GenomeNet

Database: UniProt/SWISS-PROT
Entry: TGM3_BOVIN
LinkDB: TGM3_BOVIN
Original site: 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   20-JUN-2018, entry version 59.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
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 and LOR
CC       cross-linking to form small interchain oligomers, which are
CC       further cross-linked by TGM1 onto the growing CE scaffold. In hair
CC       follicles, involved in cross-linking structural proteins to
CC       hardening the inner root sheath (By similarity). {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. {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,
CC       to a lesser extent, by CTSS (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
DR   EMBL; BC149161; AAI49162.1; -; mRNA.
DR   RefSeq; NP_001095318.1; NM_001101848.1.
DR   UniGene; Bt.13628; -.
DR   ProteinModelPortal; 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; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; A6QP57; -.
DR   KO; K05620; -.
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; Complete proteome; Cytoplasm;
KW   Keratinization; Metal-binding; Phosphoprotein; Reference proteome;
KW   Transferase; Zymogen.
FT   CHAIN         1    465       Protein-glutamine gamma-
FT                                glutamyltransferase E 50 kDa catalytic
FT                                chain.
FT                                /FTId=PRO_0000408949.
FT   CHAIN       466    691       Protein-glutamine gamma-
FT                                glutamyltransferase E 27 kDa non-
FT                                catalytic chain.
FT                                /FTId=PRO_0000408950.
FT   ACT_SITE    272    272       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    330    330       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    353    353       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       221    221       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       224    224       Calcium 1. {ECO:0000250}.
FT   METAL       226    226       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       227    227       Calcium 1. {ECO:0000250}.
FT   METAL       301    301       Calcium 2. {ECO:0000250}.
FT   METAL       303    303       Calcium 2. {ECO:0000250}.
FT   METAL       305    305       Calcium 2. {ECO:0000250}.
FT   METAL       307    307       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       324    324       Calcium 2. {ECO:0000250}.
FT   METAL       393    393       Calcium 3. {ECO:0000250}.
FT   METAL       414    414       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       442    442       Calcium 3. {ECO:0000250}.
FT   METAL       447    447       Calcium 3. {ECO:0000250}.
FT   SITE        465    466       Cleavage; by CTSL.
FT   MOD_RES     110    110       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q08188}.
FT   MOD_RES     111    111       Phosphothreonine.
FT                                {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
//
DBGET integrated database retrieval system