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A6QP57 (TGM3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length691 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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.

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 By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain
PRO_0000408949
Chain466 – 691226Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain
PRO_0000408950

Sites

Active site2721 By similarity
Active site3301 By similarity
Active site3531 By similarity
Metal binding2211Calcium 1; via carbonyl oxygen By similarity
Metal binding2241Calcium 1 By similarity
Metal binding2261Calcium 1; via carbonyl oxygen By similarity
Metal binding2271Calcium 1 By similarity
Metal binding3011Calcium 2 By similarity
Metal binding3031Calcium 2 By similarity
Metal binding3051Calcium 2 By similarity
Metal binding3071Calcium 2; via carbonyl oxygen By similarity
Metal binding3241Calcium 2 By similarity
Metal binding3931Calcium 3 By similarity
Metal binding4141Calcium 3; via carbonyl oxygen By similarity
Metal binding4421Calcium 3 By similarity
Metal binding4471Calcium 3 By similarity
Site465 – 4662Cleavage; by CTSL

Amino acid modifications

Modified residue1101Phosphotyrosine By similarity
Modified residue1111Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6QP57 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 67DB0852E0973B4D

FASTA69176,791
        10         20         30         40         50         60 
MSGLQSVDWQ IASNRQAHHT ERFYGKDLLV RRGQLFQVSL TLSQGLSSGG RVTFTASTGP 

        70         80         90        100        110        120 
YPSESANTKA VFPLSNGTSS SGWGAQLVSS RNNVLNISIL SPANAPIGRY TLNMQISSQG 

       130        140        150        160        170        180 
SDSTLKLGTF ILLFNPWLQA DSVFMSNHAE REEYVQEDAG IIFVGSTNRI SMIGWNYGQF 

       190        200        210        220        230        240 
EEGILNICLS VLDNSLNFRR DPATDVAHRN DPKYVGRVLS AMINGNDDSG VISGNWSGSY 

       250        260        270        280        290        300 
TGGRDPRNWN GSVEILKEWQ RSGFRPVRYG QCWVFAGTLN TVLRCLGIPS RVITNFNSAH 

       310        320        330        340        350        360 
DTDQNLSVDV YYDPLGRPMD KGSDSVWNFH VWNEAWFVRS DLGPSYNGWQ VLDATPQERS 

       370        380        390        400        410        420 
QGVFQCGPAS VIAIREGNVD WDFDMPFIFA EVNADRITWI YESNGALKKN SADTHSVGKH 

       430        440        450        460        470        480 
ISTKAVGSNS RMDVTEKYKY PEGSSQERQV FEKALRKLKP TMSFSATSAS SLAREEREPS 

       490        500        510        520        530        540 
ISGRFKVAGV LTVGKEVNLI LMLKNLTSDT KTVTVNMTAW TIVYNGTLVH EVWKDSVTKS 

       550        560        570        580        590        600 
LNPEEEIEHP VKIAYAQYEK YLKADNMIRT TAVCQVTDEP EVVVERDIIL DNPTLTLEVL 

       610        620        630        640        650        660 
DEARVQKPVN VQMLFSNPLD EPVKDCVLMV EGSGLLLGNL KIDVPALRPK ERSRVRFEIL 

       670        680        690 
PTRSGTKQLL ANFSCNKFPA IKAMLSVDVA E 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Basal ganglia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC149161 mRNA. Translation: AAI49162.1.
RefSeqNP_001095318.1. NM_001101848.1.
UniGeneBt.13628.

3D structure databases

ProteinModelPortalA6QP57.
SMRA6QP57. Positions 3-691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000006432.

Proteomic databases

PaxDbA6QP57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID505080.
KEGGbta:505080.

Organism-specific databases

CTD7053.

Phylogenomic databases

eggNOGNOG80379.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidA6QP57.
KOK05620.

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

NextBio20866974.

Entry information

Entry nameTGM3_BOVIN
AccessionPrimary (citable) accession number: A6QP57
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: August 21, 2007
Last modified: March 19, 2014
This is version 41 of the entry and version 1 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