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Database: UniProt/SWISS-PROT
Entry: TGM3_MOUSE
LinkDB: TGM3_MOUSE
Original site: 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   12-SEP-2018, entry version 144.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Epidermis;
RX   PubMed=8099584;
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
RT   human 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
RT   mouse 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
RT   the 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
RT   3 and 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
CC       proteins, as well as the conjugation of polyamines to proteins.
CC       Involved in the formation of the cornified envelope (CE), a
CC       specialized component consisting of covalent cross-links of
CC       proteins beneath the plasma membrane of terminally differentiated
CC       keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and
CC       SPRR2) and LOR cross-linking to form small interchain oligomers,
CC       which are further cross-linked by TGM1 onto the growing CE
CC       scaffold (By similarity). In hair follicles, involved in cross-
CC       linking structural proteins to hardening the inner root sheath.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
CC       protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
CC       {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
CC       zymogen, and binds 2 more Ca(2+) cations, or other divalent metal
CC       cations, after proteolytic processing. {ECO:0000250};
CC   -!- SUBUNIT: Consists of two polypeptide chains, which are synthesized
CC       as a 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
CC       levels, in testis, kidney and spleen (at protein level). On the
CC       basis of its catalytic activity, detected in the epidermis, around
CC       the granular and spinous layers but not in the outermost cornified
CC       layers. In hair follicles, mainly located in the medulla and the
CC       hair cortex. {ECO:0000269|PubMed:11331204,
CC       ECO:0000269|PubMed:20716179}.
CC   -!- DEVELOPMENTAL STAGE: Expression starts at 11.5 dpc in the early
CC       two-layered epidermis. From 12.5 dpc, mainly expressed in the
CC       periderm cells and weakly in the epidermal basal cells. After
CC       epidermis keratinization, at 15.5 to 17.5 dpc, detected in the
CC       granular, cornified layers and in the hair follicle. Also
CC       expressed in heart, lung, bone, muscle, testis and blood vessels
CC       at 12.5, 13.5, 14.5 and 16.5 dpc, respectively.
CC       {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,
CC       to a 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; Positions=637, 650; Evidence={ECO:0000305};
DR   EMBL; L10385; AAA40421.1; ALT_FRAME; mRNA.
DR   EMBL; AL808127; CAM19029.1; -; 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   UniGene; Mm.2961; -.
DR   ProteinModelPortal; Q08189; -.
DR   SMR; Q08189; -.
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   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   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00760000119108; -.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; Q08189; -.
DR   KO; K05620; -.
DR   OMA; KADNMIR; -.
DR   OrthoDB; EOG091G030K; -.
DR   PhylomeDB; Q08189; -.
DR   TreeFam; TF324278; -.
DR   ChiTaRS; Tgm3; mouse.
DR   PRO; PR:Q08189; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000027401; Expressed in 66 organ(s), highest expression level in esophagus.
DR   CleanEx; MM_TGM3; -.
DR   Genevisible; Q08189; MM.
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: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: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:0051262; P:protein tetramerization; 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; Complete proteome; Cytoplasm;
KW   Keratinization; Metal-binding; Phosphoprotein; Reference proteome;
KW   Transferase; Zymogen.
FT   CHAIN         1    467       Protein-glutamine gamma-
FT                                glutamyltransferase E 50 kDa catalytic
FT                                chain.
FT                                /FTId=PRO_0000033654.
FT   CHAIN       468    693       Protein-glutamine gamma-
FT                                glutamyltransferase E 27 kDa non-
FT                                catalytic chain.
FT                                /FTId=PRO_0000033655.
FT   ACT_SITE    273    273       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    331    331       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    354    354       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       222    222       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       225    225       Calcium 1. {ECO:0000250}.
FT   METAL       227    227       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       228    228       Calcium 1. {ECO:0000250}.
FT   METAL       230    230       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       302    302       Calcium 2. {ECO:0000250}.
FT   METAL       304    304       Calcium 2. {ECO:0000250}.
FT   METAL       306    306       Calcium 2. {ECO:0000250}.
FT   METAL       308    308       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       325    325       Calcium 2. {ECO:0000250}.
FT   METAL       394    394       Calcium 3. {ECO:0000250}.
FT   METAL       416    416       Calcium 3; via carbonyl oxygen.
FT   METAL       444    444       Calcium 3. {ECO:0000250}.
FT   METAL       449    449       Calcium 3. {ECO:0000250}.
FT   SITE        467    468       Cleavage; by CTSL. {ECO:0000250}.
FT   MOD_RES     111    111       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q08188}.
FT   MOD_RES     112    112       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q08188}.
FT   CONFLICT    290    290       P -> R (in Ref. 1; AAA40421).
FT                                {ECO:0000305}.
FT   CONFLICT    409    409       Q -> P (in Ref. 4; AAI29892/AAI29891).
FT                                {ECO:0000305}.
FT   CONFLICT    573    573       T -> S (in Ref. 1; AAA40421).
FT                                {ECO:0000305}.
FT   CONFLICT    588    588       R -> W (in Ref. 1; AAA40421).
FT                                {ECO:0000305}.
FT   CONFLICT    616    616       L -> I (in Ref. 1; AAA40421).
FT                                {ECO:0000305}.
FT   CONFLICT    639    639       R -> G (in Ref. 1; AAA40421).
FT                                {ECO:0000305}.
FT   CONFLICT    682    682       A -> T (in Ref. 1; AAA40421).
FT                                {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
//
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