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D4A5U3

- TGM3_RAT

UniProt

D4A5U3 - TGM3_RAT

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Protein

Protein-glutamine gamma-glutamyltransferase E

Gene

Tgm3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

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.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

  1. calcium ion binding Source: UniProtKB
  2. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB

GO - Biological processi

  1. cell envelope organization Source: Ensembl
  2. keratinization Source: UniProtKB-KW
  3. peptide cross-linking Source: UniProtKB
  4. protein tetramerization Source: Ensembl
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: Chromosome 3

Organism-specific databases

RGDi1561831. Tgm3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. extrinsic component of cytoplasmic side of plasma membrane Source: Ensembl
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

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.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00760000119108.
InParanoidiD4A5U3.
KOiK05620.
OMAiEILPTRS.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CH473949 Genomic DNA. Translation: EDL80172.1 .
RefSeqi NP_001102429.1. NM_001108959.1.
UniGenei Rn.53317.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 265783. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000063828 ; ENSRNOP00000059160 ; ENSRNOG00000006753 .
GeneIDi 366189.
KEGGi rno:366189.
UCSCi RGD:1561831. rat.

Organism-specific databases

CTDi 7053.
RGDi 1561831. Tgm3.

Phylogenomic databases

GeneTreei ENSGT00760000119108.
InParanoidi D4A5U3.
KOi K05620.
OMAi EILPTRS.
OrthoDBi EOG7WT40M.
PhylomeDBi D4A5U3.
TreeFami TF324278.

Miscellaneous databases

NextBioi 688908.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11590. PTHR11590. 1 hit.
Pfami PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
SMARTi SM00460. TGc. 1 hit.
[Graphical view ]
SUPFAMi SSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 34 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