TGM7_HUMAN
ID TGM7_HUMAN Reviewed; 710 AA.
AC Q96PF1;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase Z;
DE AltName: Full=Transglutaminase Z;
DE Short=TG(Z);
DE Short=TGZ;
DE Short=TGase Z;
DE EC=2.3.2.13;
DE AltName: Full=Transglutaminase-7;
DE Short=TGase-7;
GN Name=TGM7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11390390; DOI=10.1074/jbc.m102553200;
RA Grenard P., Bates M.K., Aeschlimann D.;
RT "Evolution of transglutaminase genes: identification of a transglutaminase
RT gene cluster on human chromosome 15q15. Structure of the gene encoding
RT transglutaminase X and a novel gene family member, transglutaminase Z.";
RL J. Biol. Chem. 276:33066-33078(2001).
CC -!- FUNCTION: Catalyzes the cross-linking of proteins and the conjugation
CC of polyamines to proteins.
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:0000255|PROSITE-
CC ProRule:PRU10024};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q96PF1; Q03989: ARID5A; NbExp=3; IntAct=EBI-12029034, EBI-948603;
CC Q96PF1; O43559: FRS3; NbExp=3; IntAct=EBI-12029034, EBI-725515;
CC Q96PF1; P55040: GEM; NbExp=3; IntAct=EBI-12029034, EBI-744104;
CC Q96PF1; P52597: HNRNPF; NbExp=3; IntAct=EBI-12029034, EBI-352986;
CC Q96PF1; P49639: HOXA1; NbExp=3; IntAct=EBI-12029034, EBI-740785;
CC Q96PF1; Q719H9: KCTD1; NbExp=3; IntAct=EBI-12029034, EBI-9027502;
CC Q96PF1; Q6A163: KRT39; NbExp=3; IntAct=EBI-12029034, EBI-11958242;
CC Q96PF1; Q9UHA4: LAMTOR3; NbExp=3; IntAct=EBI-12029034, EBI-1038192;
CC Q96PF1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-12029034, EBI-739832;
CC Q96PF1; Q96CD2: PPCDC; NbExp=3; IntAct=EBI-12029034, EBI-724333;
CC Q96PF1; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-12029034, EBI-12000762;
CC Q96PF1; O43741: PRKAB2; NbExp=3; IntAct=EBI-12029034, EBI-1053424;
CC Q96PF1; P47897: QARS1; NbExp=3; IntAct=EBI-12029034, EBI-347462;
CC Q96PF1; P20132: SDS; NbExp=3; IntAct=EBI-12029034, EBI-17859611;
CC Q96PF1; Q8TC71: SPATA18; NbExp=3; IntAct=EBI-12029034, EBI-11334239;
CC Q96PF1; O43609: SPRY1; NbExp=3; IntAct=EBI-12029034, EBI-3866665;
CC Q96PF1; P22105-1: TNXB; NbExp=3; IntAct=EBI-12029034, EBI-20753895;
CC Q96PF1; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-12029034, EBI-3918381;
CC Q96PF1; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-12029034, EBI-12817837;
CC Q96PF1; A0A1U9X8X8; NbExp=3; IntAct=EBI-12029034, EBI-17234977;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; AF363393; AAK97573.1; -; mRNA.
DR CCDS; CCDS32213.1; -.
DR RefSeq; NP_443187.1; NM_052955.2.
DR AlphaFoldDB; Q96PF1; -.
DR SMR; Q96PF1; -.
DR BioGRID; 125487; 34.
DR IntAct; Q96PF1; 20.
DR STRING; 9606.ENSP00000389466; -.
DR DrugBank; DB00130; L-Glutamine.
DR iPTMnet; Q96PF1; -.
DR PhosphoSitePlus; Q96PF1; -.
DR BioMuta; TGM7; -.
DR DMDM; 20532271; -.
DR MassIVE; Q96PF1; -.
DR PaxDb; Q96PF1; -.
DR PeptideAtlas; Q96PF1; -.
DR PRIDE; Q96PF1; -.
DR ProteomicsDB; 77686; -.
DR Antibodypedia; 23856; 137 antibodies from 29 providers.
DR DNASU; 116179; -.
DR Ensembl; ENST00000452443.3; ENSP00000389466.2; ENSG00000159495.8.
DR GeneID; 116179; -.
DR KEGG; hsa:116179; -.
DR MANE-Select; ENST00000452443.3; ENSP00000389466.2; NM_052955.3; NP_443187.1.
DR UCSC; uc001zrf.2; human.
DR CTD; 116179; -.
DR DisGeNET; 116179; -.
DR GeneCards; TGM7; -.
DR HGNC; HGNC:30790; TGM7.
DR HPA; ENSG00000159495; Tissue enhanced (lymphoid).
DR MIM; 606776; gene.
DR neXtProt; NX_Q96PF1; -.
DR OpenTargets; ENSG00000159495; -.
DR PharmGKB; PA134870048; -.
DR VEuPathDB; HostDB:ENSG00000159495; -.
DR eggNOG; ENOG502QTRA; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_1_0_1; -.
DR InParanoid; Q96PF1; -.
DR OMA; EVIWLFG; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; Q96PF1; -.
DR TreeFam; TF324278; -.
DR BRENDA; 2.3.2.13; 2681.
DR PathwayCommons; Q96PF1; -.
DR SignaLink; Q96PF1; -.
DR BioGRID-ORCS; 116179; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; TGM7; human.
DR GenomeRNAi; 116179; -.
DR Pharos; Q96PF1; Tdark.
DR PRO; PR:Q96PF1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96PF1; protein.
DR Bgee; ENSG00000159495; Expressed in secondary oocyte and 43 other tissues.
DR Genevisible; Q96PF1; HS.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
DR GO; GO:0018149; P:peptide cross-linking; IBA:GO_Central.
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; 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 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; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Calcium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..710
FT /note="Protein-glutamine gamma-glutamyltransferase Z"
FT /id="PRO_0000213716"
FT ACT_SITE 279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 710 AA; 79941 MW; 046C5ED002563909 CRC64;
MDQVATLRLE SVDLQSSRNN KEHHTQEMGV KRLTVRRGQP FYLRLSFSRP FQSQNDHITF
VAETGPKPSE LLGTRATFFL TRVQPGNVWS ASDFTIDSNS LQVSLFTPAN AVIGHYTLKI
EISQGQGHSV TYPLGTFILL FNPWSPEDDV YLPSEILLQE YIMRDYGFVY KGHERFITSW
PWNYGQFEED IIDICFEILN KSLYHLKNPA KDCSQRNDVV YVCRVVSAMI NSNDDNGVLQ
GNWGEDYSKG VSPLEWKGSV AILQQWSARG GQPVKYGQCW VFASVMCTVM RCLGVPTRVV
SNFRSAHNVD RNLTIDTYYD RNAEMLSTQK RDKIWNFHVW NECWMIRKDL PPGYNGWQVL
DPTPQQTSSG LFCCGPASVK AIREGDVHLA YDTPFVYAEV NADEVIWLLG DGQAQEILAH
NTSSIGKEIS TKMVGSDQRQ SITSSYKYPE GSPEERAVFM KASRKMLGPQ RASLPFLDLL
ESGGLRDQPA QLQLHLARIP EWGQDLQLLL RIQRVPDSTH PRGPIGLVVR FCAQALLHGG
GTQKPFWRHT VRMNLDFGKE TQWPLLLPYS NYRNKLTDEK LIRVSGIAEV EETGRSMLVL
KDICLEPPHL SIEVSERAEV GKALRVHVTL TNTLMVALSS CTMVLEGSGL INGQIAKDLG
TLVAGHTLQI QLDLYPTKAG PRQLQVLISS NEVKEIKGYK DIFVTVAGAP
