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Q99041 (TGM4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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):
Dorsal prostate transglutaminase
Dorsal protein 1
Short name=DP1
Transglutaminase-4
Short name=TGase-4
Gene names
Name:Tgm4
Synonyms:Dp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length667 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.3 Ref.6

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3. Ref.3 Ref.6 Ref.7

Cofactor

Binds 1 calcium ion per subunit. Ref.3

Subunit structure

Homodimer. Ref.5

Subcellular location

Secreted. Cell membrane; Lipid-anchorGPI-anchor Potential Ref.3 Ref.7.

Tissue specificity

Expressed in the coagulating gland, the dorsal part of the prostate and in semen (at protein level). Expressed at low levels in the lateral prostate and seminal vesicle. Not expressed in the epididymis, kidney, liver, serum, sperm plug, testes and ventral prostate. Ref.1 Ref.5

Induction

Androgen dependent, as shown by the decrease in the level of the protein following castration. Ref.1 Ref.5

Post-translational modification

The N-terminus is blocked.

Probably linked to the cell membrane via a lipid-anchor, possibly a GPI-anchor.

N-glycosylated on 2 Asn residues by a high mannose oligosaccharide consisting of five mannose residues and a fucosylated biantennary complex glycan. Ref.3 Ref.7

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 667667Protein-glutamine gamma-glutamyltransferase 4
PRO_0000213712

Sites

Active site2561 By similarity
Active site3151 By similarity
Active site3381 By similarity
Metal binding3781Calcium By similarity
Metal binding3801Calcium By similarity
Metal binding4301Calcium By similarity
Metal binding4351Calcium By similarity

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Ref.3
Glycosylation4721N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Ref.3

Experimental info

Sequence conflict1061D → N in AAA42287. Ref.1
Sequence conflict1281F → L in AAA42287. Ref.1
Sequence conflict1281F → L in AAA41092. Ref.4
Sequence conflict173 – 19624QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA42287. Ref.1
Sequence conflict173 – 19624QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA41092. Ref.4
Sequence conflict2801F → FGVLTTALRAVGIPARSVTN F in AAA41092. Ref.4
Sequence conflict2801F → FGVLTTALRAVGIPARSVTN F AA sequence Ref.4
Sequence conflict3161M → V in AAH66665. Ref.2
Sequence conflict3661I → F in AAA42287. Ref.1
Sequence conflict3661I → F in AAA41092. Ref.4
Sequence conflict394 – 4029KNVLIAVET → RRMSHRCGDC in AAA42287. Ref.1
Sequence conflict394 – 4029KNVLIAVET → RRMSHRCGDC in AAA41092. Ref.4
Sequence conflict6411G → GN in AAA42287. Ref.1
Sequence conflict6411G → GN in AAA41092. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q99041 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: FE9AED50E4677E59

FASTA66775,587
        10         20         30         40         50         60 
MDSRNMLVVY SVNLEKKLNA AAHHTIEYQT QKLVLRRGQI FSLKVMLNRP LQSHDELKLI 

        70         80         90        100        110        120 
FNTGHNMPFY TVELDPMTSY RSKGWQVKIA KQSGVEVVLN VISAADAVVG RYTMNVNEFD 

       130        140        150        160        170        180 
AGVFFLLFNP WCSDDSVFMA SEEDRAEYVL NDTGYMYMGF AKQIKEKPWT FGQFEKYILN 

       190        200        210        220        230        240 
CCFRLLTHLE PKEMQSPVLV SRAICTMMCA ANNFGVLVGN WTGDYSNGTA PYVWASSVPI 

       250        260        270        280        290        300 
LQQHYITRMP VRFGQCWVFS GVLTTALRAV GIPARSVTNF ESAHDTEKNL RVDIYLDESG 

       310        320        330        340        350        360 
KTIPHLTKDS VWNFHMWTDA WMKRQDLPQG HDGWQVLDST PQEISEGQFR IGPSPVSAIR 

       370        380        390        400        410        420 
QGLVQIMYDT TFVFTEVNGD KYIWLVKQNQ EREKNVLIAV ETASIGKNIS TKMVGENRRQ 

       430        440        450        460        470        480 
DITLHYKFPE GSPEERKAME KASGKRPDDK LNSRTLHISV LQNSVELGHP INLTIVLKRK 

       490        500        510        520        530        540 
TATPQNVNIS CSLDLQTYTG NKKTNLGVIQ KTVQIQGQES EVSLSMDSSF YIYKLGMVDD 

       550        560        570        580        590        600 
EMVIKGFIIA EIVDSGERVA TDTTLCFLYS AFSVEMPSTS KVNQPLTITC NFKNTLPIPL 

       610        620        630        640        650        660 
TNIKFSVESL GLNNMKSWEQ ETVPPGKTIN FQIECTPVKT GPRKFIVKFI SRQVKEVHAE 


KVVLITK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of rat prostate transglutaminase complementary DNA. The major androgen-regulated protein DP1 of rat dorsal prostate and coagulating gland."
Ho K.-C., Quarmby V.E., French F.S., Wilson E.M.
J. Biol. Chem. 267:12660-12667(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, INDUCTION BY ANDROGEN.
Strain: Sprague-Dawley.
Tissue: Prostate.
[2]"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].
[3]"Transglutaminase from rat coagulating gland secretion. Post-translational modifications and activation by phosphatidic acids."
Esposito C., Pucci P., Amoresano A., Marino G., Cozzolino A., Porta R.
J. Biol. Chem. 271:27416-27423(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 59-75; 276-288; 313-344 AND 503-511, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-408 AND ASN-488, GPI-ANCHOR.
[4]"Androgen regulated prostate genes: structural analysis and regulation."
Ho K.-C., Wilson E.M., French F.S.
Prog. Clin. Biol. Res. 239:125-153(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-667, PARTIAL PROTEIN SEQUENCE.
[5]"Biochemical homology between rat dorsal prostate and coagulating gland. Purification of a major androgen-induced protein."
Wilson E.M., French F.S.
J. Biol. Chem. 255:10946-10953(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBUNIT, INDUCTION BY ANDROGEN.
[6]"Transglutaminase-mediated modifications of the rat sperm surface in vitro."
Paonessa G., Metafora S., Tajana G., Abrescia P., De Santis A., Gentile V., Porta R.
Science 226:852-855(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[7]"Purification and molecular characterization of a secretory transglutaminase from coagulating gland of the rat."
Seitz J., Keppler C., Huentemann S., Rausch U., Aumueller G.
Biochim. Biophys. Acta 1078:139-146(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION, GPI-ANCHOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90310 mRNA. Translation: AAA42287.1.
BC066665 mRNA. Translation: AAH66665.1.
M32725 mRNA. Translation: AAA41092.1.
PIRA42803.
RefSeqNP_073204.2. NM_022713.2.
UniGeneRn.9964.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ99041.
PRIDEQ99041.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64679.
KEGGrno:64679.
UCSCRGD:620785. rat.

Organism-specific databases

CTD7047.
RGD620785. Tgm4.

Phylogenomic databases

eggNOGNOG80379.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidQ6NYB5.
KOK05621.
PhylomeDBQ99041.
TreeFamTF324278.

Gene expression databases

GenevestigatorQ99041.

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

NextBio613690.
PROQ99041.

Entry information

Entry nameTGM4_RAT
AccessionPrimary (citable) accession number: Q99041
Secondary accession number(s): Q6NYB5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 113 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