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Protein

Protein-glutamine gamma-glutamyltransferase E

Gene

Tgm3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 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).By similarity

Catalytic activityi

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

Cofactori

Ca2+By similarityNote: Binds 3 Ca(2+) cations per subunit. Binds 1 Ca(2+) as a zymogen, and binds 2 more Ca2+ cations, or other divalent metal cations, after proteolytic processing.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi222 – 2221Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi225 – 2251Calcium 1By similarity
Metal bindingi227 – 2271Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi228 – 2281Calcium 1By similarity
Active sitei273 – 2731PROSITE-ProRule annotation
Metal bindingi302 – 3021Calcium 2By similarity
Metal bindingi304 – 3041Calcium 2By similarity
Metal bindingi306 – 3061Calcium 2By similarity
Metal bindingi308 – 3081Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi325 – 3251Calcium 2By similarity
Active sitei331 – 3311PROSITE-ProRule annotation
Active sitei354 – 3541PROSITE-ProRule annotation
Metal bindingi394 – 3941Calcium 3By similarity
Metal bindingi416 – 4161Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi444 – 4441Calcium 3By similarity
Metal bindingi449 – 4491Calcium 3By similarity
Sitei467 – 4682Cleavage; by CTSLBy similarity

GO - Molecular functioni

GO - Biological processi

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1561831. Tgm3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 467466Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chainPRO_0000408951Add
BLAST
Chaini468 – 693226Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chainPRO_0000408952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111PhosphotyrosineBy similarity
Modified residuei112 – 1121PhosphothreonineBy similarity

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

Keywords - PTMi

Phosphoprotein, Zymogen

Expressioni

Gene expression databases

GenevisibleiD4A5U3. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi265783. 1 interaction.
STRINGi10116.ENSRNOP00000059160.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00760000119108.
InParanoidiD4A5U3.
KOiK05620.
OMAiMVGWNFG.
OrthoDBiEOG7WT40M.
PhylomeDBiD4A5U3.
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.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
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.

D4A5U3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALEVQNIN WQMPMNRRAH HTDKFSSQDF IVRRGQPWEV ILLCNRSLES
60 70 80 90 100
GDNLNFIVST GPQPSESART KAVFSISGRN TSGWSAALKA SNGNNLFIAI
110 120 130 140 150
ASPVSAPIGL YTLNVEVSSK GRVSSVKLGT FTVLFNPWQQ GDDVFMSNHA
160 170 180 190 200
ERQEYVEEDS GIIYVGSTNR IGMVGWNFGQ FEEDILSISL SILDRSLNFR
210 220 230 240 250
RDPATDVARR NDPKYVCRVL SAMINANDDS GVLSGNWSGN YSGGVDPRTW
260 270 280 290 300
NGSVEILKNW KKSGFRPVQF GQCWVFAGTL NTVLRCLGVP SRVITNFNSA
310 320 330 340 350
HDTDRNLSVD VYYDAMGNPL EKGSDSVWNF HVWNEGWFVR TDLGPSYNGW
360 370 380 390 400
QVLDATPQER SQGVFQCGPA SVNAIKDGEV DQNFDMIFIF AEVNADRITW
410 420 430 440 450
IYNNRDGSQK QNSVDTYSIG KYISTKAVGS NSRMDVTIKY KHPEGSKEER
460 470 480 490 500
QVQQKAMNKL KPNASFGATS SRGPQGEEKE PSISGKFKVT GVLAVGKEVS
510 520 530 540 550
LALILKNTTS DRKTVTTNMT AWTIVYNGTL VHEVWKDSAT ISLDPEEEIQ
560 570 580 590 600
YPVKIAYSQY DRYLKADNMI RITAVCKVPD EAEVVVERDV ILDNPTLTLE
610 620 630 640 650
VLDQAQLRKP VVVQMLFSNP LDEPVKNCVL MVEGSGLLRG SLKIDVPALR
660 670 680 690
PKEKSRVRFE IFPTRIGIKQ LLADFSCNKF PAIKAMLVIE VSE
Length:693
Mass (Da):77,230
Last modified:April 20, 2010 - v1
Checksum:iCFE4D1B46960D4C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473949 Genomic DNA. Translation: EDL80172.1.
RefSeqiNP_001102429.1. NM_001108959.1.
UniGeneiRn.53317.

Genome annotation databases

EnsembliENSRNOT00000063828; ENSRNOP00000059160; ENSRNOG00000006753.
GeneIDi366189.
KEGGirno:366189.
UCSCiRGD:1561831. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473949 Genomic DNA. Translation: EDL80172.1.
RefSeqiNP_001102429.1. NM_001108959.1.
UniGeneiRn.53317.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi265783. 1 interaction.
STRINGi10116.ENSRNOP00000059160.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000063828; ENSRNOP00000059160; ENSRNOG00000006753.
GeneIDi366189.
KEGGirno:366189.
UCSCiRGD:1561831. rat.

Organism-specific databases

CTDi7053.
RGDi1561831. Tgm3.

Phylogenomic databases

GeneTreeiENSGT00760000119108.
InParanoidiD4A5U3.
KOiK05620.
OMAiMVGWNFG.
OrthoDBiEOG7WT40M.
PhylomeDBiD4A5U3.
TreeFamiTF324278.

Miscellaneous databases

NextBioi688908.
PROiD4A5U3.

Gene expression databases

GenevisibleiD4A5U3. RN.

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.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
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...

Publicationsi

  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].

Entry informationi

Entry nameiTGM3_RAT
AccessioniPrimary (citable) accession number: D4A5U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 20, 2010
Last modified: July 22, 2015
This is version 41 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.