ID   A0A8C0RTX1_CANLF        Unreviewed;       692 AA.
AC   A0A8C0RTX1;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   03-MAY-2023, entry version 6.
DE   SubName: Full=Transglutaminase 2 {ECO:0000313|Ensembl:ENSCAFP00030041657.1};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00030041657.1, ECO:0000313|Proteomes:UP000694429};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00030041657.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000459-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR   Ensembl; ENSCAFT00030047638.1; ENSCAFP00030041657.1; ENSCAFG00030025787.1.
DR   Proteomes; UP000694429; Chromosome 24.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
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:SF6; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 2; 1.
DR   Pfam; PF00927; Transglut_C; 1.
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   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2}.
FT   DOMAIN          269..361
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          663..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        335
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         398
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         400
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         447
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         452
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   692 AA;  77507 MW;  6FE51E9D3C51F151 CRC64;
     MAEDLVLEKC DLELEANGRD HHTAGLCQGR LVVRRGQPFW LTLHFTGRSY ESSVDSLTFS
     AVTGPDPSEE AGTKARFSLS SAVEEGAWTA VVMDQQDSVL SLQLSTPPNA PVGLYRLSLE
     ASTGYQGSSF VLGHFTLLFN SWCPADAVYL DSDEERREYV LSQQGFIYQG SVKFIKSIPW
     NFGQFEDGIL DICLMLLDRN PKFLKDACRD CSSRSNPIYV GRVVSAMVNC NDDQGVLLGR
     WDNNYKDGIS PMFWIGSVDI LRRWKTSGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
     FNSAHDQNSN LLIEYVYNKF GEIQKEKSEM IWNYHCWVES WMSRPDLQPG YEGWQALDPT
     PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA AFVFAEVNAD VVNWIQQDDG SLCKSTNNSQ
     TVGMKISTKS VGRDEREDIT HNYKYPEGSP EEREAFRKAN HLNKLTEKEE TGLAMRIRVS
     ESMSMGSDFD VFAYINNNTS ESHSCRLLLH ARTVSYNGIL GPECGTKDLL NLSLEPFSEK
     SIPLRILYEK YCECLTESNL IKVRGLLVEQ AANNYLLAER DIYLENPEIK IRILGEPKQN
     RKLVAEASLR NPLTVPLLGC SFTMEGAGLT EEQKVMDVPD PVEAGEGGQA AASWKHMYPR
     ARTGSAHTLS RPPHFSPPQA WADAQTHTPA RV
//