GenomeNet

Database: UniProt/SWISS-PROT
Entry: TGM3_RAT
LinkDB: TGM3_RAT
Original site: 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   22-NOV-2017, entry version 55.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
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; CH473949; EDL80172.1; -; Genomic_DNA.
DR   RefSeq; NP_001102429.1; NM_001108959.1.
DR   UniGene; Rn.53317; -.
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; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00760000119108; -.
DR   InParanoid; D4A5U3; -.
DR   KO; K05620; -.
DR   OMA; KADNMIR; -.
DR   OrthoDB; EOG091G030K; -.
DR   PhylomeDB; D4A5U3; -.
DR   TreeFam; TF324278; -.
DR   PRO; PR:D4A5U3; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000006753; -.
DR   Genevisible; D4A5U3; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; 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: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   GO; GO:0051262; P:protein tetramerization; ISO:RGD.
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; 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; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   3: Inferred from homology;
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_0000408951.
FT   CHAIN       468    693       Protein-glutamine gamma-
FT                                glutamyltransferase E 27 kDa non-
FT                                catalytic chain.
FT                                /FTId=PRO_0000408952.
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       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                                {ECO:0000250}.
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}.
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
//
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