Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9GLK0 (TGM1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 80. 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
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 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
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length815 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 By similarity.

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 By similarity.

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 – 815815Protein-glutamine gamma-glutamyltransferase K
PRO_0000213700

Sites

Active site3751 By similarity
Active site4341 By similarity
Active site4571 By similarity
Metal binding4971Calcium By similarity
Metal binding4991Calcium By similarity
Metal binding5461Calcium By similarity
Metal binding5511Calcium By similarity

Amino acid modifications

Modified residue231Phosphoserine By similarity
Modified residue801Phosphoserine By similarity
Modified residue831Phosphoserine By similarity
Modified residue901Phosphoserine By similarity
Modified residue931Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9GLK0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 82C49D15DDD25BE4

FASTA81589,757
        10         20         30         40         50         60 
MDGPRSDVGR WGGNPWQPPT TPSPEPEPEP EPERRSRRGG RSFWARCCGC CSCRNRADDD 

        70         80         90        100        110        120 
WGPEPHRDRG SGSGRRRPDS RGSDSRRPGS RASGVNAAGD GTIREGMLVV TGVDLLSSRS 

       130        140        150        160        170        180 
DQNRREHHTD EFEYDELIIR RGQPFHMVLH FSRPYESSDR VALELLIGNN PEVGKGTHVI 

       190        200        210        220        230        240 
IPVGKGGSGG WKAQVTKASG QNLNLRVHTS PNAIIGKFQF TVRTHSEAGE FQLPFDPHNE 

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

       310        320        330        340        350        360 
YILDRRGMPY GGRGDPVSVS RVISAMVNSL DDNGVLIGNW SGDYSRGTNP SAWVGSVEIL 

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

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

       490        500        510        520        530        540 
GLVYMKYDTP FIFAEVNSDK VYWQRQDDGS FKIVYVEEKA IGTLIVTKAV GSNMQDDVTH 

       550        560        570        580        590        600 
IYKHPEGSEA ERKAVETAAA HGSKPNVYTN RDSAEDVALQ VEAQDAVMGQ DLTVSVVLTN 

       610        620        630        640        650        660 
RGSSTRTVKL HLYLSVTFYT GVTGPVFKES KKEVVLAPGA TERVSMPVAY KEYRPQIVDQ 

       670        680        690        700        710        720 
GSMLLNVSGH VKENGQVLAK QHTFRLRTPD LSLTLLGAAV VGQECEVQIV FKNPLPVTLT 

       730        740        750        760        770        780 
NVVFRLEGSG LQRPKILNVG DIGGNETVTL HQKFVPVRPG PRQLIASLDS PQLSQVHGVI 

       790        800        810 
QVDVAPAPGG GGFFSNAGGN SPLGETIPMA SRGGA

« Hide

References

[1]"DNA sequence and physical mapping of the canine transglutaminase 1 gene."
Credille K.M., Venta P.J., Breen M., Lowe J.K., Murphy K.E., Ostrander E.A., Galibert F., Dunstan R.W.
Cytogenet. Cell Genet. 93:73-76(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF262219 mRNA. Translation: AAG13662.1.
RefSeqNP_001003079.1. NM_001003079.1.
UniGeneCfa.3494.

3D structure databases

ProteinModelPortalQ9GLK0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403630.
KEGGcfa:403630.

Organism-specific databases

CTD7051.

Phylogenomic databases

eggNOGNOG80379.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidQ9GLK0.
KOK05619.
OrthoDBEOG4VX24R.

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

Other

NextBio20817135.

Entry information

Entry nameTGM1_CANFA
AccessionPrimary (citable) accession number: Q9GLK0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2001
Last modified: May 29, 2013
This is version 80 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents