NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley;
TISSUE=Prostate;
PubMed=1352290 [NCBI, ExPASy, EBI, Israel, Japan]
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 [MRNA] OF 100-668, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3309953 [NCBI, ExPASy, EBI, Israel, Japan]
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).

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.
CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N⁵-alkylglutamine + NH₃.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed in the coagulating gland and in the dorsal part of the prostate.
INDUCTION: Androgen dependent, as shown by the decrease in the level of the protein following castration.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the transglutaminase superfamily. Transglutaminase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M90310; AAA42287.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32725; AAA41092.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A42803; A42803.

UniGene

Rn.9964

3D structure databases

HSSP

Q08188; 1L9M. [HSSP ENTRY / PDB]

ModBase

Q99041.

Organism-specific databases

RGD

620785; Tgm4.

Gene expression databases

ArrayExpress

Q99041; -.

GermOnline

ENSRNOG00000004320; Rattus norvegicus.

Family and domain databases

InterPro

IPR008957; Fibronectin_typ-III-like_fold.
IPR013783; Ig-like_fold.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.
IPR002931; Trnsglumase_like.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.30; FN_III-like; 1.
G3DSA:2.60.40.10; Ig-like_fold; 1.

Pfam

PF00927; Transglut_C; 1.
PF01841; Transglut_core; 1.
PF00868; Transglut_N; 1.
Pfam graphical view of domain structure.

SMART

SM00460; TGc; 1.
SMART graphical view of domain structure.

PROSITE

PS00547; TRANSGLUTAMINASES; 1.

BLOCKS

Q99041.

Genome annotation databases

Ensembl

ENSRNOG00000004320; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

Q99041; -.

Other

ProtoNet

Q99041.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Calcium; Copulatory plug; Direct protein sequencing; Metal-binding; Secreted; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 668`	`668`	`Protein-glutamine gamma-glutamyltransferase 4.`	`PRO_0000213712`
`ACT_SITE`	`255 255`		`By similarity.`
`ACT_SITE`	`314 314`		`By similarity.`
`ACT_SITE`	`337 337`		`By similarity.`
`METAL`	`377 377`		`Calcium (By similarity).`
`METAL`	`379 379`		`Calcium (By similarity).`
`METAL`	`430 430`		`Calcium (By similarity).`
`METAL`	`435 435`		`Calcium (By similarity).`
`CONFLICT`	`106 106`		`N -> D (in Ref. 2; AAA41092).`
`CONFLICT`	`279 279`		`F -> FGVLTTALRAVGIPARSVTNF (in Ref. 2; AA sequence).`

Sequence information

Length: 668 AA [This is the length of the unprocessed precursor]

Molecular weight: 75473 Da [This is the MW of the unprocessed precursor]

CRC64: 6196DFAC7B63B294 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDSRNMLVVY SVNLEKKLNA AAHHTIEYQT QKLVLRRGQI FSLKVMLNRP LQSHDELKLI 

        70         80         90        100        110        120 
FNTGHNMPFY TVELDPMTSY RSKGWQVKIA KQSGVEVVLN VISAANAVVG RYTMNVNEFD 

       130        140        150        160        170        180 
AGVFFLLLNP WCSDDSVFMA SEEDRAEYVL NDTGYMYMGF AKQIKEKPWT FGRLRSTLEL 

       190        200        210        220        230        240 
LLPIVDPFGA QGNAEPVLVS RAICTMMCAA NNFGVLVGNW TGDYSNGTAP YVWASSVPIL 

       250        260        270        280        290        300 
QQHYITRMPV RFGQCWVFSG VLTTALRAVG IPARSVTNFE SAHDTEKNLR VDIYLDESGK 

       310        320        330        340        350        360 
TIPHLTKDSV WNFHMWTDAW MKRQDLPQGH DGWQVLDSTP QEISEGQFRI GPSPVSAIRQ 

       370        380        390        400        410        420 
GLVQFMYDTT FVFTEVNGDK YIWLVKQNQE RERRMSHRCG DCASIGKNIS 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 GNPRKFIVKF ISRQVKEVHA 


EKVVLITK

Q99041 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools