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Reviewed, UniProtKB/Swiss-Prot P23606 (TGM1_RAT)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Protein-glutamine gamma-glutamyltransferase K
    EC=2.3.2.13
Alternative name(s):
    Transglutaminase K
      Short name=TGase K
      Short name=TGK
      Short name=TG(K)
    Transglutaminase-1
    Epidermal TGase
Gene names
Name: Tgm1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum.

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

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Ontologies

Keywords
   Biological processKeratinization
   Cellular componentMembrane
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processkeratinization

Inferred from electronic annotation. Source: UniProtKB-KW

peptide cross-linking Ref.1

Non-traceable author statement. Source: RGD

   Cellular componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein-glutamine gamma-glutamyltransferase activity Ref.1

Non-traceable author statement. Source: RGD

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 824824Protein-glutamine gamma-glutamyltransferase K
PRO_0000213704

Sites

Active site3851 By similarity
Active site4441 By similarity
Active site4671 By similarity
Metal binding5071Calcium By similarity
Metal binding5091Calcium By similarity
Metal binding5561Calcium By similarity
Metal binding5611Calcium By similarity

Amino acid modifications

Modified residue701Phosphoserine By similarity
Modified residue1001Phosphoserine By similarity
Modified residue1031Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P23606-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: A7D81C148CEFD938

FASTA82490,770
        10         20         30         40         50         60 
MEGPRSDVGR WGRSPWQPTT PSPEPEPEPE PDRSSRSRRG GGRSFWARCC GCCSCGNRAD 

        70         80         90        100        110        120 
DDWGPEPSGS RSRGTSSRGG GSRGGDSRGR DSRGGRRPES RGSGVNAAGD GTIREGMLVV 

       130        140        150        160        170        180 
NGVDLLCSRS DQNRREHHTD EFEYDELILR RGQPFHIILF LNREYESSDR IALELLIGNN 

       190        200        210        220        230        240 
PEVGKGTHVI IPVGKGGSGG WKAQVTKTNG HNLTLRVHTS PNAIIGKFQF TVRTRSEAGE 

       250        260        270        280        290        300 
FQLPFDPRNE IYILFNPWCP EDIVYVDHED WRQEYVLNES GRIYYGTEAQ IGERTWNYGQ 

       310        320        330        340        350        360 
FDHGVLDACL YILDRRGMPY GGRGDPVSVS RVVSAMVNSL DDNGVLIGNW TGDYSRGTNP 

       370        380        390        400        410        420 
SAWVGSVEIL LSYLRTGYSV PYGQCWVFAG VTTTVLRCLG LATRTVTNFN SAHDTDTSLT 

       430        440        450        460        470        480 
MDIYFDENMK PLEHLNHDSV WNFHVWNDCW MKRPDLPSGF DGWQVVDATP QETSSGIFCC 

       490        500        510        520        530        540 
GPCSVESIKN GLVYMKYDTP FIFAEVNSDK VYWQRQDDGS FKIVYVEEKA IGTLIVTKAI 

       550        560        570        580        590        600 
NSNMREDITH IYKHPEGSEA ERKAVEKAAA HGSKPNVYAT RDSAEDVAMQ VEAQDAVMGQ 

       610        620        630        640        650        660 
DLTVSVVLTN RGSSRRTVKL HLYLCVTYYT GVSGPTFKET KKEVVLAPGA SDTVAMPVAY 

       670        680        690        700        710        720 
KEYKPHLVDQ GAMLLNVSGH VKESGQVLAK QHTFRLRTPD LSLTLLGAAV VGQECEVQIV 

       730        740        750        760        770        780 
FKNPLPITLT NVVFRLEGSG LQRPKVLNVG DIGGNETVTL RQTFVPVRPG PRQLIASLDS 

       790        800        810        820 
PQLSQVHGVI QVDVAPSSGG RGFSEAVGDS RSGENIPMAF RGGA

« Hide

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References

« Hide 'large scale' references
[1]"Primary structure of keratinocyte transglutaminase."
Phillips M.A., Stewart B.E., Qin Q., Chakravarty R., Floyd E.E., Jetten A.M., Rice R.H.
Proc. Natl. Acad. Sci. U.S.A. 87:9333-9337(1990) [PubMed: 1979171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.

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Cross-references

Sequence databases

M57263 mRNA. Translation: AAA63495.1.
BC097305 mRNA. Translation: AAH97305.1.
IPIIPI00212729.
PIRB38423.
RefSeqNP_113847.1.
UniGeneRn.10039

3D structure databases

HSSPHSSP built from PDB template 1EVU based on UniProtKB P00488.
ModBaseSearch...

PTM databases

PhosphoSiteP23606.

Proteomic databases

PRIDEP23606.

Genome annotation databases

EnsemblENSRNOG00000020136. Rattus norvegicus. [Contig view]
GeneID60335.
KEGGrno:60335.

Organism-specific databases

RGD61838. Tgm1.

Phylogenomic databases

HOVERGENP23606.
OMAP23606. CGCCSCR.

Enzyme and pathway databases

BRENDA2.3.2.13. 248.

Gene expression databases

ArrayExpressP23606.
GermOnlineENSRNOG00000020136. Rattus norvegicus.

Family and domain databases

InterProIPR008957. Fibronectin_typ-III-like_fold.
IPR013783. Ig-like_fold.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
SMARTSM00460. TGc. 1 hit.
[Graphical view]
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio611983.

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Entry information

Entry nameTGM1_RAT
AccessionPrimary (citable) accession number: P23606
Secondary accession number(s): Q4QRA6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents