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Q99041

- TGM4_RAT

UniProt

Q99041 - TGM4_RAT

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Protein

Protein-glutamine gamma-glutamyltransferase 4

Gene
Tgm4, Dp1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.3 Publications

Cofactori

Binds 1 calcium ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei256 – 2561 By similarity
Active sitei315 – 3151 By similarity
Active sitei338 – 3381 By similarity
Metal bindingi378 – 3781Calcium By similarity
Metal bindingi380 – 3801Calcium By similarity
Metal bindingi430 – 4301Calcium By similarity
Metal bindingi435 – 4351Calcium By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. mating plug formation Source: UniProtKB-KW
  2. peptide cross-linking Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Tgm4
Synonyms:Dp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620785. Tgm4.

Subcellular locationi

Secreted. Cell membrane; Lipid-anchorGPI-anchor Reviewed prediction 2 Publications

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Copulatory plug, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 667667Protein-glutamine gamma-glutamyltransferase 4PRO_0000213712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi151 – 1511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi220 – 2201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi227 – 2271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi408 – 4081N-linked (GlcNAc...)1 Publication
Glycosylationi472 – 4721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi488 – 4881N-linked (GlcNAc...)1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ99041.
PRIDEiQ99041.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

Androgen dependent, as shown by the decrease in the level of the protein following castration.2 Publications

Gene expression databases

GenevestigatoriQ99041.

Interactioni

Subunit structurei

Homodimer.1 Publication

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG80379.
HOGENOMiHOG000231695.
HOVERGENiHBG004342.
InParanoidiQ6NYB5.
KOiK05621.
PhylomeDBiQ99041.
TreeFamiTF324278.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. 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]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 1 hit.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99041-1 [UniParc]FASTAAdd to Basket

« Hide

MDSRNMLVVY SVNLEKKLNA AAHHTIEYQT QKLVLRRGQI FSLKVMLNRP    50
LQSHDELKLI FNTGHNMPFY TVELDPMTSY RSKGWQVKIA KQSGVEVVLN 100
VISAADAVVG RYTMNVNEFD AGVFFLLFNP WCSDDSVFMA SEEDRAEYVL 150
NDTGYMYMGF AKQIKEKPWT FGQFEKYILN CCFRLLTHLE PKEMQSPVLV 200
SRAICTMMCA ANNFGVLVGN WTGDYSNGTA PYVWASSVPI LQQHYITRMP 250
VRFGQCWVFS GVLTTALRAV GIPARSVTNF ESAHDTEKNL RVDIYLDESG 300
KTIPHLTKDS VWNFHMWTDA WMKRQDLPQG HDGWQVLDST PQEISEGQFR 350
IGPSPVSAIR QGLVQIMYDT TFVFTEVNGD KYIWLVKQNQ EREKNVLIAV 400
ETASIGKNIS TKMVGENRRQ DITLHYKFPE GSPEERKAME KASGKRPDDK 450
LNSRTLHISV LQNSVELGHP INLTIVLKRK TATPQNVNIS CSLDLQTYTG 500
NKKTNLGVIQ KTVQIQGQES EVSLSMDSSF YIYKLGMVDD EMVIKGFIIA 550
EIVDSGERVA TDTTLCFLYS AFSVEMPSTS KVNQPLTITC NFKNTLPIPL 600
TNIKFSVESL GLNNMKSWEQ ETVPPGKTIN FQIECTPVKT GPRKFIVKFI 650
SRQVKEVHAE KVVLITK 667
Length:667
Mass (Da):75,587
Last modified:September 22, 2009 - v2
Checksum:iFE9AED50E4677E59
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061D → N in AAA42287. 1 Publication
Sequence conflicti128 – 1281F → L in AAA42287. 1 Publication
Sequence conflicti128 – 1281F → L in AAA41092. 1 Publication
Sequence conflicti173 – 19624QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA42287. 1 PublicationAdd
BLAST
Sequence conflicti173 – 19624QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA41092. 1 PublicationAdd
BLAST
Sequence conflicti280 – 2801F → FGVLTTALRAVGIPARSVTN F in AAA41092. 1 Publication
Sequence conflicti280 – 2801F → FGVLTTALRAVGIPARSVTN F AA sequence 1 Publication
Sequence conflicti316 – 3161M → V in AAH66665. 1 Publication
Sequence conflicti366 – 3661I → F in AAA42287. 1 Publication
Sequence conflicti366 – 3661I → F in AAA41092. 1 Publication
Sequence conflicti394 – 4029KNVLIAVET → RRMSHRCGDC in AAA42287. 1 Publication
Sequence conflicti394 – 4029KNVLIAVET → RRMSHRCGDC in AAA41092. 1 Publication
Sequence conflicti641 – 6411G → GN in AAA42287. 1 Publication
Sequence conflicti641 – 6411G → GN in AAA41092. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90310 mRNA. Translation: AAA42287.1.
BC066665 mRNA. Translation: AAH66665.1.
M32725 mRNA. Translation: AAA41092.1.
PIRiA42803.
RefSeqiNP_073204.2. NM_022713.2.
UniGeneiRn.9964.

Genome annotation databases

GeneIDi64679.
KEGGirno:64679.
UCSCiRGD:620785. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90310 mRNA. Translation: AAA42287.1 .
BC066665 mRNA. Translation: AAH66665.1 .
M32725 mRNA. Translation: AAA41092.1 .
PIRi A42803.
RefSeqi NP_073204.2. NM_022713.2.
UniGenei Rn.9964.

3D structure databases

ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q99041.
PRIDEi Q99041.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 64679.
KEGGi rno:64679.
UCSCi RGD:620785. rat.

Organism-specific databases

CTDi 7047.
RGDi 620785. Tgm4.

Phylogenomic databases

eggNOGi NOG80379.
HOGENOMi HOG000231695.
HOVERGENi HBG004342.
InParanoidi Q6NYB5.
KOi K05621.
PhylomeDBi Q99041.
TreeFami TF324278.

Miscellaneous databases

NextBioi 613690.
PROi Q99041.

Gene expression databases

Genevestigatori Q99041.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11590. PTHR11590. 1 hit.
Pfami PF00927. Transglut_C. 1 hit.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
SMARTi SM00460. TGc. 1 hit.
[Graphical view ]
SUPFAMi SSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTGM4_RAT
AccessioniPrimary (citable) accession number: Q99041
Secondary accession number(s): Q6NYB5
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi