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Protein

Protein-glutamine gamma-glutamyltransferase E

Gene

Tgm3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

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

Cofactori

Ca2+By similarityNote: 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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi222Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi225Calcium 1By similarity1
Metal bindingi227Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi228Calcium 1By similarity1
Metal bindingi230Calcium 1; via carbonyl oxygenBy similarity1
Active sitei273PROSITE-ProRule annotation1
Metal bindingi302Calcium 2By similarity1
Metal bindingi304Calcium 2By similarity1
Metal bindingi306Calcium 2By similarity1
Metal bindingi308Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi325Calcium 2By similarity1
Active sitei331PROSITE-ProRule annotation1
Active sitei354PROSITE-ProRule annotation1
Metal bindingi394Calcium 3By similarity1
Metal bindingi416Calcium 3; via carbonyl oxygen1
Metal bindingi444Calcium 3By similarity1
Metal bindingi449Calcium 3By similarity1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • catalytic activity Source: UniProtKB
  • protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB

GO - Biological processi

  • cell envelope organization Source: UniProtKB
  • epidermis development Source: UniProtKB
  • hair cell differentiation Source: UniProtKB
  • keratinization Source: UniProtKB-KW
  • keratinocyte differentiation Source: UniProtKB
  • peptide cross-linking Source: UniProtKB
  • protein tetramerization Source: UniProtKB
  • skin development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Keratinization

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:Tgm3
Synonyms:Tgase3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98732. Tgm3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000336542 – 467Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chainAdd BLAST466
ChainiPRO_0000033655468 – 693Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chainAdd BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei111PhosphotyrosineBy similarity1
Modified residuei112PhosphothreonineBy similarity1

Post-translational modificationi

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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei467 – 468Cleavage; by CTSLBy similarity2

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

MaxQBiQ08189.
PaxDbiQ08189.
PeptideAtlasiQ08189.
PRIDEiQ08189.

PTM databases

iPTMnetiQ08189.
PhosphoSitePlusiQ08189.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiENSMUSG00000027401.
CleanExiMM_TGM3.
GenevisibleiQ08189. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ08189. 1 interactor.
STRINGi10090.ENSMUSP00000105928.

Structurei

3D structure databases

ProteinModelPortaliQ08189.
SMRiQ08189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IFMV. Eukaryota.
ENOG410XQEZ. LUCA.
GeneTreeiENSGT00760000119108.
HOGENOMiHOG000231695.
HOVERGENiHBG004342.
InParanoidiQ08189.
KOiK05620.
OMAiMVGWNFG.
OrthoDBiEOG091G030K.
PhylomeDBiQ08189.
TreeFamiTF324278.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR013808. Transglutaminase_AS.
IPR008958. Transglutaminase_C.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALQIQNVN WQVPMNRRAH HTDKFSSQDS IVRRGQPWEI ILVCNRSLES
60 70 80 90 100
GEDLNFIVST GPQPSESART KAVFSISGRS TGGWNAALKA NSGNNLAIAI
110 120 130 140 150
ASPVSAPIGL YTLSVEISSR GRASSLKLGT FIMLFNPWLQ ADDVFMSNHA
160 170 180 190 200
ERQEYVEEDS GIIYVGSTNR IGMVGWNFGQ FEEDILNISL SILDRSLNFR
210 220 230 240 250
RDPVTDVARR NDPKYVCRVL SAMINGNDDN GVISGNWSGN YTGGVDPRTW
260 270 280 290 300
NGSVEILKNW KKSGFRPVQF GQCWVFAGTL NTVLRCLGVP SRVITNFNSA
310 320 330 340 350
HDTDRNLSVD VYYDAMGNPL EKGSDSVWNF HVWNEGWFVR TDLGPTYNGW
360 370 380 390 400
QVLDATPQER SQGVFQCGPA SVNAIKAGDV DRNFDMIFIF AEVNADRITW
410 420 430 440 450
IYNNRNNTQK QNSVDTHSIG KYISTKAVGS NSRMDVTDKY KYPEGSSEER
460 470 480 490 500
QVHQKALDKL KPNASFGATS SRNPEGEDKE PSISGKFKVT GILAVGKEVS
510 520 530 540 550
LSLMLKNMTN DRKTVTMNMT AWTIVYNGTL VHEVWKDSAT ISLDPEEEIQ
560 570 580 590 600
YPVKIAYSQY ERYLKADNMI RITAVCKVPD EAEVVVERDV ILDNPALTLE
610 620 630 640 650
VLEQAHVRKP VNVQMLFSNP LDQPVNNCVL LVEGSGLLRG SLKIDVPSLR
660 670 680 690
PKEKSRIRFE IFPTRSGTKQ LLADFSCNKF PAIKAMLPID VSE
Length:693
Mass (Da):77,309
Last modified:May 31, 2011 - v2
Checksum:i834D86CD87AE0E9C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti290P → R in AAA40421 (PubMed:8099584).Curated1
Sequence conflicti409Q → P in AAI29892 (PubMed:15489334).Curated1
Sequence conflicti409Q → P in AAI29891 (PubMed:15489334).Curated1
Sequence conflicti573T → S in AAA40421 (PubMed:8099584).Curated1
Sequence conflicti588R → W in AAA40421 (PubMed:8099584).Curated1
Sequence conflicti616L → I in AAA40421 (PubMed:8099584).Curated1
Sequence conflicti639R → G in AAA40421 (PubMed:8099584).Curated1
Sequence conflicti682A → T in AAA40421 (PubMed:8099584).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS38240.1.
PIRiB45991.
RefSeqiNP_033400.2. NM_009374.3.
UniGeneiMm.2961.

Genome annotation databases

EnsembliENSMUST00000110299; ENSMUSP00000105928; ENSMUSG00000027401.
GeneIDi21818.
KEGGimmu:21818.
UCSCiuc008mig.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS38240.1.
PIRiB45991.
RefSeqiNP_033400.2. NM_009374.3.
UniGeneiMm.2961.

3D structure databases

ProteinModelPortaliQ08189.
SMRiQ08189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ08189. 1 interactor.
STRINGi10090.ENSMUSP00000105928.

PTM databases

iPTMnetiQ08189.
PhosphoSitePlusiQ08189.

Proteomic databases

MaxQBiQ08189.
PaxDbiQ08189.
PeptideAtlasiQ08189.
PRIDEiQ08189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110299; ENSMUSP00000105928; ENSMUSG00000027401.
GeneIDi21818.
KEGGimmu:21818.
UCSCiuc008mig.2. mouse.

Organism-specific databases

CTDi7053.
MGIiMGI:98732. Tgm3.

Phylogenomic databases

eggNOGiENOG410IFMV. Eukaryota.
ENOG410XQEZ. LUCA.
GeneTreeiENSGT00760000119108.
HOGENOMiHOG000231695.
HOVERGENiHBG004342.
InParanoidiQ08189.
KOiK05620.
OMAiMVGWNFG.
OrthoDBiEOG091G030K.
PhylomeDBiQ08189.
TreeFamiTF324278.

Miscellaneous databases

ChiTaRSiTgm3. mouse.
PROiQ08189.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027401.
CleanExiMM_TGM3.
GenevisibleiQ08189. MM.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR013808. Transglutaminase_AS.
IPR008958. Transglutaminase_C.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTGM3_MOUSE
AccessioniPrimary (citable) accession number: Q08189
Secondary accession number(s): A1L343, A2ANC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 31, 2011
Last modified: November 2, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.