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Q8BZH1 (TGM4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase 4

EC=2.3.2.13
Alternative name(s):
Experimental autoimmune prostatitis antigen 1
Transglutaminase-4
Short name=TGase-4
Gene names
Name:Tgm4
Synonyms:Eapa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3. Ref.4

Cofactor

Binds 1 calcium ion per subunit By similarity. UniProtKB P00488

Subunit structure

Homodimer By similarity. UniProtKB Q99041

Subcellular location

Secreted Ref.4.

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. Ref.1 Ref.4

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 670670Protein-glutamine gamma-glutamyltransferase 4
PRO_0000385448

Sites

Active site2551 By similarity UniProtKB P00488
Active site3141 By similarity UniProtKB P00488
Active site3371 By similarity UniProtKB P00488
Metal binding3771Calcium By similarity UniProtKB P00488
Metal binding3791Calcium By similarity UniProtKB P00488
Metal binding4291Calcium By similarity UniProtKB P00488
Metal binding4341Calcium By similarity UniProtKB P00488

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1341D → G in BAC29013. Ref.2
Sequence conflict4041L → I in BAC29013. Ref.2
Sequence conflict4041L → I AA sequence Ref.4
Sequence conflict4261R → K in BAC29013. Ref.2
Sequence conflict4261R → K AA sequence Ref.4
Sequence conflict5281T → A in BAC29013. Ref.2
Sequence conflict5371K → E in BAC29013. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BZH1 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: AEAD1A23E3D97EC4

FASTA67075,591
        10         20         30         40         50         60 
MDSRNVLIIY AVNVERKLNA AAHHTSEYQT KKLVLRRGQI FTLKVILNRP LQPQDELKVT 

        70         80         90        100        110        120 
FTSGQRDPPY MVELDPVTSY RSKGWQVKIA KQSGVEVILN VISAADAVVG RYKMRVNEYK 

       130        140        150        160        170        180 
AGVFYLLFNP WCSDDSVFMA SEEERAEYIL NDTGYMYMGF AKQIKEKPWT FGQFEKHILS 

       190        200        210        220        230        240 
CCFNLLFQLE NNEMQNPVLV SRAICTMMCA ANGGVLMGNW TGDYADGTAP YVWTSSVPIL 

       250        260        270        280        290        300 
QQHYVTRMPV RYGQCWVFSG ILTTALRAVG IPARSVTNFE SAHDTEKNLT VDIYLDESGK 

       310        320        330        340        350        360 
TIPHLTKDSV WNFHVWTDAW MKRQDLPHGY DGWQVLDSTP QEISDGGFRT GPSPLTAIRQ 

       370        380        390        400        410        420 
GLIQMKYDTT FVFTEVNGDK FIWLVKQNQE REKNILIAVE TASLGKKIST KMVGENRRED 

       430        440        450        460        470        480 
ITLQYRFPEG SPEERKVMAK ASGKPSDDKL NSRTLNNSLQ ISVLQNSLEL GAPIYLTITL 

       490        500        510        520        530        540 
KRKTATPQNV NISCSLNLQT YTGNKKTNLG VIQKTVQIHG QESRVFLTMD ASYYIYKLGM 

       550        560        570        580        590        600 
VDDEMVIGGF IIAEIVDSGE RVATDTTLCF LYSAFSVEMP STGKVKQPLV ITSKFTNTLP 

       610        620        630        640        650        660 
IPLTNIKFSV ESLGLANMKS WEQETVPPGK TITFQMECTP VKAGPQKFIV KFISRQVKEV 

       670 
HAEKVVLISK 

« Hide

References

« Hide 'large scale' references
[1]"Physiologic self antigens rapidly capacitate autoimmune disease-specific polyclonal CD4+ CD25+ regulatory T cells."
Setiady Y.Y., Ohno K., Samy E.T., Bagavant H., Qiao H., Sharp C., She J.X., Tung K.S.K.
Blood 107:1056-1062(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Urinary bladder.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins."
Tseng H.-C., Lin H.-J., Sudhakar Gandhi P.S., Wang C.-Y., Chen Y.-H.
J. Chromatogr. B 876:198-202(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, TISSUE SPECIFICITY.
Tissue: Coagulating gland secretion.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF486627 mRNA. Translation: AAM45940.1.
AK035279 mRNA. Translation: BAC29013.1.
BC141297 mRNA. Translation: AAI41298.1.
BC145622 mRNA. Translation: AAI45623.1.
RefSeqNP_808579.2. NM_177911.4.
UniGeneMm.195309.

3D structure databases

ProteinModelPortalQ8BZH1.
SMRQ8BZH1. Positions 5-670.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000026893.

Proteomic databases

PRIDEQ8BZH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026893; ENSMUSP00000026893; ENSMUSG00000025787.
GeneID331046.
KEGGmmu:331046.
UCSCuc009sfo.1. mouse.

Organism-specific databases

CTD7047.
MGIMGI:3027002. Tgm4.

Phylogenomic databases

eggNOGNOG80379.
GeneTreeENSGT00740000115156.
HOGENOMHOG000231695.
InParanoidQ8BZH1.
KOK05621.
OrthoDBEOG7WT40M.
PhylomeDBQ8BZH1.
TreeFamTF324278.

Gene expression databases

BgeeQ8BZH1.
GenevestigatorQ8BZH1.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERPTHR11590. PTHR11590. 1 hit.
PfamPF00927. Transglut_C. 1 hit.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFPIRSF000459. TGM_EBP42. 1 hit.
SMARTSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTGM4. mouse.
NextBio399704.
PROQ8BZH1.
SOURCESearch...

Entry information

Entry nameTGM4_MOUSE
AccessionPrimary (citable) accession number: Q8BZH1
Secondary accession number(s): B7ZP44, Q8K460
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot