TGM4_RAT
ID TGM4_RAT Reviewed; 667 AA.
AC Q99041; Q6NYB5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 4;
DE EC=2.3.2.13;
DE AltName: Full=Dorsal prostate transglutaminase;
DE AltName: Full=Dorsal protein 1;
DE Short=DP1;
DE AltName: Full=Transglutaminase-4;
DE Short=TGase-4;
GN Name=Tgm4; Synonyms=Dp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP AND INDUCTION BY ANDROGEN.
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=1352290; DOI=10.1016/s0021-9258(18)42328-9;
RA Ho K.-C., Quarmby V.E., French F.S., Wilson E.M.;
RT "Molecular cloning of rat prostate transglutaminase complementary DNA. The
RT major androgen-regulated protein DP1 of rat dorsal prostate and coagulating
RT gland.";
RL J. Biol. Chem. 267:12660-12667(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 59-75; 276-288; 313-344 AND 503-511, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP ASN-408 AND ASN-488, AND GPI-ANCHOR.
RX PubMed=8910321; DOI=10.1074/jbc.271.44.27416;
RA Esposito C., Pucci P., Amoresano A., Marino G., Cozzolino A., Porta R.;
RT "Transglutaminase from rat coagulating gland secretion. Post-translational
RT modifications and activation by phosphatidic acids.";
RL J. Biol. Chem. 271:27416-27423(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-667, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3309953;
RA Ho K.-C., Wilson E.M., French F.S.;
RT "Androgen regulated prostate genes: structural analysis and regulation.";
RL Prog. Clin. Biol. Res. 239:125-153(1987).
RN [5]
RP TISSUE SPECIFICITY, SUBUNIT, AND INDUCTION BY ANDROGEN.
RX PubMed=7191854; DOI=10.1016/s0021-9258(19)70398-6;
RA Wilson E.M., French F.S.;
RT "Biochemical homology between rat dorsal prostate and coagulating gland.
RT Purification of a major androgen-induced protein.";
RL J. Biol. Chem. 255:10946-10953(1980).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6149619; DOI=10.1126/science.6149619;
RA Paonessa G., Metafora S., Tajana G., Abrescia P., De Santis A., Gentile V.,
RA Porta R.;
RT "Transglutaminase-mediated modifications of the rat sperm surface in
RT vitro.";
RL Science 226:852-855(1984).
RN [7]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION, AND GPI-ANCHOR.
RX PubMed=1676601; DOI=10.1016/0167-4838(91)99002-a;
RA Seitz J., Keppler C., Huentemann S., Rausch U., Aumueller G.;
RT "Purification and molecular characterization of a secretory
RT transglutaminase from coagulating gland of the rat.";
RL Biochim. Biophys. Acta 1078:139-146(1991).
CC -!- FUNCTION: Associated with the mammalian reproductive process. Plays an
CC important role in the formation of the seminal coagulum through the
CC cross-linking of specific proteins present in the seminal plasma.
CC Transglutaminase is also required to stabilize the copulatory plug.
CC {ECO:0000269|PubMed:6149619, ECO:0000269|PubMed:8910321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10024, ECO:0000269|PubMed:1676601,
CC ECO:0000269|PubMed:6149619, ECO:0000269|PubMed:8910321};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8910321};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:8910321};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7191854}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1676601,
CC ECO:0000269|PubMed:8910321}. Cell membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the coagulating gland, the dorsal part
CC of the prostate and in semen (at protein level). Expressed at low
CC levels in the lateral prostate and seminal vesicle. Not expressed in
CC the epididymis, kidney, liver, serum, sperm plug, testes and ventral
CC prostate. {ECO:0000269|PubMed:1352290, ECO:0000269|PubMed:7191854}.
CC -!- INDUCTION: Androgen dependent, as shown by the decrease in the level of
CC the protein following castration. {ECO:0000269|PubMed:1352290,
CC ECO:0000269|PubMed:7191854}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Probably linked to the cell membrane via a lipid-anchor, possibly
CC a GPI-anchor.
CC -!- PTM: N-glycosylated on 2 Asn residues by a high mannose oligosaccharide
CC consisting of five mannose residues and a fucosylated biantennary
CC complex glycan. {ECO:0000269|PubMed:1676601,
CC ECO:0000269|PubMed:8910321}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; M90310; AAA42287.1; -; mRNA.
DR EMBL; BC066665; AAH66665.1; -; mRNA.
DR EMBL; M32725; AAA41092.1; -; mRNA.
DR PIR; A42803; A42803.
DR RefSeq; NP_073204.2; NM_022713.2.
DR AlphaFoldDB; Q99041; -.
DR SMR; Q99041; -.
DR STRING; 10116.ENSRNOP00000052677; -.
DR GlyGen; Q99041; 6 sites.
DR iPTMnet; Q99041; -.
DR PaxDb; Q99041; -.
DR PRIDE; Q99041; -.
DR GeneID; 64679; -.
DR KEGG; rno:64679; -.
DR UCSC; RGD:620785; rat.
DR CTD; 7047; -.
DR RGD; 620785; Tgm4.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR InParanoid; Q99041; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; Q99041; -.
DR TreeFam; TF324278; -.
DR PRO; PR:Q99041; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
DR GO; GO:0042628; P:mating plug formation; ISO:RGD.
DR GO; GO:0018149; P:peptide cross-linking; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR013808; Transglutaminase_AS.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR Pfam; PF00927; Transglut_C; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Calcium; Cell membrane; Copulatory plug;
KW Direct protein sequencing; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Secreted; Transferase.
FT CHAIN 1..667
FT /note="Protein-glutamine gamma-glutamyltransferase 4"
FT /id="PRO_0000213712"
FT REGION 430..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8910321"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8910321"
FT CONFLICT 106
FT /note="D -> N (in Ref. 1; AAA42287)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="F -> L (in Ref. 1; AAA42287 and 4; AAA41092)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..196
FT /note="QFEKYILNCCFRLLTHLEPKEMQS -> RLRSTLELLLPIVDPFGAQGNAE
FT (in Ref. 1; AAA42287 and 4; AAA41092)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="F -> FGVLTTALRAVGIPARSVTNF (in Ref. 4; AAA41092/AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="M -> V (in Ref. 2; AAH66665)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="I -> F (in Ref. 1; AAA42287 and 4; AAA41092)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..402
FT /note="KNVLIAVET -> RRMSHRCGDC (in Ref. 1; AAA42287 and 4;
FT AAA41092)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="G -> GN (in Ref. 1; AAA42287 and 4; AAA41092)"
FT /evidence="ECO:0000305"
SQ 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
