Protein-glutamine gamma-glutamyltransferase 4

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Q99041 (TGM4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	667 AA.
Sequence status	Complete.
Protein existence	Evidence 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-anchor › GPI-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.

Ontologies

Keywords
Cellular component	Cell membrane Copulatory plug Membrane Secreted
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mating plug formation Inferred from electronic annotation. Source: UniProtKB-KW peptide cross-linking Inferred from electronic annotation. Source: InterPro
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 667

667

Protein-glutamine gamma-glutamyltransferase 4

PRO_0000213712

Sites

Active site

256

By similarity

Active site

315

By similarity

Active site

338

By similarity

Metal binding

378

Calcium By similarity

Metal binding

380

Calcium By similarity

Metal binding

430

Calcium By similarity

Metal binding

435

Calcium By similarity

Amino acid modifications

Glycosylation

151

N-linked (GlcNAc...) Potential

Glycosylation

220

N-linked (GlcNAc...) Potential

Glycosylation

227

N-linked (GlcNAc...) Potential

Glycosylation

408

N-linked (GlcNAc...) Ref.3

Glycosylation

472

N-linked (GlcNAc...) Potential

Glycosylation

488

N-linked (GlcNAc...) Ref.3

Experimental info

Sequence conflict

106

D → N in AAA42287. Ref.1

Sequence conflict

128

F → L in AAA42287. Ref.1

Sequence conflict

128

F → L in AAA41092. Ref.4

Sequence conflict

173 – 196

QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA42287. Ref.1

Sequence conflict

173 – 196

QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA41092. Ref.4

Sequence conflict

280

F → FGVLTTALRAVGIPARSVTN F in AAA41092. Ref.4

Sequence conflict

280

F → FGVLTTALRAVGIPARSVTN F AA sequence Ref.4

Sequence conflict

316

M → V in AAH66665. Ref.2

Sequence conflict

366

I → F in AAA42287. Ref.1

Sequence conflict

366

I → F in AAA41092. Ref.4

Sequence conflict

394 – 402

KNVLIAVET → RRMSHRCGDC in AAA42287. Ref.1

Sequence conflict

394 – 402

KNVLIAVET → RRMSHRCGDC in AAA41092. Ref.4

Sequence conflict

641

G → GN in AAA42287. Ref.1

Sequence conflict

641

G → GN in AAA41092. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q99041 [UniParc].

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

667

75,587

        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' referencesShow '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.
IPI	IPI00197575.
PIR	A42803.
RefSeq	NP_073204.2. NM_022713.2.
UniGene	Rn.9964.
3D structure databases
ModBase	Search...
Proteomic databases
PaxDb	Q99041.
PRIDE	Q99041.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	64679.
KEGG	rno:64679.
UCSC	RGD:620785. rat.
Organism-specific databases
CTD	7047.
RGD	620785. Tgm4.
Phylogenomic databases
eggNOG	NOG80379.
HOGENOM	HOG000231695.
HOVERGEN	HBG004342.
InParanoid	Q6NYB5.
KO	K05621.
Gene expression databases
ArrayExpress	Q99041.
Genevestigator	Q99041.
GermOnline	ENSRNOG00000004320. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.40.10. 3 hits.
InterPro	IPR023608. 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]
PANTHER	PTHR11590. PTHR11590. 1 hit.
Pfam	PF00927. Transglut_C. 1 hit. PF01841. Transglut_core. 1 hit. PF00868. Transglut_N. 1 hit. [Graphical view]
PIRSF	PIRSF000459. TGM_EBP42. 1 hit.
SMART	SM00460. TGc. 1 hit. [Graphical view]
SUPFAM	SSF81296. Ig_E-set. 1 hit. SSF49309. Transglut_C. 2 hits.
PROSITE	PS00547. TRANSGLUTAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	613690.

Entry information

Entry name

TGM4_RAT

Accession

Primary (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 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents