GenomeNet

Database: UniProt/SWISS-PROT
Entry: TGM3_HUMAN
LinkDB: TGM3_HUMAN
Original site: 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   18-JUL-2018, entry version 179.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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;
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
RT   human and mouse.";
RL   J. Biol. Chem. 268:12682-12690(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-13 AND
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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;
RP   ASN-249; 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.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   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.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   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
RT   project: 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
RP   INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP   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.,
RA   Yamamoto K., Nishi K., Watts C., Reinheckel T., Schalkwijk J.,
RA   Zeeuwen P.L.;
RT   "Cystatin M/E is a high affinity inhibitor of cathepsin V and
RT   cathepsin L by a reactive site that is distinct from the legumain-
RT   binding site. A novel clue for the role of cystatin M/E in epidermal
RT   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.,
RA   Buerckstuemmer T., 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.,
RA   Romano M.T., Valentin F., Wiegmann H., Huchenq A., Kandil R.,
RA   Garcia Bartels N., Kilic A., George S., Ralser D.J., Bergner S.,
RA   Ferguson D.J., Oprisoreanu A.M., Wehner M., Thiele H., Altmueller J.,
RA   Nuernberg P., Swan D., Houniet D., Buechner A., Weibel L., Wagner N.,
RA   Grimalt R., Bygum A., Serre G., Blume-Peytavi U., Sprecher E.,
RA   Schoch S., Oji V., 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
RP   CALCIUM, 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
RP   CALCIUM AND 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
CC       proteins, as well as the conjugation of polyamines to proteins.
CC       Involved in the formation of the cornified envelope (CE), a
CC       specialized component consisting of covalent cross-links of
CC       proteins beneath the plasma membrane of terminally differentiated
CC       keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and
CC       SPRR2) and LOR cross-linking to form small interchain oligomers,
CC       which are further cross-linked by TGM1 onto the growing CE
CC       scaffold (By similarity). In hair follicles, involved in cross-
CC       linking structural proteins to hardening the inner root sheath.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
CC       protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
CC       {ECO:0000255|PROSITE-ProRule:PRU10024,
CC       ECO:0000269|PubMed:11980702, ECO:0000269|PubMed:12679341,
CC       ECO:0000269|PubMed:27866708}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:11980702,
CC         ECO:0000269|PubMed:12679341};
CC       Note=Binds 3 Ca(2+) cations per subunit. Binds 1 Ca(2+) as a
CC       zymogen, and binds 2 more Ca(2+) cations, or other divalent metal
CC       cations, after proteolytic processing.
CC       {ECO:0000269|PubMed:11980702, ECO:0000269|PubMed:12679341};
CC   -!- SUBUNIT: Consists of two polypeptide chains, which are synthesized
CC       as a precursor form of a single polypeptide.
CC       {ECO:0000269|PubMed:11980702, 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-
CC       470 and Ser-471 (PubMed:8099584) or between Pro-465 and Phe-466
CC       (PubMed:16565075). Physiological activation may be catalyzed by
CC       CTSL and, to a lesser extent, by CTSS, but not by CTSB, CTSD nor
CC       CTSV (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
CC       that is impossible to comb due to the haphazard arrangement of the
CC       hair bundles. A characteristic morphologic feature is a triangular
CC       to reniform to heart shape on cross-sections, and a groove, canal
CC       or flattening along the entire length of the hair. Most
CC       individuals are affected early in childhood and the hair takes on
CC       a spun-glass appearance with the hair becoming dry, curly, glossy,
CC       lighter in color, and progressively uncombable. The hair growth
CC       rate can range from slow to normal, and the condition improves
CC       with age. {ECO:0000269|PubMed:27866708}. Note=The disease is
CC       caused by mutations 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/";
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   UniGene; Hs.2022; -.
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   ProteinModelPortal; Q08188; -.
DR   SMR; Q08188; -.
DR   BioGrid; 112911; 26.
DR   IntAct; Q08188; 9.
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   iPTMnet; Q08188; -.
DR   PhosphoSitePlus; Q08188; -.
DR   BioMuta; TGM3; -.
DR   DMDM; 257051080; -.
DR   EPD; Q08188; -.
DR   MaxQB; Q08188; -.
DR   PaxDb; Q08188; -.
DR   PeptideAtlas; Q08188; -.
DR   PRIDE; Q08188; -.
DR   ProteomicsDB; 58578; -.
DR   TopDownProteomics; Q08188; -.
DR   Ensembl; ENST00000381458; ENSP00000370867; ENSG00000125780.
DR   GeneID; 7053; -.
DR   KEGG; hsa:7053; -.
DR   UCSC; uc002wfx.5; human.
DR   CTD; 7053; -.
DR   DisGeNET; 7053; -.
DR   EuPathDB; HostDB:ENSG00000125780.11; -.
DR   GeneCards; TGM3; -.
DR   HGNC; HGNC:11779; TGM3.
DR   HPA; HPA004728; -.
DR   MalaCards; TGM3; -.
DR   MIM; 600238; gene.
DR   MIM; 617251; phenotype.
DR   neXtProt; NX_Q08188; -.
DR   OpenTargets; ENSG00000125780; -.
DR   PharmGKB; PA36492; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00760000119108; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; Q08188; -.
DR   KO; K05620; -.
DR   OMA; KADNMIR; -.
DR   OrthoDB; EOG091G030K; -.
DR   PhylomeDB; Q08188; -.
DR   TreeFam; TF324278; -.
DR   BRENDA; 2.3.2.13; 2681.
DR   ChiTaRS; TGM3; human.
DR   EvolutionaryTrace; Q08188; -.
DR   GeneWiki; TGM3; -.
DR   GenomeRNAi; 7053; -.
DR   PRO; PR:Q08188; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; ENSG00000125780; -.
DR   CleanEx; HS_TGM3; -.
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: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:0016746; F:transferase activity, transferring acyl groups; TAS:UniProtKB.
DR   GO; GO:0043163; P:cell envelope organization; IDA:UniProtKB.
DR   GO; GO:0006464; P:cellular protein modification process; NAS: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:0051262; P:protein tetramerization; IDA: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;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Keratinization; Metal-binding; Phosphoprotein; Polymorphism;
KW   Reference proteome; Transferase; Zymogen.
FT   INIT_MET      1      1       Removed. {ECO:0000269|Ref.7}.
FT   CHAIN         2    467       Protein-glutamine gamma-
FT                                glutamyltransferase E 50 kDa catalytic
FT                                chain.
FT                                /FTId=PRO_0000033652.
FT   CHAIN       468    693       Protein-glutamine gamma-
FT                                glutamyltransferase E 27 kDa non-
FT                                catalytic chain.
FT                                /FTId=PRO_0000033653.
FT   ACT_SITE    273    273       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    331    331       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    354    354       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       222    222       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       225    225       Calcium 1. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       227    227       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       228    228       Calcium 1. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       230    230       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       302    302       Calcium 2. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       304    304       Calcium 2. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       306    306       Calcium 2. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       308    308       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       325    325       Calcium 2. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       394    394       Calcium 3. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       416    416       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       444    444       Calcium 3. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   METAL       449    449       Calcium 3. {ECO:0000269|PubMed:11980702,
FT                                ECO:0000269|PubMed:12679341}.
FT   SITE        467    468       Cleavage; by CTSL.
FT   MOD_RES       2      2       N-acetylalanine. {ECO:0000269|Ref.7}.
FT   MOD_RES     111    111       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     112    112       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   VARIANT      13     13       T -> K (in dbSNP:rs214803).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8099584,
FT                                ECO:0000269|Ref.3, ECO:0000269|Ref.5,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_040067.
FT   VARIANT     163    163       I -> L (in dbSNP:rs6048066).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_040068.
FT   VARIANT     249    249       S -> N (in dbSNP:rs214814).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_040069.
FT   VARIANT     562    562       K -> R (in dbSNP:rs1042617).
FT                                {ECO:0000269|PubMed:8099584}.
FT                                /FTId=VAR_040070.
FT   VARIANT     654    654       G -> R (in dbSNP:rs214830).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8099584,
FT                                ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
FT                                /FTId=VAR_040071.
FT   VARIANT     687    687       L -> M (in dbSNP:rs45581032).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_055360.
FT   CONFLICT     58     59       VS -> DT (in Ref. 1; AAA61155).
FT                                {ECO:0000305}.
FT   CONFLICT    251    251       N -> G (in Ref. 1; AAA61155).
FT                                {ECO:0000305}.
FT   CONFLICT    324    324       S -> G (in Ref. 2; BAF84040).
FT                                {ECO:0000305}.
FT   CONFLICT    346    346       S -> P (in Ref. 1; AAA61155).
FT                                {ECO:0000305}.
FT   CONFLICT    674    674       D -> G (in Ref. 2; BAF84040).
FT                                {ECO:0000305}.
FT   STRAND        6     10       {ECO:0000244|PDB:1L9M}.
FT   HELIX        13     19       {ECO:0000244|PDB:1L9M}.
FT   STRAND       31     33       {ECO:0000244|PDB:1L9M}.
FT   STRAND       38     46       {ECO:0000244|PDB:1L9M}.
FT   STRAND       53     59       {ECO:0000244|PDB:1L9M}.
FT   STRAND       61     63       {ECO:0000244|PDB:1L9M}.
FT   TURN         66     69       {ECO:0000244|PDB:1L9M}.
FT   STRAND       70     79       {ECO:0000244|PDB:1L9M}.
FT   STRAND       82     92       {ECO:0000244|PDB:1L9M}.
FT   STRAND       95    101       {ECO:0000244|PDB:1L9M}.
FT   STRAND      109    119       {ECO:0000244|PDB:1L9M}.
FT   STRAND      122    134       {ECO:0000244|PDB:1L9M}.
FT   HELIX       149    155       {ECO:0000244|PDB:1L9M}.
FT   STRAND      160    167       {ECO:0000244|PDB:1L9M}.
FT   STRAND      170    177       {ECO:0000244|PDB:1L9M}.
FT   HELIX       185    193       {ECO:0000244|PDB:1L9M}.
FT   HELIX       197    201       {ECO:0000244|PDB:1L9M}.
FT   HELIX       203    208       {ECO:0000244|PDB:1L9M}.
FT   HELIX       209    211       {ECO:0000244|PDB:1L9M}.
FT   HELIX       213    223       {ECO:0000244|PDB:1L9M}.
FT   TURN        227    229       {ECO:0000244|PDB:1L9M}.
FT   STRAND      231    235       {ECO:0000244|PDB:1L9M}.
FT   HELIX       247    249       {ECO:0000244|PDB:1L9M}.
FT   HELIX       253    262       {ECO:0000244|PDB:1L9M}.
FT   STRAND      268    271       {ECO:0000244|PDB:1L9M}.
FT   HELIX       273    287       {ECO:0000244|PDB:1L9M}.
FT   STRAND      291    300       {ECO:0000244|PDB:1L9M}.
FT   STRAND      305    313       {ECO:0000244|PDB:1L9M}.
FT   TURN        322    325       {ECO:0000244|PDB:1L9M}.
FT   STRAND      326    337       {ECO:0000244|PDB:1L9M}.
FT   TURN        341    343       {ECO:0000244|PDB:1L9M}.
FT   HELIX       345    347       {ECO:0000244|PDB:1NUG}.
FT   STRAND      349    353       {ECO:0000244|PDB:1L9M}.
FT   STRAND      356    359       {ECO:0000244|PDB:1NUD}.
FT   HELIX       372    377       {ECO:0000244|PDB:1L9M}.
FT   TURN        383    385       {ECO:0000244|PDB:1L9M}.
FT   HELIX       386    394       {ECO:0000244|PDB:1L9M}.
FT   STRAND      396    403       {ECO:0000244|PDB:1L9M}.
FT   TURN        404    407       {ECO:0000244|PDB:1L9M}.
FT   STRAND      408    426       {ECO:0000244|PDB:1L9M}.
FT   STRAND      433    435       {ECO:0000244|PDB:1L9M}.
FT   HELIX       437    440       {ECO:0000244|PDB:1L9M}.
FT   STRAND      444    446       {ECO:0000244|PDB:1NUF}.
FT   HELIX       447    460       {ECO:0000244|PDB:1L9M}.
FT   STRAND      482    489       {ECO:0000244|PDB:1L9M}.
FT   STRAND      499    507       {ECO:0000244|PDB:1L9M}.
FT   STRAND      509    511       {ECO:0000244|PDB:1L9M}.
FT   STRAND      513    524       {ECO:0000244|PDB:1L9M}.
FT   STRAND      530    543       {ECO:0000244|PDB:1L9M}.
FT   STRAND      548    555       {ECO:0000244|PDB:1L9M}.
FT   HELIX       557    560       {ECO:0000244|PDB:1L9M}.
FT   TURN        561    563       {ECO:0000244|PDB:1L9M}.
FT   STRAND      569    577       {ECO:0000244|PDB:1L9M}.
FT   STRAND      584    591       {ECO:0000244|PDB:1L9M}.
FT   STRAND      597    603       {ECO:0000244|PDB:1L9M}.
FT   STRAND      611    618       {ECO:0000244|PDB:1L9M}.
FT   STRAND      621    623       {ECO:0000244|PDB:1L9M}.
FT   STRAND      627    633       {ECO:0000244|PDB:1L9M}.
FT   TURN        635    637       {ECO:0000244|PDB:1L9M}.
FT   STRAND      638    640       {ECO:0000244|PDB:1L9N}.
FT   STRAND      642    646       {ECO:0000244|PDB:1L9M}.
FT   STRAND      654    661       {ECO:0000244|PDB:1L9M}.
FT   STRAND      667    677       {ECO:0000244|PDB:1L9M}.
FT   STRAND      680    692       {ECO:0000244|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
//
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