Protein-glutamine gamma-glutamyltransferase E precursor

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Q08189 (TGM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:

Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain
Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain

Gene names

Name:	Tgm3
Synonyms:	Tgase3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 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.
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 process	Keratinization
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell envelope organization Inferred from sequence or structural similarity. 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_component	cornified envelope Traceable author statement Ref.6. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB extrinsic to internal side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GDP binding Inferred from sequence or structural similarity. Source: UniProtKB GTP binding Inferred from sequence or structural similarity. Source: UniProtKB GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein-glutamine gamma-glutamyltransferase activity Inferred from sequence or structural similarity Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 467

466

Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain

PRO_0000033654

Chain

468 – 693

226

Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain

PRO_0000033655

Sites

Active site

273

By similarity

Active site

331

By similarity

Active site

354

By similarity

Metal binding

394

Calcium By similarity

Metal binding

396

Calcium By similarity

Metal binding

444

Calcium By similarity

Metal binding

449

Calcium By similarity

Site

467 – 468

Cleavage; by CTSL By similarity

Amino acid modifications

Modified residue

111

Phosphotyrosine By similarity

Modified residue

112

Phosphothreonine By similarity

Experimental info

Sequence conflict

290

P → R in AAA40421. Ref.1

Sequence conflict

409

Q → P in AAI29892. Ref.4

Sequence conflict

409

Q → P in AAI29891. Ref.4

Sequence conflict

573

T → S in AAA40421. Ref.1

Sequence conflict

588

R → W in AAA40421. Ref.1

Sequence conflict

616

L → I in AAA40421. Ref.1

Sequence conflict

639

R → G in AAA40421. Ref.1

Sequence conflict

682

A → T in AAA40421. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q08189 [UniParc].

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

693

77,309

        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' referencesShow '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. 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.
IPI	IPI00117475.
PIR	B45991.
RefSeq	NP_033400.2. NM_009374.2.
UniGene	Mm.2961.
3D structure databases
ProteinModelPortal	Q08189.
SMR	Q08189. Positions 2-693.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000105928.
PTM databases
PhosphoSite	Q08189.
Proteomic databases
PaxDb	Q08189.
PRIDE	Q08189.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000110299; ENSMUSP00000105928; ENSMUSG00000027401.
GeneID	21818.
KEGG	mmu:21818.
Organism-specific databases
CTD	7053.
MGI	MGI:98732. Tgm3.
Phylogenomic databases
eggNOG	NOG80379.
GeneTree	ENSGT00690000101863.
HOGENOM	HOG000231695.
HOVERGEN	HBG004342.
InParanoid	A1L343.
KO	K05620.
OMA	LVHEVWK.
OrthoDB	EOG4GMTWG.
Gene expression databases
Bgee	Q08189.
CleanEx	MM_TGM3.
Genevestigator	Q08189.
GermOnline	ENSMUSG00000027401. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 3 hits.
InterPro	IPR023608. 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]
PANTHER	PTHR11590. PTHR11590. 1 hit.
Pfam	PF00927. Transglut_C. 2 hits. PF01841. Transglut_core. 1 hit. PF00868. Transglut_N. 1 hit. [Graphical view]
PIRSF	PIRSF000459. TGM_EBP42. 1 hit.
SMART	SM00460. TGc. 1 hit. [Graphical view]
SUPFAM	SSF81296. Ig_E-set. 1 hit. SSF49309. Transglut_C. 2 hits.
PROSITE	PS00547. TRANSGLUTAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	301228.
SOURCE	Search...

Entry information

Entry name

TGM3_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents