TGM4_MOUSE
ID TGM4_MOUSE Reviewed; 670 AA.
AC Q8BZH1; B7ZP44; Q8K460;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 4 {ECO:0000303|PubMed:19027372};
DE EC=2.3.2.13;
DE AltName: Full=Experimental autoimmune prostatitis antigen 1 {ECO:0000303|PubMed:16223778};
DE AltName: Full=Transglutaminase-4 {ECO:0000303|PubMed:19027372};
DE Short=TGase-4 {ECO:0000250|UniProtKB:Q99041};
GN Name=Tgm4 {ECO:0000312|EMBL:BAC29013.1, ECO:0000312|MGI:MGI:3027002};
GN Synonyms=Eapa1 {ECO:0000312|EMBL:AAM45940.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAM45940.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM45940.1};
RX PubMed=16223778; DOI=10.1182/blood-2005-08-3088;
RA Setiady Y.Y., Ohno K., Samy E.T., Bagavant H., Qiao H., Sharp C., She J.X.,
RA Tung K.S.K.;
RT "Physiologic self antigens rapidly capacitate autoimmune disease-specific
RT polyclonal CD4+ CD25+ regulatory T cells.";
RL Blood 107:1056-1062(2006).
RN [2] {ECO:0000312|EMBL:BAC29013.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29013.1};
RC TISSUE=Urinary bladder {ECO:0000312|EMBL:BAC29013.1};
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 [3] {ECO:0000312|EMBL:AAI41298.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 5-19; 37-58; 67-81; 146-162; 166-176; 288-300; 308-322;
RP 324-359; 368-386; 394-406; 418-435; 484-500; 525-536 AND 595-642, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Coagulating gland secretion {ECO:0000269|PubMed:19027372};
RX PubMed=19027372; DOI=10.1016/j.jchromb.2008.10.041;
RA Tseng H.-C., Lin H.-J., Sudhakar Gandhi P.S., Wang C.-Y., Chen Y.-H.;
RT "Purification and identification of transglutaminase from mouse coagulating
RT gland and its cross-linking activity among seminal vesicle secretion
RT proteins.";
RL J. Chromatogr. B 876:198-202(2008).
CC -!- FUNCTION: Associated with the mammalian reproductive process. Plays an
CC important role in the formation of the seminal coagulum through the
CC cross-linking of specific proteins present in the seminal plasma.
CC Transglutaminase is also required to stabilize the copulatory plug.
CC {ECO:0000269|PubMed:19027372}.
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:19027372};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00488};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00488};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99041}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19027372}.
CC -!- TISSUE SPECIFICITY: Expressed in the coagulating gland and in the
CC dorsal part of the prostate. Not expressed in the brain, heart, kidney,
CC liver, lung, muscle, pancreas, spleen, stomach, testis and thymus.
CC {ECO:0000269|PubMed:16223778, ECO:0000269|PubMed:19027372}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000255}.
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DR EMBL; AF486627; AAM45940.1; -; mRNA.
DR EMBL; AK035279; BAC29013.1; -; mRNA.
DR EMBL; BC141297; AAI41298.1; -; mRNA.
DR EMBL; BC145622; AAI45623.1; -; mRNA.
DR CCDS; CCDS23653.1; -.
DR RefSeq; NP_808579.2; NM_177911.4.
DR AlphaFoldDB; Q8BZH1; -.
DR SMR; Q8BZH1; -.
DR STRING; 10090.ENSMUSP00000026893; -.
DR GlyGen; Q8BZH1; 5 sites.
DR iPTMnet; Q8BZH1; -.
DR PhosphoSitePlus; Q8BZH1; -.
DR PaxDb; Q8BZH1; -.
DR PRIDE; Q8BZH1; -.
DR ProteomicsDB; 262902; -.
DR DNASU; 331046; -.
DR GeneID; 331046; -.
DR KEGG; mmu:331046; -.
DR UCSC; uc009sfo.1; mouse.
DR CTD; 7047; -.
DR MGI; MGI:3027002; Tgm4.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR InParanoid; Q8BZH1; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; Q8BZH1; -.
DR TreeFam; TF324278; -.
DR BRENDA; 2.3.2.13; 3474.
DR BioGRID-ORCS; 331046; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Tgm4; mouse.
DR PRO; PR:Q8BZH1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BZH1; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0042628; P:mating plug formation; IMP:MGI.
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; Copulatory plug; Direct protein sequencing;
KW Glycoprotein; Metal-binding; Reference proteome; Secreted; Transferase.
FT CHAIN 1..670
FT /note="Protein-glutamine gamma-glutamyltransferase 4"
FT /id="PRO_0000385448"
FT ACT_SITE 255
FT /evidence="ECO:0000250|UniProtKB:P00488,
FT ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 314
FT /evidence="ECO:0000250|UniProtKB:P00488,
FT ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 337
FT /evidence="ECO:0000250|UniProtKB:P00488,
FT ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 134
FT /note="D -> G (in Ref. 2; BAC29013)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="L -> I (in Ref. 2; BAC29013 and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="R -> K (in Ref. 2; BAC29013 and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="T -> A (in Ref. 2; BAC29013)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="K -> E (in Ref. 2; BAC29013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 75591 MW; AEAD1A23E3D97EC4 CRC64;
MDSRNVLIIY AVNVERKLNA AAHHTSEYQT KKLVLRRGQI FTLKVILNRP LQPQDELKVT
FTSGQRDPPY MVELDPVTSY RSKGWQVKIA KQSGVEVILN VISAADAVVG RYKMRVNEYK
AGVFYLLFNP WCSDDSVFMA SEEERAEYIL NDTGYMYMGF AKQIKEKPWT FGQFEKHILS
CCFNLLFQLE NNEMQNPVLV SRAICTMMCA ANGGVLMGNW TGDYADGTAP YVWTSSVPIL
QQHYVTRMPV RYGQCWVFSG ILTTALRAVG IPARSVTNFE SAHDTEKNLT VDIYLDESGK
TIPHLTKDSV WNFHVWTDAW MKRQDLPHGY DGWQVLDSTP QEISDGGFRT GPSPLTAIRQ
GLIQMKYDTT FVFTEVNGDK FIWLVKQNQE REKNILIAVE TASLGKKIST KMVGENRRED
ITLQYRFPEG SPEERKVMAK ASGKPSDDKL NSRTLNNSLQ ISVLQNSLEL GAPIYLTITL
KRKTATPQNV NISCSLNLQT YTGNKKTNLG VIQKTVQIHG QESRVFLTMD ASYYIYKLGM
VDDEMVIGGF IIAEIVDSGE RVATDTTLCF LYSAFSVEMP STGKVKQPLV ITSKFTNTLP
IPLTNIKFSV ESLGLANMKS WEQETVPPGK TITFQMECTP VKAGPQKFIV KFISRQVKEV
HAEKVVLISK
