TGM4_HUMAN
ID TGM4_HUMAN Reviewed; 684 AA.
AC P49221; Q16707; Q96QN4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 4;
DE EC=2.3.2.13;
DE AltName: Full=Fibrinoligase;
DE AltName: Full=Prostate transglutaminase;
DE AltName: Full=Prostate-specific transglutaminase;
DE AltName: Full=Transglutaminase P;
DE Short=TG(P);
DE Short=TGP;
DE Short=TGase P;
DE AltName: Full=Transglutaminase-4;
DE Short=TGase-4;
GN Name=TGM4;
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].
RC TISSUE=Prostate;
RX PubMed=7916568; DOI=10.1006/bbrc.1994.2298;
RA Grant F.J., Taylor D.A., Sheppard P.O., Mathewes S.L., Lint W., Vanaja E.,
RA Bishop P.D., O'Hara P.J.;
RT "Molecular cloning and characterization of a novel transglutaminase cDNA
RT from a human prostate cDNA library.";
RL Biochem. Biophys. Res. Commun. 203:1117-1123(1994).
RN [2]
RP SEQUENCE REVISION.
RA Grant F.J.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANT LYS-313.
RC TISSUE=Prostate;
RX PubMed=8645175; DOI=10.1042/bj3150901;
RA Dubbink H.J., Verkaik N.S., Faber P.W., Trapman J., Schroeder F.H.,
RA Romijn J.C.;
RT "Tissue specific and androgen-regulated expression of human prostate-
RT specific transglutaminase.";
RL Biochem. J. 315:901-908(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Associated with the mammalian reproductive process. Catalyzes
CC the cross-linking of proteins and the conjugation of polyamines to
CC specific proteins in the seminal tract.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Prostate.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; L34840; AAB95430.1; -; mRNA.
DR EMBL; U31905; AAC50516.1; -; mRNA.
DR EMBL; BC007003; AAH07003.1; -; mRNA.
DR CCDS; CCDS2723.1; -.
DR PIR; S71105; S71105.
DR RefSeq; NP_003232.2; NM_003241.3.
DR AlphaFoldDB; P49221; -.
DR SMR; P49221; -.
DR BioGRID; 112905; 9.
DR IntAct; P49221; 4.
DR STRING; 9606.ENSP00000296125; -.
DR DrugBank; DB00130; L-Glutamine.
DR iPTMnet; P49221; -.
DR PhosphoSitePlus; P49221; -.
DR BioMuta; TGM4; -.
DR DMDM; 3915892; -.
DR jPOST; P49221; -.
DR MassIVE; P49221; -.
DR MaxQB; P49221; -.
DR PaxDb; P49221; -.
DR PeptideAtlas; P49221; -.
DR PRIDE; P49221; -.
DR ProteomicsDB; 55971; -.
DR Antibodypedia; 29511; 321 antibodies from 33 providers.
DR DNASU; 7047; -.
DR Ensembl; ENST00000296125.9; ENSP00000296125.4; ENSG00000163810.12.
DR Ensembl; ENST00000628744.3; ENSP00000487307.1; ENSG00000281886.3.
DR GeneID; 7047; -.
DR KEGG; hsa:7047; -.
DR MANE-Select; ENST00000296125.9; ENSP00000296125.4; NM_003241.4; NP_003232.2.
DR UCSC; uc003coc.5; human.
DR CTD; 7047; -.
DR DisGeNET; 7047; -.
DR GeneCards; TGM4; -.
DR HGNC; HGNC:11780; TGM4.
DR HPA; ENSG00000163810; Tissue enriched (prostate).
DR MIM; 600585; gene.
DR neXtProt; NX_P49221; -.
DR OpenTargets; ENSG00000163810; -.
DR PharmGKB; PA36493; -.
DR VEuPathDB; HostDB:ENSG00000163810; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR InParanoid; P49221; -.
DR OMA; DHHNWQA; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; P49221; -.
DR TreeFam; TF324278; -.
DR BRENDA; 2.3.2.13; 2681.
DR PathwayCommons; P49221; -.
DR SignaLink; P49221; -.
DR BioGRID-ORCS; 7047; 8 hits in 1062 CRISPR screens.
DR ChiTaRS; TGM4; human.
DR GeneWiki; TGM4; -.
DR GenomeRNAi; 7047; -.
DR Pharos; P49221; Tbio.
DR PRO; PR:P49221; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P49221; protein.
DR Bgee; ENSG00000163810; Expressed in prostate gland and 72 other tissues.
DR ExpressionAtlas; P49221; baseline and differential.
DR Genevisible; P49221; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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..684
FT /note="Protein-glutamine gamma-glutamyltransferase 4"
FT /id="PRO_0000213711"
FT ACT_SITE 268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT VARIANT 100
FT /note="E -> D (in dbSNP:rs2271087)"
FT /id="VAR_052555"
FT VARIANT 244
FT /note="Y -> H (in dbSNP:rs9818345)"
FT /id="VAR_052556"
FT VARIANT 249
FT /note="S -> T (in dbSNP:rs937838)"
FT /id="VAR_052557"
FT VARIANT 313
FT /note="E -> K (in dbSNP:rs1995641)"
FT /evidence="ECO:0000269|PubMed:8645175"
FT /id="VAR_052558"
FT VARIANT 372
FT /note="R -> C (in dbSNP:rs3749195)"
FT /id="VAR_052559"
FT VARIANT 372
FT /note="R -> H (in dbSNP:rs13326552)"
FT /id="VAR_052560"
FT VARIANT 376
FT /note="I -> V (in dbSNP:rs17077022)"
FT /id="VAR_052561"
FT VARIANT 409
FT /note="V -> I (in dbSNP:rs9876921)"
FT /id="VAR_052562"
FT VARIANT 437
FT /note="E -> Q (in dbSNP:rs1395388)"
FT /id="VAR_052563"
FT CONFLICT 353
FT /note="P -> S (in Ref. 4; AAH07003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 77145 MW; 64A3E754EA46BFEC CRC64;
MMDASKELQV LHIDFLNQDN AVSHHTWEFQ TSSPVFRRGQ VFHLRLVLNQ PLQSYHQLKL
EFSTGPNPSI AKHTLVVLDP RTPSDHYNWQ ATLQNESGKE VTVAVTSSPN AILGKYQLNV
KTGNHILKSE ENILYLLFNP WCKEDMVFMP DEDERKEYIL NDTGCHYVGA ARSIKCKPWN
FGQFEKNVLD CCISLLTESS LKPTDRRDPV LVCRAMCAMM SFEKGQGVLI GNWTGDYEGG
TAPYKWTGSA PILQQYYNTK QAVCFGQCWV FAGILTTVLR ALGIPARSVT GFDSAHDTER
NLTVDTYVNE NGEKITSMTH DSVWNFHVWT DAWMKRPDLP KGYDGWQAVD ATPQERSQGV
FCCGPSPLTA IRKGDIFIVY DTRFVFSEVN GDRLIWLVKM VNGQEELHVI SMETTSIGKN
ISTKAVGQDR RRDITYEYKY PEGSSEERQV MDHAFLLLSS EREHRRPVKE NFLHMSVQSD
DVLLGNSVNF TVILKRKTAA LQNVNILGSF ELQLYTGKKM AKLCDLNKTS QIQGQVSEVT
LTLDSKTYIN SLAILDDEPV IRGFIIAEIV ESKEIMASEV FTSFQYPEFS IELPNTGRIG
QLLVCNCIFK NTLAIPLTDV KFSLESLGIS SLQTSDHGTV QPGETIQSQI KCTPIKTGPK
KFIVKLSSKQ VKEINAQKIV LITK
