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Database: UniProt
Entry: TGM4_MOUSE
LinkDB: TGM4_MOUSE
Original site: 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   20-JUN-2018, entry version 109.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She J.X., Tung K.S.K.;
RT   "Physiologic self antigens rapidly capacitate autoimmune disease-
RT   specific 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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;
RP   308-322; 324-359; 368-386; 394-406; 418-435; 484-500; 525-536 AND
RP   595-642, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   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
RT   coagulating gland and its cross-linking activity among seminal vesicle
RT   secretion proteins.";
RL   J. Chromatogr. B 876:198-202(2008).
CC   -!- FUNCTION: Associated with the mammalian reproductive process.
CC       Plays an important role in the formation of the seminal coagulum
CC       through the cross-linking of specific proteins present in the
CC       seminal plasma. Transglutaminase is also required to stabilize the
CC       copulatory plug. {ECO:0000269|PubMed:19027372}.
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: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.
CC       {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,
CC       kidney, liver, lung, muscle, pancreas, spleen, stomach, testis and
CC       thymus. {ECO:0000269|PubMed:16223778,
CC       ECO:0000269|PubMed:19027372}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000255}.
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   UniGene; Mm.195309; -.
DR   ProteinModelPortal; Q8BZH1; -.
DR   SMR; Q8BZH1; -.
DR   STRING; 10090.ENSMUSP00000026893; -.
DR   iPTMnet; Q8BZH1; -.
DR   PhosphoSitePlus; Q8BZH1; -.
DR   PaxDb; Q8BZH1; -.
DR   PRIDE; Q8BZH1; -.
DR   GeneID; 331046; -.
DR   KEGG; mmu:331046; -.
DR   UCSC; uc009sfo.1; mouse.
DR   CTD; 7047; -.
DR   MGI; MGI:3027002; Tgm4.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   InParanoid; Q8BZH1; -.
DR   KO; K05621; -.
DR   PhylomeDB; Q8BZH1; -.
DR   TreeFam; TF324278; -.
DR   BRENDA; 2.3.2.13; 3474.
DR   ChiTaRS; Tgm4; mouse.
DR   PRO; PR:Q8BZH1; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; ISO:MGI.
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; IEA:UniProtKB-EC.
DR   GO; GO:0042628; P:mating plug formation; IMP:MGI.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
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; Complete proteome; Copulatory plug;
KW   Direct protein sequencing; Glycoprotein; Metal-binding;
KW   Reference proteome; Secreted; Transferase.
FT   CHAIN         1    670       Protein-glutamine gamma-
FT                                glutamyltransferase 4.
FT                                /FTId=PRO_0000385448.
FT   ACT_SITE    255    255       {ECO:0000250|UniProtKB:P00488,
FT                                ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    314    314       {ECO:0000250|UniProtKB:P00488,
FT                                ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    337    337       {ECO:0000250|UniProtKB:P00488,
FT                                ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       377    377       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       379    379       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       429    429       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       434    434       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    219    219       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    491    491       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    134    134       D -> G (in Ref. 2; BAC29013).
FT                                {ECO:0000305}.
FT   CONFLICT    404    404       L -> I (in Ref. 2; BAC29013 and 4; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    426    426       R -> K (in Ref. 2; BAC29013 and 4; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    528    528       T -> A (in Ref. 2; BAC29013).
FT                                {ECO:0000305}.
FT   CONFLICT    537    537       K -> E (in Ref. 2; BAC29013).
FT                                {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
//
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