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Protein-glutamine gamma-glutamyltransferase 4 (EC 2.3.2.13) (Experimental autoimmune prostatitis antigen 1) (Transglutaminase-4) (TGase-4)

 TGM4_MOUSE              Reviewed;         670 AA.
Q8BZH1; B7ZP44; Q8K460;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 2.
22-NOV-2017, entry version 107.
RecName: Full=Protein-glutamine gamma-glutamyltransferase 4 {ECO:0000303|PubMed:19027372};
EC=2.3.2.13;
AltName: Full=Experimental autoimmune prostatitis antigen 1 {ECO:0000303|PubMed:16223778};
AltName: Full=Transglutaminase-4 {ECO:0000303|PubMed:19027372};
Short=TGase-4 {ECO:0000250|UniProtKB:Q99041};
Name=Tgm4 {ECO:0000312|EMBL:BAC29013.1, ECO:0000312|MGI:MGI:3027002};
Synonyms=Eapa1 {ECO:0000312|EMBL:AAM45940.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAM45940.1}
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM45940.1};
PubMed=16223778; DOI=10.1182/blood-2005-08-3088;
Setiady Y.Y., Ohno K., Samy E.T., Bagavant H., Qiao H., Sharp C.,
She J.X., Tung K.S.K.;
"Physiologic self antigens rapidly capacitate autoimmune disease-
specific polyclonal CD4+ CD25+ regulatory T cells.";
Blood 107:1056-1062(2006).
[2] {ECO:0000312|EMBL:BAC29013.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29013.1};
TISSUE=Urinary bladder {ECO:0000312|EMBL:BAC29013.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000312|EMBL:AAI41298.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305}
PROTEIN SEQUENCE OF 5-19; 37-58; 67-81; 146-162; 166-176; 288-300;
308-322; 324-359; 368-386; 394-406; 418-435; 484-500; 525-536 AND
595-642, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Coagulating gland secretion {ECO:0000269|PubMed:19027372};
PubMed=19027372; DOI=10.1016/j.jchromb.2008.10.041;
Tseng H.-C., Lin H.-J., Sudhakar Gandhi P.S., Wang C.-Y., Chen Y.-H.;
"Purification and identification of transglutaminase from mouse
coagulating gland and its cross-linking activity among seminal vesicle
secretion proteins.";
J. Chromatogr. B 876:198-202(2008).
-!- FUNCTION: Associated with the mammalian reproductive process.
Plays an important role in the formation of the seminal coagulum
through the cross-linking of specific proteins present in the
seminal plasma. Transglutaminase is also required to stabilize the
copulatory plug. {ECO:0000269|PubMed:19027372}.
-!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
{ECO:0000255|PROSITE-ProRule:PRU10024,
ECO:0000269|PubMed:19027372}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P00488};
Note=Binds 1 Ca(2+) ion per subunit.
{ECO:0000250|UniProtKB:P00488};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99041}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19027372}.
-!- TISSUE SPECIFICITY: Expressed in the coagulating gland and in the
dorsal part of the prostate. Not expressed in the brain, heart,
kidney, liver, lung, muscle, pancreas, spleen, stomach, testis and
thymus. {ECO:0000269|PubMed:16223778,
ECO:0000269|PubMed:19027372}.
-!- SIMILARITY: Belongs to the transglutaminase superfamily.
Transglutaminase family. {ECO:0000255}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF486627; AAM45940.1; -; mRNA.
EMBL; AK035279; BAC29013.1; -; mRNA.
EMBL; BC141297; AAI41298.1; -; mRNA.
EMBL; BC145622; AAI45623.1; -; mRNA.
CCDS; CCDS23653.1; -.
RefSeq; NP_808579.2; NM_177911.4.
UniGene; Mm.195309; -.
ProteinModelPortal; Q8BZH1; -.
SMR; Q8BZH1; -.
STRING; 10090.ENSMUSP00000026893; -.
iPTMnet; Q8BZH1; -.
PhosphoSitePlus; Q8BZH1; -.
PaxDb; Q8BZH1; -.
PRIDE; Q8BZH1; -.
GeneID; 331046; -.
KEGG; mmu:331046; -.
UCSC; uc009sfo.1; mouse.
CTD; 7047; -.
MGI; MGI:3027002; Tgm4.
eggNOG; ENOG410IFMV; Eukaryota.
eggNOG; ENOG410XQEZ; LUCA.
HOGENOM; HOG000231695; -.
InParanoid; Q8BZH1; -.
KO; K05621; -.
PhylomeDB; Q8BZH1; -.
TreeFam; TF324278; -.
BRENDA; 2.3.2.13; 3474.
ChiTaRS; Tgm4; mouse.
PRO; PR:Q8BZH1; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0042628; P:mating plug formation; IMP:MGI.
GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.90.260.10; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002931; Transglutaminase-like.
InterPro; IPR036985; Transglutaminase-like_sf.
InterPro; IPR023608; Transglutaminase_animal.
InterPro; IPR013808; Transglutaminase_AS.
InterPro; IPR008958; Transglutaminase_C.
InterPro; IPR036238; Transglutaminase_C_sf.
InterPro; IPR001102; Transglutaminase_N.
Pfam; PF00927; Transglut_C; 1.
Pfam; PF01841; Transglut_core; 1.
Pfam; PF00868; Transglut_N; 1.
PIRSF; PIRSF000459; TGM_EBP42; 1.
SMART; SM00460; TGc; 1.
SUPFAM; SSF49309; SSF49309; 2.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS00547; TRANSGLUTAMINASES; 1.
1: Evidence at protein level;
Acyltransferase; Calcium; Complete proteome; Copulatory plug;
Direct protein sequencing; Glycoprotein; Metal-binding;
Reference proteome; Secreted; Transferase.
CHAIN 1 670 Protein-glutamine gamma-
glutamyltransferase 4.
/FTId=PRO_0000385448.
ACT_SITE 255 255 {ECO:0000250|UniProtKB:P00488,
ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 314 314 {ECO:0000250|UniProtKB:P00488,
ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 337 337 {ECO:0000250|UniProtKB:P00488,
ECO:0000255|PROSITE-ProRule:PRU10024}.
METAL 377 377 Calcium. {ECO:0000250|UniProtKB:P00488}.
METAL 379 379 Calcium. {ECO:0000250|UniProtKB:P00488}.
METAL 429 429 Calcium. {ECO:0000250|UniProtKB:P00488}.
METAL 434 434 Calcium. {ECO:0000250|UniProtKB:P00488}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 456 456 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 134 134 D -> G (in Ref. 2; BAC29013).
{ECO:0000305}.
CONFLICT 404 404 L -> I (in Ref. 2; BAC29013 and 4; AA
sequence). {ECO:0000305}.
CONFLICT 426 426 R -> K (in Ref. 2; BAC29013 and 4; AA
sequence). {ECO:0000305}.
CONFLICT 528 528 T -> A (in Ref. 2; BAC29013).
{ECO:0000305}.
CONFLICT 537 537 K -> E (in Ref. 2; BAC29013).
{ECO:0000305}.
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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