Reviewed, UniProtKB/Swiss-Prot Q9JLF6 (TGM1_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	815 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
Tissue specificity	Expressed in large amounts in epithelial tissues (lung, liver and kidney). Ref.1
Post-translational modification	Tyrosine-phosphorylated. Ref.1 Ref.3 Ref.4
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
Biological process	Keratinization
Cellular component	Membrane
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	keratinization Inferred from electronic annotation. Source: UniProtKB-KW organ morphogenesis Ref.1 Inferred from mutant phenotype. Source: MGI peptide cross-linking Inferred from electronic annotation. Source: InterPro
Cellular component	cell-cell adherens junction Ref.1 Inferred from direct assay. Source: MGI extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW calcium 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 815	815	Protein-glutamine gamma-glutamyltransferase K		PRO_0000213702
Sites
	Active site	376	1	By similarity
	Active site	435	1	By similarity
	Active site	458	1	By similarity
	Metal binding	498	1	Calcium By similarity
	Metal binding	500	1	Calcium By similarity
	Metal binding	547	1	Calcium By similarity
	Metal binding	552	1	Calcium By similarity
Amino acid modifications
	Modified residue	71	1	Phosphoserine Ref.3
	Modified residue	91	1	Phosphoserine Ref.3
	Modified residue	94	1	Phosphoserine Ref.3 Ref.4
Experimental info
	Sequence conflict	29	1	E → V in AAF35986. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9JLF6-1 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 326DD4E512AEA23E	FASTA	815	89,826
	10 20 30 40 50 60 MEGPRSDVGR WGRSPWQPPT TPSPEPEPEP EPDRRSRSRR GGGRSFWARC CGCCSCGNRG 70 80 90 100 110 120 DDDWGPEPSG SRSRGTSSRG RDSRGGRRPE SRGSGVNAAG DGTIREGMLV VTGVDLLCSR 130 140 150 160 170 180 SDQNRREHHT DEFEYDELIV RRGQPFHMIL FLNREYESSD RIALELLIGS NPEVGKGTHV 190 200 210 220 230 240 IIPVGKGGSG GWKAQVTKNN GHNLNLRVHT SPNAIIGKFQ FTVRTRSEAG EFQLPFDPRN 250 260 270 280 290 300 EIYILFNPWC PEDIVYVDHE DWRQEYVLNE SGRIYYGTEA QIGERTWNYG QFDHGVLDAC 310 320 330 340 350 360 LYILDRRGMP YGGRGDPVSV SRVVSAMVNS LDDNGVLIGN WTGDYSRGTN PSAWVGSVEI 370 380 390 400 410 420 LLSYLRTGYS VPYGQCWVFA GVTTTVLRCL GFATRTVTNF NSAHDTDTSL TMDIYFDENM 430 440 450 460 470 480 KPLEHLNHDS VWNFHVWNDC WMKRPDLPSG FDGWQVVDAT PQETSSGIFC CGPCSVESVK 490 500 510 520 530 540 NGLVYMKYDT PFIFAEVNSD KVYWQRQDDG SFKIVYVEEK AIGTLIVTKA IHSNNREDIT 550 560 570 580 590 600 HIYKHPEGSE AERRAVEKAA AHGSKPNVYA TRDSAEDVAM QVEAQDAVMG QDLAVSVVLT 610 620 630 640 650 660 NRGSSRRTVK LHLYLCVTYY TGVSGPTFKE AKKEVTLAPG ASDSVTMPVA YKEYKPHLVD 670 680 690 700 710 720 QGAMLLNVSG HVKESGQVLA KQHTFRLRTP DLSLTLLGAA VVGQECGVQI VFKNPLPVTL 730 740 750 760 770 780 TNVVFRLEGS GLQRPKVLNV GDIGGNETVT LRQTFVPVRP GPRQLIASLD SPQLSQVHGV 790 800 810 IQVDVAPASG GSGFSDAGGD SRSGENIPMA YRGGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells." Hiiragi T., Sasaki H., Nagafuchi A., Sabe H., Shen S.C., Matsuki M., Yamanishi K., Tsukita S. J. Biol. Chem. 274:34148-34154(1999) [PubMed: 10567386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, TISSUE SPECIFICITY.
[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]. Strain: FVB/N. Tissue: Kidney.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-91 AND SER-94, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF186373 mRNA. Translation: AAF35986.1. BC026422 mRNA. Translation: AAH26422.1.
IPI	IPI00331573.
RefSeq	NP_001155186.1. NP_001155187.1. NP_064368.3.
UniGene	Mm.41964
3D structure databases
SMR	Q9JLF6. Positions 105-786.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JLF6.
PTM databases
PhosphoSite	Q9JLF6.
Proteomic databases
PRIDE	Q9JLF6.
Genome annotation databases
Ensembl	ENSMUST00000002389; ENSMUSP00000002389; ENSMUSG00000022218; Mus musculus. [Genome view]
GeneID	21816.
KEGG	mmu:21816.
UCSC	uc007uag.1. mouse.
Organism-specific databases
CTD	21816.
MGI	MGI:98730. Tgm1.
Phylogenomic databases
eggNOG	roNOG07181.
HOGENOM	HBG444754.
HOVERGEN	Q9JLF6.
InParanoid	Q9JLF6.
OrthoDB	EOG9B017K.
Enzyme and pathway databases
BRENDA	2.3.2.13. 244.
Gene expression databases
ArrayExpress	Q9JLF6.
Bgee	Q9JLF6.
CleanEx	MM_TGM1.
Genevestigator	Q9JLF6.
GermOnline	ENSMUSG00000022218. Mus musculus.
Family and domain databases
InterPro	IPR008957. Fibronectin_typ-III-like_fold. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR002931. Transglutaminase-like. IPR008958. Transglutaminase_C. IPR013808. Transglutaminase_CS. IPR001102. Transglutaminase_N. [Graphical view]
Gene3D	G3DSA:2.60.40.30. FN_III-like. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF00927. Transglut_C. 2 hits. PF01841. Transglut_core. 1 hit. PF00868. Transglut_N. 1 hit. [Graphical view]
SMART	SM00460. TGc. 1 hit. [Graphical view]
PROSITE	PS00547. TRANSGLUTAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	301220.
SOURCE	Search...

Entry information

Entry name

TGM1_MOUSE

Accession

Primary (citable) accession number: Q9JLF6
Secondary accession number(s): Q8R0T9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	January 19, 2010
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)