TGM3_BOVIN
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 03-AUG-2022, entry version 68.
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}.
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DR EMBL; BC149161; AAI49162.1; -; mRNA.
DR RefSeq; NP_001095318.1; NM_001101848.1.
DR AlphaFoldDB; A6QP57; -.
DR SMR; A6QP57; -.
DR STRING; 9913.ENSBTAP00000006432; -.
DR PaxDb; A6QP57; -.
DR PeptideAtlas; A6QP57; -.
DR PRIDE; A6QP57; -.
DR GeneID; 505080; -.
DR KEGG; bta:505080; -.
DR CTD; 7053; -.
DR eggNOG; ENOG502QUPB; Eukaryota.
DR InParanoid; A6QP57; -.
DR OrthoDB; 297055at2759; -.
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; -; 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 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
