ID H2NN09_PONAB Unreviewed; 710 AA. AC H2NN09; A0A2J8S5B3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 2. DT 02-SEP-2026, entry version 74. DE RecName: Full=Protein-glutamine gamma-glutamyltransferase {ECO:0000256|ARBA:ARBA00024222, ECO:0000256|PROSITE-ProRule:PRU10024}; DE EC=2.3.2.13 {ECO:0000256|ARBA:ARBA00024222, ECO:0000256|PROSITE-ProRule:PRU10024}; GN Name=TGM7 {ECO:0000313|Ensembl:ENSPPYP00000007262.2}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000007262.2, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000007262.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000007262.2} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L- CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, CC ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU10024}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; H2NN09; -. DR Ensembl; ENSPPYT00000007563.2; ENSPPYP00000007262.2; ENSPPYG00000006409.2. DR eggNOG; ENOG502QTRA; Eukaryota. DR GeneTree; ENSGT01050000244866; -. DR HOGENOM; CLU_013435_1_0_1; -. DR OMA; TDHITFV; -. DR Proteomes; UP000001595; Chromosome 15. DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC. DR FunFam; 2.60.40.10:FF:000090; Protein-glutamine gamma-glutamyltransferase 2; 1. DR FunFam; 2.60.40.10:FF:000278; Protein-glutamine gamma-glutamyltransferase 2; 1. DR FunFam; 3.90.260.10:FF:000001; Protein-glutamine gamma-glutamyltransferase 2; 1. DR FunFam; 2.60.40.10:FF:001300; protein-glutamine gamma-glutamyltransferase Z; 1. 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; IPR050779; Transglutaminase. 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:SF41; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE Z; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR000459-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000459-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 271..364 FT /note="Transglutaminase-like" FT /evidence="ECO:0000259|SMART:SM00460" FT ACT_SITE 279 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1, FT ECO:0000256|PROSITE-ProRule:PRU10024" FT ACT_SITE 338 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 361 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT BINDING 401 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 403 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 450 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 455 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" SQ SEQUENCE 710 AA; 79767 MW; 457013EA0CA588D0 CRC64; MDQVATLQLE SVDLQSSRNN KEHHTQEMGV KRLTVRRGQP FYLQLSFSRP FQSQSDHITF VAETGPKPSE LLGTRATFFL TRVQPGNVWS TSDFTIDSNS LQVSLFTPAN AVIGHYTLKI EVPQGQGHSV TYPLGTFILL FNPWSPEDDV YLPSEILLQE YIMRDYGFVY KGHEKFITSW PWNYGQFEED IIDICFEILN KSLYYLKNPA KDCSQRNDVV YVCRVVSAMI NSNDDNGVLQ GNWGEDYSKG VSPLEWNGSV AILRQWSARG GQPVKYGQCW VFASVMCTVM RCLGIPTRVV SNFRSAHNVD RNLTIDTYYD RNAEMLSTQK RDKIWNFHVW NECWMIRKDL PPGYDGWQVL DPTPQQTSSG LFCCGPASVK AIREGDVHLA YDTPFVYAEV NADEVIWLLG DGQAQEILAH NTSSIGKEIS TKMVGSDQRH SITSSYKYPE GSPEERAVFM KASRKMLGPQ RASLPFLDLL ESGGLRDQPA QLQLHLAGIP EWGQDLQLLL RIQRVPDSTH PRGPIGLVVR FCAQALLHGG GTQKPLWRHT VRLNLDFGKE TQWPLLLPYS NYRNKLTDEK LIRVSGIAEV EETGRSMLVL KDISLEPPHL SIEVSERAEV GKALRVHVTL TNTLMLALSS CTMVLEGSGL VNGQVAKDLG TLVAGHTLQI RLDLYPTKAG PRQLQVLISS NEVKEIKGYK DIFVTVAGAP //