ID   H2QJU1_PANTR            Unreviewed;       693 AA.
AC   H2QJU1; A0A2J8MS45;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Transglutaminase 3 {ECO:0000313|Ensembl:ENSPTRP00000022553.3};
GN   Name=TGM3 {ECO:0000313|Ensembl:ENSPTRP00000022553.3,
GN   ECO:0000313|VGNC:VGNC:6281};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000022553.3, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000022553.3, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000022553.3}
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; AACZ04065006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2QJU1; -.
DR   STRING; 9598.ENSPTRP00000022553; -.
DR   PaxDb; 9598-ENSPTRP00000022553; -.
DR   Ensembl; ENSPTRT00000024449.4; ENSPTRP00000022553.3; ENSPTRG00000013174.4.
DR   VGNC; VGNC:6281; TGM3.
DR   eggNOG; ENOG502QUPB; Eukaryota.
DR   GeneTree; ENSGT01050000244866; -.
DR   HOGENOM; CLU_013435_1_0_1; -.
DR   InParanoid; H2QJU1; -.
DR   OMA; SMVGWNF; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000002277; Chromosome 20.
DR   Bgee; ENSPTRG00000013174; Expressed in testis and 13 other cell types or tissues.
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; IBA:GO_Central.
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:UP000002277}.
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;  76730 MW;  3C787B2CB7D93611 CRC64;
     MAALGVQSIN WQTAFNRQAH HTDRFSSQEL ILRRGQNFQV LMIMNKGLGS NERLEFIVST
     GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI SSPASAPIGR YTMALQIFSQ
     GGISSVKLGT FILLFNPWLN VDSVFMGNHA EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ
     FEEDILSICL SILDRSLNFR RDAAADVARR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT
     YTGGRDPRNW NGSVEILKTW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA
     HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW QVLDATPQER
     SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW LYNNTTGKQW KNSVNSHTIG
     RYISTKAVGS NARMDVTDKY KYPEGSDQER QVFQKALGKL KPNASFGATS SMGLETEEQE
     PSIIGKLKVA GMLAVGKEVS LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT
     MSLDPEEEAE HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDV ILDNPTLTLE
     VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG PKERSRVRFD
     ILPTRSGTKQ LLADFSCNKF PAIKAMLSID VAE
//