ID TGM3_BOVIN Reviewed; 691 AA. AC A6QP57; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 24-JAN-2024, entry version 73. 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; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Basal ganglia; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUL-2007) 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}. 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; BC149161; AAI49162.1; -; mRNA. DR RefSeq; NP_001095318.1; NM_001101848.1. DR AlphaFoldDB; A6QP57; -. DR SMR; A6QP57; -. DR STRING; 9913.ENSBTAP00000058423; -. DR PaxDb; 9913-ENSBTAP00000006432; -. DR PeptideAtlas; A6QP57; -. DR GeneID; 505080; -. DR KEGG; bta:505080; -. DR CTD; 7053; -. DR eggNOG; ENOG502QUPB; Eukaryota. DR InParanoid; A6QP57; -. DR OrthoDB; 5344745at2759; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISS:UniProtKB. DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW. DR GO; GO:0018149; P:peptide cross-linking; ISS:UniProtKB. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 3.90.260.10; Transglutaminase-like; 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 PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1. DR PANTHER; PTHR11590:SF36; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE E; 1. 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; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2. DR PROSITE; PS00547; TRANSGLUTAMINASES; 1. PE 2: Evidence at transcript level; KW Acyltransferase; Calcium; Cytoplasm; Keratinization; Metal-binding; KW Phosphoprotein; Reference proteome; Transferase; Zymogen. FT CHAIN 1..465 FT /note="Protein-glutamine gamma-glutamyltransferase E 50 kDa FT catalytic chain" FT /id="PRO_0000408949" FT CHAIN 466..691 FT /note="Protein-glutamine gamma-glutamyltransferase E 27 kDa FT non-catalytic chain" FT /id="PRO_0000408950" FT ACT_SITE 272 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024" FT ACT_SITE 330 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024" FT ACT_SITE 353 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 226 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 301 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 303 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 305 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 307 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 324 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 393 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 414 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 442 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 447 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250" FT SITE 465..466 FT /note="Cleavage; by CTSL" FT MOD_RES 110 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q08188" FT MOD_RES 111 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q08188" SQ SEQUENCE 691 AA; 76791 MW; 67DB0852E0973B4D CRC64; MSGLQSVDWQ IASNRQAHHT ERFYGKDLLV RRGQLFQVSL TLSQGLSSGG RVTFTASTGP YPSESANTKA VFPLSNGTSS SGWGAQLVSS RNNVLNISIL SPANAPIGRY TLNMQISSQG SDSTLKLGTF ILLFNPWLQA DSVFMSNHAE REEYVQEDAG IIFVGSTNRI SMIGWNYGQF EEGILNICLS VLDNSLNFRR DPATDVAHRN DPKYVGRVLS AMINGNDDSG VISGNWSGSY TGGRDPRNWN GSVEILKEWQ RSGFRPVRYG QCWVFAGTLN TVLRCLGIPS RVITNFNSAH DTDQNLSVDV YYDPLGRPMD KGSDSVWNFH VWNEAWFVRS DLGPSYNGWQ VLDATPQERS QGVFQCGPAS VIAIREGNVD WDFDMPFIFA EVNADRITWI YESNGALKKN SADTHSVGKH ISTKAVGSNS RMDVTEKYKY PEGSSQERQV FEKALRKLKP TMSFSATSAS SLAREEREPS ISGRFKVAGV LTVGKEVNLI LMLKNLTSDT KTVTVNMTAW TIVYNGTLVH EVWKDSVTKS LNPEEEIEHP VKIAYAQYEK YLKADNMIRT TAVCQVTDEP EVVVERDIIL DNPTLTLEVL DEARVQKPVN VQMLFSNPLD EPVKDCVLMV EGSGLLLGNL KIDVPALRPK ERSRVRFEIL PTRSGTKQLL ANFSCNKFPA IKAMLSVDVA E //