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Q99041

- TGM4_RAT

UniProt

Q99041 - TGM4_RAT

Protein

Protein-glutamine gamma-glutamyltransferase 4

Gene

Tgm4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (22 Sep 2009)
      Previous versions | rss
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    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 PublicationsPROSITE-ProRule annotation

    Cofactori

    Binds 1 calcium ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei256 – 2561PROSITE-ProRule annotation
    Active sitei315 – 3151PROSITE-ProRule annotation
    Active sitei338 – 3381PROSITE-ProRule annotation
    Metal bindingi378 – 3781CalciumBy similarity
    Metal bindingi380 – 3801CalciumBy similarity
    Metal bindingi430 – 4301CalciumBy similarity
    Metal bindingi435 – 4351CalciumBy 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

    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 2 Publications. Cell membrane Curated; Lipid-anchorGPI-anchor Curated

    GO - Cellular componenti

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

    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...)Sequence Analysis
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi408 – 4081N-linked (GlcNAc...)2 Publications
    Glycosylationi472 – 4721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi488 – 4881N-linked (GlcNAc...)2 Publications

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061D → N in AAA42287. (PubMed:1352290)Curated
    Sequence conflicti128 – 1281F → L in AAA42287. (PubMed:1352290)Curated
    Sequence conflicti128 – 1281F → L in AAA41092. (PubMed:3309953)Curated
    Sequence conflicti173 – 19624QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA42287. (PubMed:1352290)CuratedAdd
    BLAST
    Sequence conflicti173 – 19624QFEKY…KEMQS → RLRSTLELLLPIVDPFGAQG NAE in AAA41092. (PubMed:3309953)CuratedAdd
    BLAST
    Sequence conflicti280 – 2801F → FGVLTTALRAVGIPARSVTN F in AAA41092. (PubMed:3309953)Curated
    Sequence conflicti280 – 2801F → FGVLTTALRAVGIPARSVTN F AA sequence (PubMed:3309953)Curated
    Sequence conflicti316 – 3161M → V in AAH66665. (PubMed:15489334)Curated
    Sequence conflicti366 – 3661I → F in AAA42287. (PubMed:1352290)Curated
    Sequence conflicti366 – 3661I → F in AAA41092. (PubMed:3309953)Curated
    Sequence conflicti394 – 4029KNVLIAVET → RRMSHRCGDC in AAA42287. (PubMed:1352290)Curated
    Sequence conflicti394 – 4029KNVLIAVET → RRMSHRCGDC in AAA41092. (PubMed:3309953)Curated
    Sequence conflicti641 – 6411G → GN in AAA42287. (PubMed:1352290)Curated
    Sequence conflicti641 – 6411G → GN in AAA41092. (PubMed:3309953)Curated

    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

    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: October 1, 2014
    This is version 114 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