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P22758 (TGM1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase K
EC=2.3.2.13
Alternative name(s):
Epidermal TGase
Transglutaminase K
Short name=TG(K)
Short name=TGK
Short name=TGase K
Transglutaminase-1
Short name=TGase-1
Gene names
Name:TGM1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length836 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Enzyme regulation

Inhibited by retinoic acid, but phorbol ester treatment activates it.

Subcellular location

Membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
   Biological processKeratinization
   Cellular componentMembrane
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processkeratinization

Inferred from electronic annotation. Source: UniProtKB-KW

peptide cross-linking

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein-glutamine gamma-glutamyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 836836Protein-glutamine gamma-glutamyltransferase K
PRO_0000213703

Sites

Active site3971 By similarity
Active site4561 By similarity
Active site4791 By similarity
Metal binding5191Calcium By similarity
Metal binding5211Calcium By similarity
Metal binding5681Calcium By similarity
Metal binding5731Calcium By similarity

Amino acid modifications

Modified residue481Phosphoserine By similarity
Modified residue981Phosphoserine By similarity
Modified residue1121Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P22758 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: B3D281F7BECB9C00

FASTA83691,935
        10         20         30         40         50         60 
MDGPRSDMGR SDVSRSDMSR SDMGRSDMGR SDVGRCGGGP LQPSATPSPE PEPEPEPEPD 

        70         80         90        100        110        120 
RGSRSRGGRG RSFWARCCGC CSCRNAADDD WGREPSDSRD RGSSSRGGRP DSRGGGVNAA 

       130        140        150        160        170        180 
GDGTIREGML VVTGVDLLSS RSDQNRREHH TDEFEYEELI VRRGQPFHLV LFLSRPYESS 

       190        200        210        220        230        240 
DRIALELQIG NNPEVGKGTH VIIPVGKGNS GGWKAQVTKA SGQTLNLRVH SPASAIIGKF 

       250        260        270        280        290        300 
QFTVRTRTEA GEFQLPFDPR NEIYILFNPW CPEDIVYVDH EDWRQDYVLN ESGRIYYGTE 

       310        320        330        340        350        360 
AQIGERTWNY GQFDHGVLDA CLYILDRRGM PYGGRGDPVS VSRVISAMVN SLDDNGVLIG 

       370        380        390        400        410        420 
NWSGDYSRGT NPSAWVGSVE ILLSYLRTGY SVPYGQCWVF AGVTTTVLRC LGLATRTVTN 

       430        440        450        460        470        480 
FNSAHDTDTS LTMDIYFDEN MKPLEHLNRD SVWNFHVWND CWMKRPDLPS GFDGWQVVDA 

       490        500        510        520        530        540 
TPQETSSGIF CCGPCSVESV KNGLVYMKYD TPFIFAEVNS DKVYWQRQDD GSFKIVYVEE 

       550        560        570        580        590        600 
KAIGTLIVTK AVRSHMREDI THIYKHPEGS DAERKAVETA AAHGSKPNVY DSRDSAEDVA 

       610        620        630        640        650        660 
MQVEAQDAVM GQDLTVSVVL TNRSSSRRTV KLHLYLSVTF YTGVTGSIFK ESKKEVVLAA 

       670        680        690        700        710        720 
GSSDSVVMPV AYKEYRPHLV DQGAMLLNVS GHVKESGQVL AKQHTFRVRT PDLSLTLLGA 

       730        740        750        760        770        780 
AVVGQECEVQ IVFRNPLPIT LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQTFVPVR 

       790        800        810        820        830 
PGPRQLIASL DSPQLSQVHG VIQVDVAPAS GGRGFLHAGG DSYSGETIPM TSRGEA

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References

[1]"Regulation of transglutaminase type I expression in squamous differentiating rabbit tracheal epithelial cells and human epidermal keratinocytes: effects of retinoic acid and phorbol esters."
Saunders N.A., Bernacki S.H., Vollberg T.M., Jetten A.M.
Mol. Endocrinol. 7:387-398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Tracheobronchial epithelium.
[2]"Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids."
Floyd E.E., Jetten A.M.
Mol. Cell. Biol. 9:4846-4851(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-749.
[3]"The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones."
Kim H.C., Idler W.W., Kim I.-G., Han J.H., Chung S.-I., Steinert P.M.
J. Biol. Chem. 266:536-539(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L10714 mRNA. No translation available.
M30468 mRNA. Translation: AAA31475.1.
PIRA33477.
A54269.
UniGeneOcu.1972.

3D structure databases

ProteinModelPortalP22758.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000002542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG80379.
HOGENOMHOG000231695.
HOVERGENHBG004342.
OrthoDBEOG4VX24R.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
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]
SUPFAMSSF81296. Ig_E-set. 1 hit.
SSF49309. Transglut_C. 2 hits.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTGM1_RABIT
AccessionPrimary (citable) accession number: P22758
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 103 of the entry and version 2 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

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