TGM5_MOUSE
ID TGM5_MOUSE Reviewed; 724 AA.
AC Q9D7I9; A2AQ62; Q3V1F9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 5;
DE EC=2.3.2.13;
DE AltName: Full=Transglutaminase-5;
DE Short=TGase-5;
GN Name=Tgm5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Catalyzes the cross-linking of proteins and the conjugation
CC of polyamines to proteins. Contributes to the formation of the
CC cornified cell envelope of keratinocytes (By similarity).
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};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated with
CC intermediate filaments. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; AK009196; BAB26133.1; -; mRNA.
DR EMBL; AK132482; BAE21192.1; -; mRNA.
DR EMBL; AL844548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16632.1; -.
DR RefSeq; NP_083075.1; NM_028799.2.
DR AlphaFoldDB; Q9D7I9; -.
DR SMR; Q9D7I9; -.
DR STRING; 10090.ENSMUSP00000028721; -.
DR PhosphoSitePlus; Q9D7I9; -.
DR MaxQB; Q9D7I9; -.
DR PaxDb; Q9D7I9; -.
DR PRIDE; Q9D7I9; -.
DR ProteomicsDB; 262903; -.
DR Antibodypedia; 23845; 191 antibodies from 27 providers.
DR DNASU; 74176; -.
DR Ensembl; ENSMUST00000028721; ENSMUSP00000028721; ENSMUSG00000053675.
DR GeneID; 74176; -.
DR KEGG; mmu:74176; -.
DR UCSC; uc008lxl.1; mouse.
DR CTD; 9333; -.
DR MGI; MGI:1921426; Tgm5.
DR VEuPathDB; HostDB:ENSMUSG00000053675; -.
DR eggNOG; ENOG502QTRA; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_1_0_1; -.
DR InParanoid; Q9D7I9; -.
DR OMA; RSSWNNV; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; Q9D7I9; -.
DR TreeFam; TF324278; -.
DR BioGRID-ORCS; 74176; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9D7I9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D7I9; protein.
DR Bgee; ENSMUSG00000053675; Expressed in coelomic epithelium and 53 other tissues.
DR Genevisible; Q9D7I9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Calcium; Cytoplasm; Metal-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43548"
FT CHAIN 2..724
FT /note="Protein-glutamine gamma-glutamyltransferase 5"
FT /id="PRO_0000213714"
FT REGION 473..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43548"
SQ SEQUENCE 724 AA; 81014 MW; FB6A22FDEB5F8329 CRC64;
MAQGCPITGL EVALTDLQSS QNNVRHHTEE ISVDRLVVRR GQAFSITLYF KNRGFQPGMD
SIMFVAETGP LPDLAKGTRA VFSFTGSGGP SPWIASLEAN RANSLEVSLC APPIAAVGRY
LLKIRIDSYQ GFVTAYQLGE FILLFNPWCP ADSVYLESEP QRQEYVVNDY GFIYQGSKSW
IRPCPWNYGQ FEENIIDICL ELLEKSLNFQ VDPSTDCALR GSPVYTSRVV CAMINSNDDN
GVLNGNWSEN YVDGINPAEW TGSVAILKQW HATGCQPVRY GQCWVFAAVM CTVMRCLGIP
TRVITNFDSG HDTDGNLIID EYYDNTGRIL ENMKKDTVWN FHVWNECWMA RKDLPPGYGG
WQVLDATPQE TSNGLYCCGP ASVKAIKEGE IDLNYDTRFA FSMVNADCMS WLVYGGKEQK
LHQDTATVGN FISTKSIQSD ERDDITESYK YEEGSLQERE VFLKALQKLQ ATRSQGPHQA
NSNPFSSVPP RHNSARSPDS PSLQPSDVLQ VSLKFELLDS PKMGQDINFV LLAVNMSPQF
KDLKLNLSAQ SLLHDGSPLV PFWQDTAFIT LFPEEEKSYP CKILYSQYSQ YLSTDKLIRI
SALGEEKNSP EKILVNKIIT LTFPGIMINV LGAAFVNQPL TVQVVFSNPL SEPVEDCVLT
LEGSGLFRKQ QRVLIGVLKP HHKASITLKT VPFKSGQRQI QANLRSNRFK DIKGYKNVYV
DIGL
