TGM3_HUMAN
ID TGM3_HUMAN Reviewed; 693 AA.
AC Q08188; A8K5N6; B2RCR6; D3DVX1; O95933; Q32ML9; Q32MM0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase E;
DE EC=2.3.2.13 {ECO:0000269|PubMed:11980702, ECO:0000269|PubMed:12679341, ECO:0000269|PubMed:27866708};
DE AltName: Full=Transglutaminase E;
DE Short=TG(E);
DE Short=TGE;
DE Short=TGase E;
DE AltName: Full=Transglutaminase-3;
DE Short=TGase-3;
DE Contains:
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain;
DE Contains:
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain;
DE Flags: Precursor;
GN Name=TGM3;
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], AND VARIANTS LYS-13; ARG-562 AND ARG-654.
RC TISSUE=Foreskin;
RX PubMed=8099584; DOI=10.1016/s0021-9258(18)31442-x;
RA Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M.;
RT "The deduced sequence of the novel protransglutaminase E (TGase3) of human
RT and mouse.";
RL J. Biol. Chem. 268:12682-12690(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-13 AND ARG-654.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-13; LEU-163; ASN-249;
RP ARG-654 AND MET-687.
RG NIEHS SNPs program;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-13 AND
RP ARG-654.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-13 AND ARG-654.
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).
RN [7]
RP PROTEIN SEQUENCE OF 2-13 AND 670-684, VARIANT LYS-13, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Bensaad K., Vousden K.H.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 468-479, AND PROTEOLYTIC CLEAVAGE BY CTSL.
RX PubMed=16565075; DOI=10.1074/jbc.m600694200;
RA Cheng T., Hitomi K., van Vlijmen-Willems I.M., de Jongh G.J., Yamamoto K.,
RA Nishi K., Watts C., Reinheckel T., Schalkwijk J., Zeeuwen P.L.;
RT "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L
RT by a reactive site that is distinct from the legumain-binding site. A novel
RT clue for the role of cystatin M/E in epidermal cornification.";
RL J. Biol. Chem. 281:15893-15899(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-111 AND THR-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INVOLVEMENT IN UHS2, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=27866708; DOI=10.1016/j.ajhg.2016.10.004;
RA Ue Basmanav F.B., Cau L., Tafazzoli A., Mechin M.C., Wolf S., Romano M.T.,
RA Valentin F., Wiegmann H., Huchenq A., Kandil R., Garcia Bartels N.,
RA Kilic A., George S., Ralser D.J., Bergner S., Ferguson D.J.,
RA Oprisoreanu A.M., Wehner M., Thiele H., Altmueller J., Nuernberg P.,
RA Swan D., Houniet D., Buechner A., Weibel L., Wagner N., Grimalt R.,
RA Bygum A., Serre G., Blume-Peytavi U., Sprecher E., Schoch S., Oji V.,
RA Hamm H., Farrant P., Simon M., Betz R.C.;
RT "Mutations in three genes encoding proteins involved in hair shaft
RT formation cause uncombable hair syndrome.";
RL Am. J. Hum. Genet. 99:1292-1304(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-693 IN COMPLEX WITH CALCIUM,
RP COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=11980702; DOI=10.1093/emboj/21.9.2055;
RA Ahvazi B., Kim H.C., Kee S.H., Nemes Z., Steinert P.M.;
RT "Three-dimensional structure of the human transglutaminase 3 enzyme:
RT binding of calcium ions changes structure for activation.";
RL EMBO J. 21:2055-2067(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-693 IN COMPLEX WITH CALCIUM AND
RP MAGNESIUM, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=12679341; DOI=10.1074/jbc.m301162200;
RA Ahvazi B., Boeshans K.M., Idler W., Baxa U., Steinert P.M.;
RT "Roles of calcium ions in the activation and activity of the
RT transglutaminase 3 enzyme.";
RL J. Biol. Chem. 278:23834-23841(2003).
CC -!- FUNCTION: Catalyzes the calcium-dependent formation of isopeptide
CC cross-links between glutamine and lysine residues in various proteins,
CC as well as the conjugation of polyamines to proteins. Involved in the
CC formation of the cornified envelope (CE), a specialized component
CC consisting of covalent cross-links of proteins beneath the plasma
CC membrane of terminally differentiated keratinocytes. Catalyzes small
CC proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form
CC small interchain oligomers, which are further cross-linked by TGM1 onto
CC the growing CE scaffold (By similarity). In hair follicles, involved in
CC cross-linking structural proteins to hardening the inner root sheath.
CC {ECO:0000250}.
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, ECO:0000269|PubMed:11980702,
CC ECO:0000269|PubMed:12679341, ECO:0000269|PubMed:27866708};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11980702, ECO:0000269|PubMed:12679341};
CC Note=Binds 3 Ca(2+) cations per subunit. Binds 1 Ca(2+) as a zymogen,
CC and binds 2 more Ca(2+) cations, or other divalent metal cations, after
CC proteolytic processing. {ECO:0000269|PubMed:11980702,
CC ECO:0000269|PubMed:12679341};
CC -!- SUBUNIT: Consists of two polypeptide chains, which are synthesized as a
CC precursor form of a single polypeptide. {ECO:0000269|PubMed:11980702,
CC ECO:0000269|PubMed:12679341}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27866708}.
CC -!- PTM: Activated by proteolytic processing. In vitro activation is
CC commonly achieved by cleavage with dispase, a neutral bacterial
CC protease. Dispase cleavage site was proposed to lie between Ser-470 and
CC Ser-471 (PubMed:8099584) or between Pro-465 and Phe-466
CC (PubMed:16565075). Physiological activation may be catalyzed by CTSL
CC and, to a lesser extent, by CTSS, but not by CTSB, CTSD nor CTSV
CC (PubMed:16565075). {ECO:0000269|PubMed:16565075,
CC ECO:0000269|PubMed:8099584}.
CC -!- DISEASE: Uncombable hair syndrome 2 (UHS2) [MIM:617251]: A form of
CC uncombable hair syndrome, a condition characterized by scalp hair that
CC is impossible to comb due to the haphazard arrangement of the hair
CC bundles. A characteristic morphologic feature is a triangular to
CC reniform to heart shape on cross-sections, and a groove, canal or
CC flattening along the entire length of the hair. Most individuals are
CC affected early in childhood and the hair takes on a spun-glass
CC appearance with the hair becoming dry, curly, glossy, lighter in color,
CC and progressively uncombable. The hair growth rate can range from slow
CC to normal, and the condition improves with age.
CC {ECO:0000269|PubMed:27866708}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tgm3/";
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DR EMBL; L10386; AAA61155.1; -; mRNA.
DR EMBL; AK290324; BAF83013.1; -; mRNA.
DR EMBL; AK291351; BAF84040.1; -; mRNA.
DR EMBL; AK315236; BAG37663.1; -; mRNA.
DR EMBL; EF102483; ABK41960.1; -; Genomic_DNA.
DR EMBL; AL031678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10601.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10602.1; -; Genomic_DNA.
DR EMBL; BC109075; AAI09076.1; -; mRNA.
DR EMBL; BC109076; AAI09077.1; -; mRNA.
DR CCDS; CCDS33435.1; -.
DR PIR; A45991; A45991.
DR RefSeq; NP_003236.3; NM_003245.3.
DR PDB; 1L9M; X-ray; 2.10 A; A/B=2-693.
DR PDB; 1L9N; X-ray; 2.10 A; A/B=2-693.
DR PDB; 1NUD; X-ray; 2.70 A; A/B=2-693.
DR PDB; 1NUF; X-ray; 2.70 A; A=2-693.
DR PDB; 1NUG; X-ray; 2.40 A; A/B=2-693.
DR PDBsum; 1L9M; -.
DR PDBsum; 1L9N; -.
DR PDBsum; 1NUD; -.
DR PDBsum; 1NUF; -.
DR PDBsum; 1NUG; -.
DR AlphaFoldDB; Q08188; -.
DR SMR; Q08188; -.
DR BioGRID; 112911; 159.
DR IntAct; Q08188; 27.
DR MINT; Q08188; -.
DR STRING; 9606.ENSP00000370867; -.
DR BindingDB; Q08188; -.
DR ChEMBL; CHEMBL3363; -.
DR DrugBank; DB01864; 5'-Guanosine-Diphosphate-Monothiophosphate.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR DrugBank; DB00130; L-Glutamine.
DR GlyGen; Q08188; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08188; -.
DR PhosphoSitePlus; Q08188; -.
DR BioMuta; TGM3; -.
DR DMDM; 257051080; -.
DR EPD; Q08188; -.
DR jPOST; Q08188; -.
DR MassIVE; Q08188; -.
DR MaxQB; Q08188; -.
DR PaxDb; Q08188; -.
DR PeptideAtlas; Q08188; -.
DR PRIDE; Q08188; -.
DR ProteomicsDB; 58578; -.
DR TopDownProteomics; Q08188; -.
DR Antibodypedia; 1375; 312 antibodies from 32 providers.
DR DNASU; 7053; -.
DR Ensembl; ENST00000381458.6; ENSP00000370867.5; ENSG00000125780.12.
DR GeneID; 7053; -.
DR KEGG; hsa:7053; -.
DR MANE-Select; ENST00000381458.6; ENSP00000370867.5; NM_003245.4; NP_003236.3.
DR UCSC; uc002wfx.5; human.
DR CTD; 7053; -.
DR DisGeNET; 7053; -.
DR GeneCards; TGM3; -.
DR HGNC; HGNC:11779; TGM3.
DR HPA; ENSG00000125780; Tissue enriched (esophagus).
DR MalaCards; TGM3; -.
DR MIM; 600238; gene.
DR MIM; 617251; phenotype.
DR neXtProt; NX_Q08188; -.
DR OpenTargets; ENSG00000125780; -.
DR Orphanet; 1410; Uncombable hair syndrome.
DR PharmGKB; PA36492; -.
DR VEuPathDB; HostDB:ENSG00000125780; -.
DR eggNOG; ENOG502QUPB; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_1_0_1; -.
DR InParanoid; Q08188; -.
DR OMA; SMVGWNF; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; Q08188; -.
DR TreeFam; TF324278; -.
DR BRENDA; 2.3.2.13; 2681.
DR PathwayCommons; Q08188; -.
DR SignaLink; Q08188; -.
DR BioGRID-ORCS; 7053; 4 hits in 1064 CRISPR screens.
DR ChiTaRS; TGM3; human.
DR EvolutionaryTrace; Q08188; -.
DR GeneWiki; TGM3; -.
DR GenomeRNAi; 7053; -.
DR Pharos; Q08188; Tchem.
DR PRO; PR:Q08188; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q08188; protein.
DR Bgee; ENSG00000125780; Expressed in lower esophagus mucosa and 83 other tissues.
DR Genevisible; Q08188; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; TAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0043163; P:cell envelope organization; IDA:UniProtKB.
DR GO; GO:0031069; P:hair follicle morphogenesis; TAS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0030216; P:keratinocyte differentiation; IEP:UniProtKB.
DR GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
DR GO; GO:0036211; P:protein modification process; NAS:UniProtKB.
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; 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; 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 3D-structure; Acetylation; Acyltransferase; Calcium; Cytoplasm;
KW Direct protein sequencing; Keratinization; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..467
FT /note="Protein-glutamine gamma-glutamyltransferase E 50 kDa
FT catalytic chain"
FT /id="PRO_0000033652"
FT CHAIN 468..693
FT /note="Protein-glutamine gamma-glutamyltransferase E 27 kDa
FT non-catalytic chain"
FT /id="PRO_0000033653"
FT ACT_SITE 273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11980702,
FT ECO:0000269|PubMed:12679341"
FT SITE 467..468
FT /note="Cleavage; by CTSL"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 111
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VARIANT 13
FT /note="T -> K (in dbSNP:rs214803)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8099584,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5, ECO:0000269|Ref.7"
FT /id="VAR_040067"
FT VARIANT 163
FT /note="I -> L (in dbSNP:rs6048066)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_040068"
FT VARIANT 249
FT /note="S -> N (in dbSNP:rs214814)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_040069"
FT VARIANT 562
FT /note="K -> R (in dbSNP:rs1042617)"
FT /evidence="ECO:0000269|PubMed:8099584"
FT /id="VAR_040070"
FT VARIANT 654
FT /note="G -> R (in dbSNP:rs214830)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8099584,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5"
FT /id="VAR_040071"
FT VARIANT 687
FT /note="L -> M (in dbSNP:rs45581032)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_055360"
FT CONFLICT 58..59
FT /note="VS -> DT (in Ref. 1; AAA61155)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="N -> G (in Ref. 1; AAA61155)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> G (in Ref. 2; BAF84040)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="S -> P (in Ref. 1; AAA61155)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="D -> G (in Ref. 2; BAF84040)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 122..134
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 326..337
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1NUG"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1NUD"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 408..426
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:1NUF"
FT HELIX 447..460
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 499..507
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 513..524
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 530..543
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 548..555
FT /evidence="ECO:0007829|PDB:1L9M"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 569..577
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 584..591
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 597..603
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 611..618
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 627..633
FT /evidence="ECO:0007829|PDB:1L9M"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:1L9N"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 654..661
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 667..677
FT /evidence="ECO:0007829|PDB:1L9M"
FT STRAND 680..692
FT /evidence="ECO:0007829|PDB:1L9M"
SQ SEQUENCE 693 AA; 76632 MW; EAFAC0C9A8AA5FD6 CRC64;
MAALGVQSIN WQTAFNRQAH HTDKFSSQEL ILRRGQNFQV LMIMNKGLGS NERLEFIVST
GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI SSPASAPIGR YTMALQIFSQ
GGISSVKLGT FILLFNPWLN VDSVFMGNHA EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ
FEEDILSICL SILDRSLNFR RDAATDVASR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT
YTGGRDPRSW NGSVEILKNW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA
HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW QVLDATPQER
SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW LYDNTTGKQW KNSVNSHTIG
RYISTKAVGS NARMDVTDKY KYPEGSDQER QVFQKALGKL KPNTPFAATS SMGLETEEQE
PSIIGKLKVA GMLAVGKEVN LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT
MSLDPEEEAE HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDI ILDNPTLTLE
VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG PKEGSRVRFD
ILPSRSGTKQ LLADFSCNKF PAIKAMLSID VAE
