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Protein-glutamine gamma-glutamyltransferase 4 (EC 2.3.2.13) (Dorsal prostate transglutaminase) (Dorsal protein 1) (DP1) (Transglutaminase-4) (TGase-4)

 TGM4_RAT                Reviewed;         667 AA.
Q99041; Q6NYB5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 2.
20-JUN-2018, entry version 128.
RecName: Full=Protein-glutamine gamma-glutamyltransferase 4;
EC=2.3.2.13;
AltName: Full=Dorsal prostate transglutaminase;
AltName: Full=Dorsal protein 1;
Short=DP1;
AltName: Full=Transglutaminase-4;
Short=TGase-4;
Name=Tgm4; Synonyms=Dp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE
SPECIFICITY, AND INDUCTION BY ANDROGEN.
STRAIN=Sprague-Dawley; TISSUE=Prostate;
PubMed=1352290;
Ho K.-C., Quarmby V.E., French F.S., Wilson E.M.;
"Molecular cloning of rat prostate transglutaminase complementary DNA.
The major androgen-regulated protein DP1 of rat dorsal prostate and
coagulating gland.";
J. Biol. Chem. 267:12660-12667(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
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, AND GPI-ANCHOR.
PubMed=8910321; DOI=10.1074/jbc.271.44.27416;
Esposito C., Pucci P., Amoresano A., Marino G., Cozzolino A.,
Porta R.;
"Transglutaminase from rat coagulating gland secretion. Post-
translational modifications and activation by phosphatidic acids.";
J. Biol. Chem. 271:27416-27423(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 100-667, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3309953;
Ho K.-C., Wilson E.M., French F.S.;
"Androgen regulated prostate genes: structural analysis and
regulation.";
Prog. Clin. Biol. Res. 239:125-153(1987).
[5]
TISSUE SPECIFICITY, SUBUNIT, AND INDUCTION BY ANDROGEN.
PubMed=7191854;
Wilson E.M., French F.S.;
"Biochemical homology between rat dorsal prostate and coagulating
gland. Purification of a major androgen-induced protein.";
J. Biol. Chem. 255:10946-10953(1980).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=6149619; DOI=10.1126/science.6149619;
Paonessa G., Metafora S., Tajana G., Abrescia P., De Santis A.,
Gentile V., Porta R.;
"Transglutaminase-mediated modifications of the rat sperm surface in
vitro.";
Science 226:852-855(1984).
[7]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
GPI-ANCHOR.
PubMed=1676601;
Seitz J., Keppler C., Huentemann S., Rausch U., Aumueller G.;
"Purification and molecular characterization of a secretory
transglutaminase from coagulating gland of the rat.";
Biochim. Biophys. Acta 1078:139-146(1991).
-!- 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. {ECO:0000269|PubMed:6149619,
ECO:0000269|PubMed:8910321}.
-!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
{ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000269|PubMed:1676601,
ECO:0000269|PubMed:6149619, ECO:0000269|PubMed:8910321}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:8910321};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:8910321};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7191854}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1676601,
ECO:0000269|PubMed:8910321}. Cell membrane {ECO:0000305}; Lipid-
anchor, GPI-anchor {ECO:0000305}.
-!- 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. {ECO:0000269|PubMed:1352290,
ECO:0000269|PubMed:7191854}.
-!- INDUCTION: Androgen dependent, as shown by the decrease in the
level of the protein following castration.
{ECO:0000269|PubMed:1352290, ECO:0000269|PubMed:7191854}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Probably linked to the cell membrane via a lipid-anchor,
possibly a GPI-anchor.
-!- PTM: N-glycosylated on 2 Asn residues by a high mannose
oligosaccharide consisting of five mannose residues and a
fucosylated biantennary complex glycan.
{ECO:0000269|PubMed:1676601, ECO:0000269|PubMed:8910321}.
-!- SIMILARITY: Belongs to the transglutaminase superfamily.
Transglutaminase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M90310; AAA42287.1; -; mRNA.
EMBL; BC066665; AAH66665.1; -; mRNA.
EMBL; M32725; AAA41092.1; -; mRNA.
PIR; A42803; A42803.
RefSeq; NP_073204.2; NM_022713.2.
UniGene; Rn.9964; -.
SMR; Q99041; -.
STRING; 10116.ENSRNOP00000052677; -.
iPTMnet; Q99041; -.
PaxDb; Q99041; -.
PRIDE; Q99041; -.
GeneID; 64679; -.
KEGG; rno:64679; -.
UCSC; RGD:620785; rat.
CTD; 7047; -.
RGD; 620785; Tgm4.
eggNOG; ENOG410IFMV; Eukaryota.
eggNOG; ENOG410XQEZ; LUCA.
HOGENOM; HOG000231695; -.
HOVERGEN; HBG004342; -.
InParanoid; Q99041; -.
KO; K05621; -.
PhylomeDB; Q99041; -.
TreeFam; TF324278; -.
PRO; PR:Q99041; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0042628; P:mating plug formation; IEA:UniProtKB-KW.
GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.90.260.10; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR002931; Transglutaminase-like.
InterPro; IPR036985; Transglutaminase-like_sf.
InterPro; IPR023608; Transglutaminase_animal.
InterPro; IPR013808; Transglutaminase_AS.
InterPro; IPR008958; Transglutaminase_C.
InterPro; IPR036238; Transglutaminase_C_sf.
InterPro; IPR001102; Transglutaminase_N.
Pfam; PF00927; Transglut_C; 1.
Pfam; PF01841; Transglut_core; 1.
Pfam; PF00868; Transglut_N; 1.
PIRSF; PIRSF000459; TGM_EBP42; 1.
SMART; SM00460; TGc; 1.
SUPFAM; SSF49309; SSF49309; 2.
SUPFAM; SSF54001; SSF54001; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS00547; TRANSGLUTAMINASES; 1.
1: Evidence at protein level;
Acyltransferase; Calcium; Cell membrane; Complete proteome;
Copulatory plug; Direct protein sequencing; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Metal-binding; Reference proteome; Secreted;
Transferase.
CHAIN 1 667 Protein-glutamine gamma-
glutamyltransferase 4.
/FTId=PRO_0000213712.
ACT_SITE 256 256 {ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 315 315 {ECO:0000255|PROSITE-ProRule:PRU10024}.
ACT_SITE 338 338 {ECO:0000255|PROSITE-ProRule:PRU10024}.
METAL 378 378 Calcium. {ECO:0000250}.
METAL 380 380 Calcium. {ECO:0000250}.
METAL 430 430 Calcium. {ECO:0000250}.
METAL 435 435 Calcium. {ECO:0000250}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8910321}.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8910321}.
CONFLICT 106 106 D -> N (in Ref. 1; AAA42287).
{ECO:0000305}.
CONFLICT 128 128 F -> L (in Ref. 1; AAA42287 and 4;
AAA41092). {ECO:0000305}.
CONFLICT 173 196 QFEKYILNCCFRLLTHLEPKEMQS -> RLRSTLELLLPIV
DPFGAQGNAE (in Ref. 1; AAA42287 and 4;
AAA41092). {ECO:0000305}.
CONFLICT 280 280 F -> FGVLTTALRAVGIPARSVTNF (in Ref. 4;
AAA41092/AA sequence). {ECO:0000305}.
CONFLICT 316 316 M -> V (in Ref. 2; AAH66665).
{ECO:0000305}.
CONFLICT 366 366 I -> F (in Ref. 1; AAA42287 and 4;
AAA41092). {ECO:0000305}.
CONFLICT 394 402 KNVLIAVET -> RRMSHRCGDC (in Ref. 1;
AAA42287 and 4; AAA41092). {ECO:0000305}.
CONFLICT 641 641 G -> GN (in Ref. 1; AAA42287 and 4;
AAA41092). {ECO:0000305}.
SEQUENCE 667 AA; 75587 MW; FE9AED50E4677E59 CRC64;
MDSRNMLVVY SVNLEKKLNA AAHHTIEYQT QKLVLRRGQI FSLKVMLNRP LQSHDELKLI
FNTGHNMPFY TVELDPMTSY RSKGWQVKIA KQSGVEVVLN VISAADAVVG RYTMNVNEFD
AGVFFLLFNP WCSDDSVFMA SEEDRAEYVL NDTGYMYMGF AKQIKEKPWT FGQFEKYILN
CCFRLLTHLE PKEMQSPVLV SRAICTMMCA ANNFGVLVGN WTGDYSNGTA PYVWASSVPI
LQQHYITRMP VRFGQCWVFS GVLTTALRAV GIPARSVTNF ESAHDTEKNL RVDIYLDESG
KTIPHLTKDS VWNFHMWTDA WMKRQDLPQG HDGWQVLDST PQEISEGQFR IGPSPVSAIR
QGLVQIMYDT TFVFTEVNGD KYIWLVKQNQ EREKNVLIAV ETASIGKNIS TKMVGENRRQ
DITLHYKFPE GSPEERKAME KASGKRPDDK LNSRTLHISV LQNSVELGHP INLTIVLKRK
TATPQNVNIS CSLDLQTYTG NKKTNLGVIQ KTVQIQGQES EVSLSMDSSF YIYKLGMVDD
EMVIKGFIIA EIVDSGERVA TDTTLCFLYS AFSVEMPSTS KVNQPLTITC NFKNTLPIPL
TNIKFSVESL GLNNMKSWEQ ETVPPGKTIN FQIECTPVKT GPRKFIVKFI SRQVKEVHAE
KVVLITK


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