ID A0A0D9REE4_CHLSB Unreviewed; 693 AA.
AC A0A0D9REE4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Transglutaminase 3 {ECO:0000313|Ensembl:ENSCSAP00000006983.1};
GN Name=TGM3 {ECO:0000313|Ensembl:ENSCSAP00000006983.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000006983.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000006983.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000006983.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AQIB01152732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9REE4; -.
DR STRING; 60711.ENSCSAP00000006983; -.
DR Ensembl; ENSCSAT00000008849.1; ENSCSAP00000006983.1; ENSCSAG00000010799.1.
DR eggNOG; ENOG502QUPB; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR OMA; SMVGWNF; -.
DR Proteomes; UP000029965; Chromosome 2.
DR Bgee; ENSCSAG00000010799; Expressed in pituitary gland and 1 other cell type or tissue.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
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 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT DOMAIN 265..357
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT ACT_SITE 273
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 331
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 354
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 693 AA; 76806 MW; 0D6839C17FC516BA CRC64;
LTALGLQSIN WQTAFNRQAH HTHKFSSREL ILRRGQNFQV LMLMNKGLGS NERLEFIVST
GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI SSPASAPIGQ YTMALQISSQ
GGVSSVKLGT FILLFNPWLN ADSVFMGNHA EREEYVQEDA GIIYVGSTNR ISMIGWNFGQ
FEEDILSICL SILDRSLNFR RDPATDVARR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT
YTGGRDPRNW NGSVEILKDW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFSSA
HDTDRNLSVD VYYDAMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW QVLDATPQER
SQGVFQCGPA SVIGIREGDV NLNFDMPFIF AEVNADRITW LYDGTTGRQM KNSVDTRTIG
RYISTKAVGS NARMDVTDKY KYPEGSDQER RVFQKALGKL KPNASFGATS SMGLEAEERE
SSIIGKFKVT GMLAVGKEVN LVLLLKNLSS DTKTVTVNMT AWTIVYNGTL VHEVWKDSAT
MSLDPEEEAE HPVKISYAQY EKYLKSDNMI RITAVCKVPD EPGVVVERDI ILDNPTLTLE
VLDEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLR PKERSRVRFE
ILPTRSGTKQ LLADFSCNKF HAIKAMLSID VVE
//
