TGM3_RAT
ID TGM3_RAT Reviewed; 693 AA.
AC D4A5U3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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.
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 and LOR cross-linking to form small interchain
CC oligomers, which are further cross-linked by TGM1 onto the growing CE
CC scaffold. In hair follicles, involved in cross-linking structural
CC proteins to hardening the inner root sheath (By similarity).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08188}.
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}.
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DR EMBL; CH473949; EDL80172.1; -; Genomic_DNA.
DR RefSeq; NP_001102429.1; NM_001108959.1.
DR AlphaFoldDB; D4A5U3; -.
DR SMR; D4A5U3; -.
DR BioGRID; 265783; 1.
DR STRING; 10116.ENSRNOP00000059160; -.
DR iPTMnet; D4A5U3; -.
DR PhosphoSitePlus; D4A5U3; -.
DR PaxDb; D4A5U3; -.
DR PRIDE; D4A5U3; -.
DR Ensembl; ENSRNOT00000063828; ENSRNOP00000059160; ENSRNOG00000006753.
DR GeneID; 366189; -.
DR KEGG; rno:366189; -.
DR UCSC; RGD:1561831; rat.
DR CTD; 7053; -.
DR RGD; 1561831; Tgm3.
DR eggNOG; ENOG502QUPB; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_1_0_1; -.
DR InParanoid; D4A5U3; -.
DR OMA; VDQNFDM; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; D4A5U3; -.
DR TreeFam; TF324278; -.
DR PRO; PR:D4A5U3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000006753; Expressed in esophagus and 12 other tissues.
DR Genevisible; D4A5U3; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; ISO:RGD.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; ISO:RGD.
DR GO; GO:0043163; P:cell envelope organization; ISO:RGD.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0018149; P:peptide cross-linking; ISS: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 3: Inferred from homology;
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_0000408951"
FT CHAIN 468..693
FT /note="Protein-glutamine gamma-glutamyltransferase E 27 kDa
FT non-catalytic chain"
FT /id="PRO_0000408952"
FT REGION 455..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..477
FT /note="Polar residues"
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 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 /evidence="ECO:0000250"
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"
SQ SEQUENCE 693 AA; 77230 MW; CFE4D1B46960D4C2 CRC64;
MSALEVQNIN WQMPMNRRAH HTDKFSSQDF IVRRGQPWEV ILLCNRSLES GDNLNFIVST
GPQPSESART KAVFSISGRN TSGWSAALKA SNGNNLFIAI ASPVSAPIGL YTLNVEVSSK
GRVSSVKLGT FTVLFNPWQQ GDDVFMSNHA ERQEYVEEDS GIIYVGSTNR IGMVGWNFGQ
FEEDILSISL SILDRSLNFR RDPATDVARR NDPKYVCRVL SAMINANDDS GVLSGNWSGN
YSGGVDPRTW NGSVEILKNW KKSGFRPVQF GQCWVFAGTL NTVLRCLGVP SRVITNFNSA
HDTDRNLSVD VYYDAMGNPL EKGSDSVWNF HVWNEGWFVR TDLGPSYNGW QVLDATPQER
SQGVFQCGPA SVNAIKDGEV DQNFDMIFIF AEVNADRITW IYNNRDGSQK QNSVDTYSIG
KYISTKAVGS NSRMDVTIKY KHPEGSKEER QVQQKAMNKL KPNASFGATS SRGPQGEEKE
PSISGKFKVT GVLAVGKEVS LALILKNTTS DRKTVTTNMT AWTIVYNGTL VHEVWKDSAT
ISLDPEEEIQ YPVKIAYSQY DRYLKADNMI RITAVCKVPD EAEVVVERDV ILDNPTLTLE
VLDQAQLRKP VVVQMLFSNP LDEPVKNCVL MVEGSGLLRG SLKIDVPALR PKEKSRVRFE
IFPTRIGIKQ LLADFSCNKF PAIKAMLVIE VSE
