TGM3_MOUSE
ID TGM3_MOUSE Reviewed; 693 AA.
AC Q08189; A1L343; A2ANC3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase E;
DE EC=2.3.2.13 {ECO:0000250|UniProtKB:Q08188};
DE AltName: Full=Transglutaminase E;
DE Short=TG(E);
DE Short=TGE;
DE Short=TGase E;
DE AltName: Full=Transglutaminase-3;
DE Short=TGase-3;
DE Contains:
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain;
DE Contains:
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain;
DE Flags: Precursor;
GN Name=Tgm3; Synonyms=Tgase3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Epidermis;
RX PubMed=8099584; DOI=10.1016/s0021-9258(18)31442-x;
RA Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M.;
RT "The deduced sequence of the novel protransglutaminase E (TGase3) of human
RT and mouse.";
RL J. Biol. Chem. 268:12682-12690(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11331204; DOI=10.1016/s1357-2725(01)00033-4;
RA Hitomi K., Horio Y., Ikura K., Yamanishi K., Maki M.;
RT "Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse
RT tissues and cell lines.";
RL Int. J. Biochem. Cell Biol. 33:491-498(2001).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=15740639; DOI=10.1038/sj.cr.7290274;
RA Zhang J., Zhi H.Y., Ding F., Luo A.P., Liu Z.H.;
RT "Transglutaminase 3 expression in C57BL/6J mouse embryo epidermis and the
RT correlation with its differentiation.";
RL Cell Res. 15:105-110(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=20716179; DOI=10.1111/j.1742-4658.2010.07765.x;
RA Yamane A., Fukui M., Sugimura Y., Itoh M., Alea M.P., Thomas V.,
RA El Alaoui S., Akiyama M., Hitomi K.;
RT "Identification of a preferred substrate peptide for transglutaminase 3 and
RT detection of in situ activity in skin and hair follicles.";
RL FEBS J. 277:3564-3574(2010).
CC -!- FUNCTION: Catalyzes the calcium-dependent formation of isopeptide
CC cross-links between glutamine and lysine residues in various proteins,
CC as well as the conjugation of polyamines to proteins. Involved in the
CC formation of the cornified envelope (CE), a specialized component
CC consisting of covalent cross-links of proteins beneath the plasma
CC membrane of terminally differentiated keratinocytes. Catalyzes small
CC proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form
CC small interchain oligomers, which are further cross-linked by TGM1 onto
CC the growing CE scaffold (By similarity). In hair follicles, involved in
CC cross-linking structural proteins to hardening the inner root sheath.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:138370; EC=2.3.2.13;
CC Evidence={ECO:0000250|UniProtKB:Q08188, ECO:0000255|PROSITE-
CC ProRule:PRU10024};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 3 Ca(2+) cations per subunit. Binds 1 Ca(2+) as a zymogen,
CC and binds 2 more Ca(2+) cations, or other divalent metal cations, after
CC proteolytic processing. {ECO:0000250};
CC -!- SUBUNIT: Consists of two polypeptide chains, which are synthesized as a
CC precursor form of a single polypeptide.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08188}.
CC -!- TISSUE SPECIFICITY: Expressed in skin and stomach and, at lower levels,
CC in testis, kidney and spleen (at protein level). On the basis of its
CC catalytic activity, detected in the epidermis, around the granular and
CC spinous layers but not in the outermost cornified layers. In hair
CC follicles, mainly located in the medulla and the hair cortex.
CC {ECO:0000269|PubMed:11331204, ECO:0000269|PubMed:20716179}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 11.5 dpc in the early two-
CC layered epidermis. From 12.5 dpc, mainly expressed in the periderm
CC cells and weakly in the epidermal basal cells. After epidermis
CC keratinization, at 15.5 to 17.5 dpc, detected in the granular,
CC cornified layers and in the hair follicle. Also expressed in heart,
CC lung, bone, muscle, testis and blood vessels at 12.5, 13.5, 14.5 and
CC 16.5 dpc, respectively. {ECO:0000269|PubMed:15740639}.
CC -!- PTM: Activated by proteolytic processing. In vitro activation is
CC commonly achieved by cleavage with dispase, a neutral bacterial
CC protease. Physiological activation may be catalyzed by CTSL and, to a
CC lesser extent, by CTSS (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40421.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L10385; AAA40421.1; ALT_FRAME; mRNA.
DR EMBL; AL808127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28248.1; -; Genomic_DNA.
DR EMBL; BC129890; AAI29891.1; -; mRNA.
DR EMBL; BC129891; AAI29892.1; -; mRNA.
DR CCDS; CCDS38240.1; -.
DR PIR; B45991; B45991.
DR RefSeq; NP_033400.2; NM_009374.3.
DR AlphaFoldDB; Q08189; -.
DR SMR; Q08189; -.
DR BioGRID; 204169; 11.
DR IntAct; Q08189; 3.
DR STRING; 10090.ENSMUSP00000105928; -.
DR iPTMnet; Q08189; -.
DR PhosphoSitePlus; Q08189; -.
DR MaxQB; Q08189; -.
DR PaxDb; Q08189; -.
DR PeptideAtlas; Q08189; -.
DR PRIDE; Q08189; -.
DR ProteomicsDB; 263169; -.
DR DNASU; 21818; -.
DR Ensembl; ENSMUST00000110299; ENSMUSP00000105928; ENSMUSG00000027401.
DR GeneID; 21818; -.
DR KEGG; mmu:21818; -.
DR UCSC; uc008mig.2; mouse.
DR CTD; 7053; -.
DR MGI; MGI:98732; Tgm3.
DR VEuPathDB; HostDB:ENSMUSG00000027401; -.
DR eggNOG; ENOG502QUPB; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_1_0_1; -.
DR InParanoid; Q08189; -.
DR OMA; SMVGWNF; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; Q08189; -.
DR TreeFam; TF324278; -.
DR BioGRID-ORCS; 21818; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tgm3; mouse.
DR PRO; PR:Q08189; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q08189; protein.
DR Bgee; ENSMUSG00000027401; Expressed in esophagus and 46 other tissues.
DR Genevisible; Q08189; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0001533; C:cornified envelope; TAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; ISS:UniProtKB.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0043163; P:cell envelope organization; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; TAS:UniProtKB.
DR GO; GO:0035315; P:hair cell differentiation; TAS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0018149; P:peptide cross-linking; ISS:UniProtKB.
DR GO; GO:0043588; P:skin development; TAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR013808; Transglutaminase_AS.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Calcium; Cytoplasm; Keratinization; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Zymogen.
FT CHAIN 1..467
FT /note="Protein-glutamine gamma-glutamyltransferase E 50 kDa
FT catalytic chain"
FT /id="PRO_0000033654"
FT CHAIN 468..693
FT /note="Protein-glutamine gamma-glutamyltransferase E 27 kDa
FT non-catalytic chain"
FT /id="PRO_0000033655"
FT REGION 457..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT SITE 467..468
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250"
FT MOD_RES 111
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q08188"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08188"
FT CONFLICT 290
FT /note="P -> R (in Ref. 1; AAA40421)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="Q -> P (in Ref. 4; AAI29892/AAI29891)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="T -> S (in Ref. 1; AAA40421)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="R -> W (in Ref. 1; AAA40421)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="L -> I (in Ref. 1; AAA40421)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="R -> G (in Ref. 1; AAA40421)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="A -> T (in Ref. 1; AAA40421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 77309 MW; 834D86CD87AE0E9C CRC64;
MSALQIQNVN WQVPMNRRAH HTDKFSSQDS IVRRGQPWEI ILVCNRSLES GEDLNFIVST
GPQPSESART KAVFSISGRS TGGWNAALKA NSGNNLAIAI ASPVSAPIGL YTLSVEISSR
GRASSLKLGT FIMLFNPWLQ ADDVFMSNHA ERQEYVEEDS GIIYVGSTNR IGMVGWNFGQ
FEEDILNISL SILDRSLNFR RDPVTDVARR NDPKYVCRVL SAMINGNDDN GVISGNWSGN
YTGGVDPRTW NGSVEILKNW KKSGFRPVQF GQCWVFAGTL NTVLRCLGVP SRVITNFNSA
HDTDRNLSVD VYYDAMGNPL EKGSDSVWNF HVWNEGWFVR TDLGPTYNGW QVLDATPQER
SQGVFQCGPA SVNAIKAGDV DRNFDMIFIF AEVNADRITW IYNNRNNTQK QNSVDTHSIG
KYISTKAVGS NSRMDVTDKY KYPEGSSEER QVHQKALDKL KPNASFGATS SRNPEGEDKE
PSISGKFKVT GILAVGKEVS LSLMLKNMTN DRKTVTMNMT AWTIVYNGTL VHEVWKDSAT
ISLDPEEEIQ YPVKIAYSQY ERYLKADNMI RITAVCKVPD EAEVVVERDV ILDNPALTLE
VLEQAHVRKP VNVQMLFSNP LDQPVNNCVL LVEGSGLLRG SLKIDVPSLR PKEKSRIRFE
IFPTRSGTKQ LLADFSCNKF PAIKAMLPID VSE
