Reviewed, UniProtKB/Swiss-Prot P21981 (TGM2_MOUSE)

Names and origin

Protein names

Recommended name:
    Protein-glutamine gamma-glutamyltransferase 2
    EC=2.3.2.13
Alternative name(s):
    Tissue transglutaminase
    TGase C
      Short name=TGC
      Short name=TG(C)
    Transglutaminase-2

Gene names

Name:

Tgm2

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	686 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
Catalytic activity	Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Monomer.
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	branching involved in salivary gland morphogenesis Inferred from mutant phenotype. Source: MGI positive regulation of cell adhesion Inferred from mutant phenotype. Source: UniProtKB salivary gland cavitation Inferred from mutant phenotype. Source: MGI
Cellular component	cytosol Traceable author statement. Source: UniProtKB proteinaceous extracellular matrix Traceable author statement. Source: UniProtKB
Molecular function	GTP binding Ref.2 Non-traceable author statement. Source: UniProtKB acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Non-traceable author statement. Source: UniProtKB protein-glutamine gamma-glutamyltransferase activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 686	685	Protein-glutamine gamma-glutamyltransferase 2		PRO_0000213708
Sites
	Active site	277	1	By similarity
	Active site	335	1	By similarity
	Active site	358	1	By similarity
	Metal binding	398	1	Calcium By similarity
	Metal binding	400	1	Calcium By similarity
	Metal binding	447	1	Calcium By similarity
	Metal binding	452	1	Calcium By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8
	Modified residue	219	1	Phosphotyrosine By similarity
	Modified residue	369	1	Phosphotyrosine By similarity
	Modified residue	427	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	32 – 33	2	VL → LV in AAA40420. Ref.1
	Sequence conflict	51	1	E → Q in AAA40420. Ref.1
	Sequence conflict	51	1	E → Q in AAD37501. Ref.2
	Sequence conflict	186	1	E → Q in AAA40420. Ref.1
	Sequence conflict	226	1	A → D in AAA40420. Ref.1
	Sequence conflict	325	1	S → T in AAA40420. Ref.1
	Sequence conflict	357	1	I → L in AAA40420. Ref.1
	Sequence conflict	357	1	I → L in AAD37501. Ref.2
	Sequence conflict	396	1	E → K in BAC40899. Ref.4
	Sequence conflict	408 – 409	2	ED → DE in AAA40420. Ref.1
	Sequence conflict	415 – 416	2	SI → WM in AAA40420. Ref.1
	Sequence conflict	421	1	V → I in AAA40420. Ref.1
	Sequence conflict	481 – 485	5	DSMSM → QYEH in AAA40420. Ref.1
	Sequence conflict	539	1	N → K in BAE38690. Ref.4
	Sequence conflict	552	1	G → D in AAA40420. Ref.1
	Sequence conflict	583	1	L → V in AAA40420. Ref.1
	Sequence conflict	583	1	L → V in AAD37501. Ref.2
	Sequence conflict	654	1	F → S in AAA40420. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21981-1 [UniParc]. Last modified March 18, 2008. Version 4. Checksum: 9B64B074D3F837DE	FASTA	686	77,061
	10 20 30 40 50 60 MAEELLLERC DLEIQANGRD HHTADLCQEK LVLRRGQRFR LTLYFEGRGY EASVDSLTFG 70 80 90 100 110 120 AVTGPDPSEE AGTKARFSLS DNVEEGSWSA SVLDQQDNVL SLQLCTPANA PIGLYRLSLE 130 140 150 160 170 180 ASTGYQGSSF VLGHFILLYN AWCPADDVYL DSEEERREYV LTQQGFIYQG SVKFIKSVPW 190 200 210 220 230 240 NFGQFEDGIL DTCLMLLDMN PKFLKNRSRD CSRRSSPIYV GRVVSAMVNC NDDQGVLLGR 250 260 270 280 290 300 WDNNYGDGIS PMAWIGSVDI LRRWKEHGCQ QVKYGQCWVF AAVACTVLRC LGIPTRVVTN 310 320 330 340 350 360 YNSAHDQNSN LLIEYFRNEF GELESNKSEM IWNFHCWVES WMTRPDLQPG YEGWQAIDPT 370 380 390 400 410 420 PQEKSEGTYC CGPVSVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIRQEDG SVLKSINRSL 430 440 450 460 470 480 VVGQKISTKS VGRDDREDIT HTYKYPEGSP EEREVFTKAN HLNKLAEKEE TGVAMRIRVG 490 500 510 520 530 540 DSMSMGNDFD VFAHIGNDTS ETRECRLLLC ARTVSYNGVL GPECGTEDIN LTLDPYSENS 550 560 570 580 590 600 IPLRILYEKY SGCLTESNLI KVRGLLIEPA ANSYLLAERD LYLENPEIKI RVLGEPKQNR 610 620 630 640 650 660 KLVAEVSLKN PLSDPLYDCI FTVEGAGLTK EQKSVEVSDP VPAGDLVKAR VDLFPTDIGL 670 680 HKLVVNFQCD KLKSVKGYRN VIIGPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases." Gentile V., Saydak M., Chiocca E.A., Akande O., Birckbichler P.J., Lee K.N., Stein J.P., Davies P.J.A. J. Biol. Chem. 266:478-483(1991) [PubMed: 1670766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Macrophage.
[2]	"Organization and chromosomal mapping of mouse Gh/tissue transglutaminase gene (Tgm2)." Nanda N., Iismaa S.E., Copeland N.G., Gilbert D.J., Jenkins N., Graham R.M., Sutrave P. Arch. Biochem. Biophys. 366:151-156(1999) [PubMed: 10334875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/SvJ.
[3]	"Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2) gene: absence of mutations in MRLlpr/lpr mice." D'Amato M., Iannicola C., Monteriu G., Piacentini M. Cell Death Differ. 6:216-217(1999) [PubMed: 10200571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain cortex, Dendritic cell, Embryonic heart, Heart, Macrophage, Mammary gland and Spleen.
[5]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[6]	"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: NMRI. Tissue: Mammary tumor.
[7]	"Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter." Nagy L., Saydak M., Shipley N., Lu S., Basilion J.P., Yan Z.H., Syka P., Chandraratna R.A.S., Stein J.P., Heyman R.A., Davies P.J.A. J. Biol. Chem. 271:4355-4365(1996) [PubMed: 8626785] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3. Strain: Swiss.
[8]	Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-19; 41-74; 158-173; 215-222; 290-327; 550-561; 564-589; 601-609; 634-648 AND 651-671, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[9]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 378-387, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55154 mRNA. Translation: AAA40420.1. AF114266 mRNA. Translation: AAD37501.1. AF076928 mRNA. Translation: AAC62014.1. AK052912 mRNA. Translation: BAC35200.1. AK080224 mRNA. Translation: BAC37852.1. AK080593 mRNA. Translation: BAC37952.1. AK089481 mRNA. Translation: BAC40899.1. AK143712 mRNA. Translation: BAE25511.1. AK151776 mRNA. Translation: BAE30682.1. AK152152 mRNA. Translation: BAE30987.1. AK152627 mRNA. Translation: BAE31370.1. AK159255 mRNA. Translation: BAE34936.1. AK166302 mRNA. Translation: BAE38690.1. AK168990 mRNA. Translation: BAE40790.1. AK169356 mRNA. Translation: BAE41105.1. AL669824 Genomic DNA. Translation: CAM23188.1. BC016492 mRNA. Translation: AAH16492.1. U24148 Genomic DNA. No translation available.
IPI	IPI00126861.
PIR	B39045.
RefSeq	NP_033399.1.
UniGene	Mm.330731
3D structure databases
SMR	P21981. Positions 15-686.
ModBase	Search...
Protein-protein interaction databases
STRING	P21981.
PTM databases
PhosphoSite	P21981.
Proteomic databases
PRIDE	P21981.
Genome annotation databases
Ensembl	ENSMUST00000103122; ENSMUSP00000099411; ENSMUSG00000037820; Mus musculus. [Genome view]
GeneID	21817.
KEGG	mmu:21817.
Organism-specific databases
CTD	21817.
MGI	MGI:98731. Tgm2.
Phylogenomic databases
eggNOG	maNOG06398.
HOGENOM	HBG444754.
HOVERGEN	P21981.
InParanoid	P21981.
OMA	MAMRIRV.
OrthoDB	EOG9B017K.
PhylomeDB	P21981.
Enzyme and pathway databases
BRENDA	2.3.2.13. 244.
Gene expression databases
ArrayExpress	P21981.
Bgee	P21981.
CleanEx	MM_TGM2.
Genevestigator	P21981.
GermOnline	ENSMUSG00000037820. 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	301224.
SOURCE	Search...

Entry information

Entry name

TGM2_MOUSE

Accession

Primary (citable) accession number: P21981
Secondary accession number(s): O88901 , Q3TLV2, Q8C217, Q91VG9, Q9R1F7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	March 18, 2008
Last modified:	January 19, 2010
This is version 101 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)