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Protein-glutamine gamma-glutamyltransferase 2 (EC 2.3.2.13) (Tissue transglutaminase) (Transglutaminase C) (TG(C)) (TGC) (TGase C) (Transglutaminase-2) (TGase-2)

 TGM2_MOUSE              Reviewed;         686 AA.
P21981; O88901; Q3TLV2; Q8C217; Q91VG9; Q9R1F7;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 4.
12-SEP-2018, entry version 168.
RecName: Full=Protein-glutamine gamma-glutamyltransferase 2;
EC=2.3.2.13;
AltName: Full=Tissue transglutaminase;
AltName: Full=Transglutaminase C;
Short=TG(C);
Short=TGC;
Short=TGase C;
AltName: Full=Transglutaminase-2;
Short=TGase-2;
Name=Tgm2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
PubMed=1670766;
Gentile V., Saydak M., Chiocca E.A., Akande O., Birckbichler P.J.,
Lee K.N., Stein J.P., Davies P.J.A.;
"Isolation and characterization of cDNA clones to mouse macrophage and
human endothelial cell tissue transglutaminases.";
J. Biol. Chem. 266:478-483(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/SvJ;
PubMed=10334875; DOI=10.1006/abbi.1999.1189;
Nanda N., Iismaa S.E., Copeland N.G., Gilbert D.J., Jenkins N.,
Graham R.M., Sutrave P.;
"Organization and chromosomal mapping of mouse Gh/tissue
transglutaminase gene (Tgm2).";
Arch. Biochem. Biophys. 366:151-156(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10200571; DOI=10.1038/sj.cdd.4400494;
D'Amato M., Iannicola C., Monteriu G., Piacentini M.;
"Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2)
gene: absence of mutations in MRLlpr/lpr mice.";
Cell Death Differ. 6:216-217(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain cortex, Dendritic cell, Embryonic heart, Heart,
Macrophage, Mammary gland, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
STRAIN=SWR/J;
PubMed=8626785; DOI=10.1074/jbc.271.8.4355;
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.;
"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.";
J. Biol. Chem. 271:4355-4365(1996).
[8]
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, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryonic fibroblast;
Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
Submitted (FEB-2008) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 378-387, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-468, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Catalyzes the cross-linking of proteins and the
conjugation of polyamines to proteins.
-!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
{ECO:0000255|PROSITE-ProRule:PRU10024}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the transglutaminase superfamily.
Transglutaminase family. {ECO:0000305}.
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EMBL; M55154; AAA40420.1; -; mRNA.
EMBL; AF114266; AAD37501.1; -; mRNA.
EMBL; AF076928; AAC62014.1; -; mRNA.
EMBL; AK052912; BAC35200.1; -; mRNA.
EMBL; AK080224; BAC37852.1; -; mRNA.
EMBL; AK080593; BAC37952.1; -; mRNA.
EMBL; AK089481; BAC40899.1; -; mRNA.
EMBL; AK143712; BAE25511.1; -; mRNA.
EMBL; AK151776; BAE30682.1; -; mRNA.
EMBL; AK152152; BAE30987.1; -; mRNA.
EMBL; AK152627; BAE31370.1; -; mRNA.
EMBL; AK159255; BAE34936.1; -; mRNA.
EMBL; AK166302; BAE38690.1; -; mRNA.
EMBL; AK168990; BAE40790.1; -; mRNA.
EMBL; AK169356; BAE41105.1; -; mRNA.
EMBL; AL669824; CAM23188.1; -; Genomic_DNA.
EMBL; BC016492; AAH16492.1; -; mRNA.
EMBL; U24148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS16985.1; -.
PIR; B39045; B39045.
RefSeq; NP_033399.1; NM_009373.3.
UniGene; Mm.330731; -.
ProteinModelPortal; P21981; -.
SMR; P21981; -.
BioGrid; 204168; 2.
IntAct; P21981; 4.
MINT; P21981; -.
STRING; 10090.ENSMUSP00000099411; -.
BindingDB; P21981; -.
ChEMBL; CHEMBL2079853; -.
iPTMnet; P21981; -.
PhosphoSitePlus; P21981; -.
SwissPalm; P21981; -.
EPD; P21981; -.
MaxQB; P21981; -.
PaxDb; P21981; -.
PeptideAtlas; P21981; -.
PRIDE; P21981; -.
Ensembl; ENSMUST00000103122; ENSMUSP00000099411; ENSMUSG00000037820.
GeneID; 21817; -.
KEGG; mmu:21817; -.
UCSC; uc008npr.1; mouse.
CTD; 7052; -.
MGI; MGI:98731; Tgm2.
eggNOG; ENOG410IFMV; Eukaryota.
eggNOG; ENOG410XQEZ; LUCA.
GeneTree; ENSGT00760000119108; -.
HOGENOM; HOG000231695; -.
HOVERGEN; HBG004342; -.
InParanoid; P21981; -.
KO; K05625; -.
OMA; AHITNNT; -.
OrthoDB; EOG091G030K; -.
PhylomeDB; P21981; -.
TreeFam; TF324278; -.
PRO; PR:P21981; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000037820; Expressed in 304 organ(s), highest expression level in cornea.
CleanEx; MM_TGM2; -.
ExpressionAtlas; P21981; baseline and differential.
Genevisible; P21981; MM.
GO; GO:0005737; C:cytoplasm; ISA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
GO; GO:0016020; C:membrane; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IMP:UniProtKB.
GO; GO:0008483; F:transaminase activity; ISO:MGI.
GO; GO:0043277; P:apoptotic cell clearance; ISO:MGI.
GO; GO:0001974; P:blood vessel remodeling; ISO:MGI.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:UniProtKB.
GO; GO:0018153; P:isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine; ISO:MGI.
GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IMP:UniProtKB.
GO; GO:0018149; P:peptide cross-linking; TAS:UniProtKB.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; ISA:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IMP:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0060662; P:salivary gland cavitation; IMP:MGI.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.90.260.10; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR002931; Transglutaminase-like.
InterPro; IPR036985; Transglutaminase-like_sf.
InterPro; IPR023608; Transglutaminase_animal.
InterPro; IPR013808; Transglutaminase_AS.
InterPro; IPR008958; Transglutaminase_C.
InterPro; IPR036238; Transglutaminase_C_sf.
InterPro; IPR001102; Transglutaminase_N.
Pfam; PF00927; Transglut_C; 2.
Pfam; PF01841; Transglut_core; 1.
Pfam; PF00868; Transglut_N; 1.
PIRSF; PIRSF000459; TGM_EBP42; 1.
SMART; SM00460; TGc; 1.
SUPFAM; SSF49309; SSF49309; 2.
SUPFAM; SSF54001; SSF54001; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS00547; TRANSGLUTAMINASES; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Calcium; Complete proteome;
Direct protein sequencing; Metal-binding; Reference proteome;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8}.
CHAIN 2 686 Protein-glutamine gamma-
glutamyltransferase 2.
/FTId=PRO_0000213708.
ACT_SITE 277 277 {ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 335 335 {ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 358 358 {ECO:0000255|PROSITE-ProRule:PRU10024}.
METAL 398 398 Calcium. {ECO:0000250}.
METAL 400 400 Calcium. {ECO:0000250}.
METAL 447 447 Calcium. {ECO:0000250}.
METAL 452 452 Calcium. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.8}.
MOD_RES 468 468 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CONFLICT 32 33 VL -> LV (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 51 51 E -> Q (in Ref. 1; AAA40420 and 2;
AAD37501). {ECO:0000305}.
CONFLICT 186 186 E -> Q (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 226 226 A -> D (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 325 325 S -> T (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 357 357 I -> L (in Ref. 1; AAA40420 and 2;
AAD37501). {ECO:0000305}.
CONFLICT 396 396 E -> K (in Ref. 4; BAC40899).
{ECO:0000305}.
CONFLICT 408 409 ED -> DE (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 415 416 SI -> WM (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 421 421 V -> I (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 481 485 DSMSM -> QYEH (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 539 539 N -> K (in Ref. 4; BAE38690).
{ECO:0000305}.
CONFLICT 552 552 G -> D (in Ref. 1; AAA40420).
{ECO:0000305}.
CONFLICT 583 583 L -> V (in Ref. 1; AAA40420 and 2;
AAD37501). {ECO:0000305}.
CONFLICT 654 654 F -> S (in Ref. 1; AAA40420).
{ECO:0000305}.
SEQUENCE 686 AA; 77061 MW; 9B64B074D3F837DE CRC64;
MAEELLLERC DLEIQANGRD HHTADLCQEK LVLRRGQRFR LTLYFEGRGY EASVDSLTFG
AVTGPDPSEE AGTKARFSLS DNVEEGSWSA SVLDQQDNVL SLQLCTPANA PIGLYRLSLE
ASTGYQGSSF VLGHFILLYN AWCPADDVYL DSEEERREYV LTQQGFIYQG SVKFIKSVPW
NFGQFEDGIL DTCLMLLDMN PKFLKNRSRD CSRRSSPIYV GRVVSAMVNC NDDQGVLLGR
WDNNYGDGIS PMAWIGSVDI LRRWKEHGCQ QVKYGQCWVF AAVACTVLRC LGIPTRVVTN
YNSAHDQNSN LLIEYFRNEF GELESNKSEM IWNFHCWVES WMTRPDLQPG YEGWQAIDPT
PQEKSEGTYC CGPVSVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIRQEDG SVLKSINRSL
VVGQKISTKS VGRDDREDIT HTYKYPEGSP EEREVFTKAN HLNKLAEKEE TGVAMRIRVG
DSMSMGNDFD VFAHIGNDTS ETRECRLLLC ARTVSYNGVL GPECGTEDIN LTLDPYSENS
IPLRILYEKY SGCLTESNLI KVRGLLIEPA ANSYLLAERD LYLENPEIKI RVLGEPKQNR
KLVAEVSLKN PLSDPLYDCI FTVEGAGLTK EQKSVEVSDP VPAGDLVKAR VDLFPTDIGL
HKLVVNFQCD KLKSVKGYRN VIIGPA


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EIAAB42185 Homo sapiens,Human,Protein-glutamine gamma-glutamyltransferase 5,TG(X),TGase X,TGase-5,TGM5,TGMX,TGX,Transglutaminase X,Transglutaminase-5
EIAAB42179 Bos taurus,Bovine,Protein-glutamine gamma-glutamyltransferase E,TG(E),TGase E,TGase-3,TGE,TGM3,Transglutaminase E,Transglutaminase-3
EIAAB42170 Canis familiaris,Canis lupus familiaris,Dog,Epidermal TGase,Protein-glutamine gamma-glutamyltransferase K,TG(K),TGase K,TGase-1,TGK,TGM1,Transglutaminase K,Transglutaminase-1
20-783-73427 MOUSE ANTI HUMAN KERATINOCYTE TRANSGLUTAMINASE - EC 2.3.2.13; Transglutaminase K; TGase K; TGK; TG(K); Transglutaminase-1; Epidermal TGase Monoclonal 0.5 ml
EIAAB42181 Dorsal prostate transglutaminase,Dorsal protein 1,DP1,Dp1,Protein-glutamine gamma-glutamyltransferase 4,Rat,Rattus norvegicus,TGase-4,Tgm4,Transglutaminase-4


 

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