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   08-NOV-2023, entry version 128.
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   GlyCosmos; Q8BZH1; 5 sites, No reported glycans.
DR   GlyGen; Q8BZH1; 5 sites.
DR   iPTMnet; Q8BZH1; -.
DR   PhosphoSitePlus; Q8BZH1; -.
DR   PaxDb; 10090-ENSMUSP00000026893; -.
DR   ProteomicsDB; 262902; -.
DR   DNASU; 331046; -.
DR   GeneID; 331046; -.
DR   KEGG; mmu:331046; -.
DR   UCSC; uc009sfo.1; mouse.
DR   AGR; MGI:3027002; -.
DR   CTD; 7047; -.
DR   MGI; MGI:3027002; Tgm4.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   InParanoid; Q8BZH1; -.
DR   OrthoDB; 5344745at2759; -.
DR   PhylomeDB; Q8BZH1; -.
DR   TreeFam; TF324278; -.
DR   BRENDA; 2.3.2.13; 3474.
DR   BioGRID-ORCS; 331046; 0 hits in 76 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   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 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   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11590:SF70; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 4; 1.
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; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
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
//