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Q08189 (TGM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Gene names
Name:Tgm3
Synonyms:Tgase3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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.

Catalytic activity

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

Cofactor

Binds 3 calcium ions per subunit. Binds 1 calcium ion as a zymogen, and binds 2 more calcium ions, or other divalent metal cations, after proteolytic processing By similarity.

Subunit structure

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

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. Ref.5 Ref.7

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. Ref.6

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 caution

The sequence AAA40421.1 differs from that shown. Reason: Frameshift at positions 637 and 650.

Ontologies

Keywords
   Biological processKeratinization
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell envelope organization

Inferred from sequence or structural similarity. Source: UniProtKB

epidermis development

Traceable author statement Ref.6. Source: UniProtKB

hair cell differentiation

Traceable author statement Ref.6. Source: UniProtKB

keratinization

Inferred from electronic annotation. Source: UniProtKB-KW

keratinocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

peptide cross-linking

Inferred from sequence or structural similarity. Source: UniProtKB

protein tetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

skin development

Traceable author statement Ref.6. Source: UniProtKB

   Cellular_componentcornified envelope

Traceable author statement Ref.6. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extrinsic component of cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from electronic annotation. Source: Ensembl

GTPase activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

catalytic activity

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: Ensembl

protein-glutamine gamma-glutamyltransferase activity

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

Complete GO annotation...

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_0000033654
Chain468 – 693226Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain
PRO_0000033655

Sites

Active site2731 By similarity
Active site3311 By similarity
Active site3541 By similarity
Metal binding2221Calcium 1; via carbonyl oxygen By similarity
Metal binding2251Calcium 1 By similarity
Metal binding2271Calcium 1; via carbonyl oxygen By similarity
Metal binding2281Calcium 1 By similarity
Metal binding2301Calcium 1; via carbonyl oxygen By similarity
Metal binding3021Calcium 2 By similarity
Metal binding3041Calcium 2 By similarity
Metal binding3061Calcium 2 By similarity
Metal binding3081Calcium 2; via carbonyl oxygen By similarity
Metal binding3251Calcium 2 By similarity
Metal binding3941Calcium 3 By similarity
Metal binding4161Calcium 3; via carbonyl oxygen
Metal binding4441Calcium 3 By similarity
Metal binding4491Calcium 3 By similarity
Site467 – 4682Cleavage; by CTSL By similarity

Amino acid modifications

Modified residue1111Phosphotyrosine By similarity
Modified residue1121Phosphothreonine By similarity

Experimental info

Sequence conflict2901P → R in AAA40421. Ref.1
Sequence conflict4091Q → P in AAI29892. Ref.4
Sequence conflict4091Q → P in AAI29891. Ref.4
Sequence conflict5731T → S in AAA40421. Ref.1
Sequence conflict5881R → W in AAA40421. Ref.1
Sequence conflict6161L → I in AAA40421. Ref.1
Sequence conflict6391R → G in AAA40421. Ref.1
Sequence conflict6821A → T in AAA40421. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q08189 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: 834D86CD87AE0E9C

FASTA69377,309
        10         20         30         40         50         60 
MSALQIQNVN WQVPMNRRAH HTDKFSSQDS IVRRGQPWEI ILVCNRSLES GEDLNFIVST 

        70         80         90        100        110        120 
GPQPSESART KAVFSISGRS TGGWNAALKA NSGNNLAIAI ASPVSAPIGL YTLSVEISSR 

       130        140        150        160        170        180 
GRASSLKLGT FIMLFNPWLQ ADDVFMSNHA ERQEYVEEDS GIIYVGSTNR IGMVGWNFGQ 

       190        200        210        220        230        240 
FEEDILNISL SILDRSLNFR RDPVTDVARR NDPKYVCRVL SAMINGNDDN GVISGNWSGN 

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

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

       370        380        390        400        410        420 
SQGVFQCGPA SVNAIKAGDV DRNFDMIFIF AEVNADRITW IYNNRNNTQK QNSVDTHSIG 

       430        440        450        460        470        480 
KYISTKAVGS NSRMDVTDKY KYPEGSSEER QVHQKALDKL KPNASFGATS SRNPEGEDKE 

       490        500        510        520        530        540 
PSISGKFKVT GILAVGKEVS LSLMLKNMTN DRKTVTMNMT AWTIVYNGTL VHEVWKDSAT 

       550        560        570        580        590        600 
ISLDPEEEIQ YPVKIAYSQY ERYLKADNMI RITAVCKVPD EAEVVVERDV ILDNPALTLE 

       610        620        630        640        650        660 
VLEQAHVRKP VNVQMLFSNP LDQPVNNCVL LVEGSGLLRG SLKIDVPSLR PKEKSRIRFE 

       670        680        690 
IFPTRSGTKQ LLADFSCNKF PAIKAMLPID VSE 

« Hide

References

« Hide 'large scale' references
[1]"The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse."
Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M.
J. Biol. Chem. 268:12682-12690(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Epidermis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]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].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse tissues and cell lines."
Hitomi K., Horio Y., Ikura K., Yamanishi K., Maki M.
Int. J. Biochem. Cell Biol. 33:491-498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Transglutaminase 3 expression in C57BL/6J mouse embryo epidermis and the correlation with its differentiation."
Zhang J., Zhi H.Y., Ding F., Luo A.P., Liu Z.H.
Cell Res. 15:105-110(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[7]"Identification of a preferred substrate peptide for transglutaminase 3 and detection of in situ activity in skin and hair follicles."
Yamane A., Fukui M., Sugimura Y., Itoh M., Alea M.P., Thomas V., El Alaoui S., Akiyama M., Hitomi K.
FEBS J. 277:3564-3574(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10385 mRNA. Translation: AAA40421.1. Frameshift.
AL808127 Genomic DNA. Translation: CAM19029.1.
CH466519 Genomic DNA. Translation: EDL28248.1.
BC129890 mRNA. Translation: AAI29891.1.
BC129891 mRNA. Translation: AAI29892.1.
PIRB45991.
RefSeqNP_033400.2. NM_009374.3.
UniGeneMm.2961.

3D structure databases

ProteinModelPortalQ08189.
SMRQ08189. Positions 2-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000105928.

PTM databases

PhosphoSiteQ08189.

Proteomic databases

PaxDbQ08189.
PRIDEQ08189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000110299; ENSMUSP00000105928; ENSMUSG00000027401.
GeneID21818.
KEGGmmu:21818.
UCSCuc008mig.1. mouse.

Organism-specific databases

CTD7053.
MGIMGI:98732. Tgm3.

Phylogenomic databases

eggNOGNOG80379.
GeneTreeENSGT00740000115034.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidA1L343.
KOK05620.
OMAEILPTRS.
OrthoDBEOG7WT40M.
PhylomeDBQ08189.
TreeFamTF324278.

Gene expression databases

BgeeQ08189.
CleanExMM_TGM3.
GenevestigatorQ08189.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
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]
SUPFAMSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301228.
PROQ08189.
SOURCESearch...

Entry information

Entry nameTGM3_MOUSE
AccessionPrimary (citable) accession number: Q08189
Secondary accession number(s): A1L343, A2ANC3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 31, 2011
Last modified: April 16, 2014
This is version 116 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot