320        330        340        350        360 
HDTDRNLSVD VYYDAMGNPL EKGSDSVWNF HVWNEGWFVR TDLGPSYNGW QVLDATPQER 

       370        380        390        400        410        420 
SQGVFQCGPA SVNAIKDGEV DQNFDMIFIF AEVNADRITW IYNNRDGSQK QNSVDTYSIG 

       430        440        450        460        470        480 
KYISTKAVGS NSRMDVTIKY KHPEGSKEER QVQQKAMNKL KPNASFGATS SRGPQGEEKE 

       490        500        510        520        530        540 
PSISGKFKVT GVLAVGKEVS LALILKNTTS DRKTVTTNMT AWTIVYNGTL VHEVWKDSAT 

       550        560        570        580        590        600 
ISLDPEEEIQ YPVKIAYSQY DRYLKADNMI RITAVCKVPD EAEVVVERDV ILDNPTLTLE 

       610        620        630        640        650        660 
VLDQAQLRKP VVVQMLFSNP LDEPVKNCVL MVEGSGLLRG SLKIDVPALR PKEKSRVRFE 

       670        680        690 
IFPTRIGIKQ LLADFSCNKF PAIKAMLVIE VSE

« Hide

References

[1]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH473949 Genomic DNA. Translation: EDL80172.1.
IPIIPI00951867.
RefSeqNP_001102429.1. NM_001108959.1.
UniGeneRn.53317.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000063828; ENSRNOP00000059160; ENSRNOG00000006753.
GeneID366189.
KEGGrno:366189.
UCSCRGD:1561831. rat.

Organism-specific databases

CTD7053.
RGD1561831. Tgm3.

Phylogenomic databases

GeneTreeENSGT00690000101863.
KOK05620.
OrthoDBEOG4GMTWG.

Gene expression databases

ArrayExpressD4A5U3.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERPTHR11590. PTHR11590. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFPIRSF000459. TGM_EBP42. 1 hit.
SMARTSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMSSF81296. Ig_E-set. 1 hit.
SSF49309. Transglut_C. 2 hits.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio688908.

Entry information

Entry nameTGM3_RAT
AccessionPrimary (citable) accession number: D4A5U3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 20, 2010
Last modified: March 6, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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